NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6573322|pdb|1B16|A]
View 

Chain A, PROTEIN (ALCOHOL DEHYDROGENASE)

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143139)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to alcohol dehydrogenase that catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-245 4.35e-94

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


:

Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 276.49  E-value: 4.35e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTALAELKAINPKVNITFHTYDVTVPVAESKkLLKKIFDQLKTV 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAA-AFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       86 DILINGAGILDDH----------QIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPVYSASK 155
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      156 AAVVSFTNSLAKLAP-ITGVTAYSINPGITRTPLVHTFNSWLdveprvAELLLSHPTQTSEQCGQNFVKAIEAN-KNGAI 233
Cdd:cd05323 159 HGVVGFTRSLADLLEyKTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDeKNGAI 232

                       250
                ....*....|..
1B16_A      234 WKLDLGTLEAIE 245
Cdd:cd05323 233 WIVDGGKLIEIE 244
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-245 4.35e-94

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 276.49  E-value: 4.35e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTALAELKAINPKVNITFHTYDVTVPVAESKkLLKKIFDQLKTV 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAA-AFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       86 DILINGAGILDDH----------QIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPVYSASK 155
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      156 AAVVSFTNSLAKLAP-ITGVTAYSINPGITRTPLVHTFNSWLdveprvAELLLSHPTQTSEQCGQNFVKAIEAN-KNGAI 233
Cdd:cd05323 159 HGVVGFTRSLADLLEyKTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDeKNGAI 232

                       250
                ....*....|..
1B16_A      234 WKLDLGTLEAIE 245
Cdd:cd05323 233 WIVDGGKLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-197 4.56e-51

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 165.09  E-value: 4.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A          6 KNVIFVAALGGIGLDTSRELVKRNLKNFVIlDRVENP--TALAELKAINPKvnITFHTYDVTVPvAESKKLLKKIFDQLK 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLV-DRSEEKleAVAKELGALGGK--ALFIQGDVTDR-AQVKALVEQAVERLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         84 TVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSASK 155
Cdd:pfam00106  77 RLDILVNNAGItglgpfseLSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGG---RIVNISSVAGLVPYPGGSAYSASK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1B16_A        156 AAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFNSWLD 197
Cdd:pfam00106 154 AAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-229 6.33e-40

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 138.46  E-value: 6.33e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        1 MDLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKA--INPKVNITFHTYDVTVPvAESKKLLKKI 78
Cdd:COG0300   1 MSLTGKTVLITGASSGIGRALARALAARG-ARVVLVAR--DAERLEALAAelRAAGARVEVVALDVTDP-DAVAALAEAV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       79 FDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPV 150
Cdd:COG0300  77 LARFGPIDVLVNNAGVggggpfeeLDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRG---RIVNVSSVAGLRGLPGMAA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      151 YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHTfnswldveprvAELLLSHPTQTSEQCGQNFVKAIEANK 229
Cdd:COG0300 154 YAASKAALEGFSESLRAeLAP-TGVRVTAVCPGPVDTPFTAR-----------AGAPAGRPLLSPEEVARAILRALERGR 221
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-193 3.64e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 99.50  E-value: 3.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKAINPKVNITFHTYDVTVPVAES-KKLLKKIF 79
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGAN--VVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESvERAVDEAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDfwDKRKGGPGGIIaNICSVTGF-NAIHQVPv 150
Cdd:PRK05557  79 AEFGGVDILVNNAGITRDNLLmrmkeedwDRVIDTNLTGVFNLTKAVAR--PMMKQRSGRII-NISSVVGLmGNPGQAN- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
1B16_A       151 YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHTFN 193
Cdd:PRK05557 155 YAASKAGVIGFTKSLAReLAS-RGITVNAVAPGFIETDMTDALP 197
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-97 3.61e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 40.16  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A          13 ALGGIGLDTSRELVKRNLKNFVILDRVENPTA-----LAELKAINPKVniTFHTYDVTVPVAeSKKLLKKIFDQLKTVDI 87
Cdd:smart00822   8 GLGGLGRALARWLAERGARRLVLLSRSGPDAPgaaalLAELEAAGARV--TVVACDVADRDA-LAAVLAAIPAVEGPLTG 84

                           90
                   ....*....|
1B16_A          88 LINGAGILDD 97
Cdd:smart00822  85 VIHAAGVLDD 94
 
Name Accession Description Interval E-value
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 6-245 4.35e-94

insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains insect type ADH, and 15-hydroxyprostaglandin dehydrogenase (15-PGDH) type I; these proteins are classical SDRs. ADH catalyzes the NAD+-dependent oxidation of alcohols to aldehydes/ketones. This subgroup is distinct from the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase/reductase family, and evolved in fruit flies to allow the digestion of fermenting fruit. 15-PGDH catalyzes the NAD-dependent interconversion of (5Z,13E)-(15S)-11alpha,15-dihydroxy-9-oxoprost-13-enoate and (5Z,13E)-11alpha-hydroxy-9,15-dioxoprost-13-enoate, and has a typical SDR glycine-rich NAD-binding motif, which is not fully present in ADH. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 276.49  E-value: 4.35e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTALAELKAINPKVNITFHTYDVTVPVAESKkLLKKIFDQLKTV 85
Cdd:cd05323   1 KVAIITGGASGIGLATAKLLLKKG-AKVAILDRNENPGAAAELQAINPKVKATFVQCDVTSWEQLAA-AFKKAIEKFGRV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       86 DILINGAGILDDH----------QIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPVYSASK 155
Cdd:cd05323  79 DILINNAGILDEKsylfagklppPWEKTIDVNLTGVINTTYLALHYMDKNKGGKGGVIVNIGSVAGLYPAPQFPVYSASK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      156 AAVVSFTNSLAKLAP-ITGVTAYSINPGITRTPLVHTFNSWLdveprvAELLLSHPTQTSEQCGQNFVKAIEAN-KNGAI 233
Cdd:cd05323 159 HGVVGFTRSLADLLEyKTGVRVNAICPGFTNTPLLPDLVAKE------AEMLPSAPTQSPEVVAKAIVYLIEDDeKNGAI 232

                       250
                ....*....|..
1B16_A      234 WKLDLGTLEAIE 245
Cdd:cd05323 233 WIVDGGKLIEIE 244
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 6-197 4.56e-51

short chain dehydrogenase; This family contains a wide variety of dehydrogenases.


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 165.09  E-value: 4.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A          6 KNVIFVAALGGIGLDTSRELVKRNLKNFVIlDRVENP--TALAELKAINPKvnITFHTYDVTVPvAESKKLLKKIFDQLK 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLV-DRSEEKleAVAKELGALGGK--ALFIQGDVTDR-AQVKALVEQAVERLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         84 TVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSASK 155
Cdd:pfam00106  77 RLDILVNNAGItglgpfseLSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGG---RIVNISSVAGLVPYPGGSAYSASK 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
1B16_A        156 AAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFNSWLD 197
Cdd:pfam00106 154 AAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMTKELREDEG 195
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 8-237 3.54e-40

classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 138.57  E-value: 3.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        8 VIFVAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKAIN-PKVNITFHTYDVTVPvAESKKLLKKIFDQLKTVD 86
Cdd:cd05233   1 ALVTGASSGIGRAIARRLAREG-AKVVLADR--NEEALAELAAIEaLGGNAVAVQADVSDE-EDVEALVEEALEEFGRLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       87 ILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSASKAAV 158
Cdd:cd05233  77 ILVNNAGIarpgpleeLTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGG---RIVNISSVAGLRPLPGQAAYAASKAAL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      159 VSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFNSWlDVEPRVAELLLSHPTQTSEQCGQNFVKAIEANK---NGAIWK 235
Cdd:cd05233 154 EGLTRSLALELAPYGIRVNAVAPGLVDTPMLAKLGPE-EAEKELAAAIPLGRLGTPEEVAEAVVFLASDEAsyiTGQVIP 232


                ..
1B16_A      236 LD 237
Cdd:cd05233 233 VD 234
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-229 6.33e-40

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 138.46  E-value: 6.33e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        1 MDLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKA--INPKVNITFHTYDVTVPvAESKKLLKKI 78
Cdd:COG0300   1 MSLTGKTVLITGASSGIGRALARALAARG-ARVVLVAR--DAERLEALAAelRAAGARVEVVALDVTDP-DAVAALAEAV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       79 FDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPV 150
Cdd:COG0300  77 LARFGPIDVLVNNAGVggggpfeeLDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRG---RIVNVSSVAGLRGLPGMAA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      151 YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHTfnswldveprvAELLLSHPTQTSEQCGQNFVKAIEANK 229
Cdd:COG0300 154 YAASKAALEGFSESLRAeLAP-TGVRVTAVCPGPVDTPFTAR-----------AGAPAGRPLLSPEEVARAILRALERGR 221
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 2-210 1.57e-32

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 119.12  E-value: 1.57e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        2 DLTNKNVIFVAALGGIGLDTSRELVKR--NLknfVILDRVENP--TALAELKAINPKVniTFHTYDVTVPvAESKKLLKK 77
Cdd:COG1028   3 RLKGKVALVTGGSSGIGRAIARALAAEgaRV---VITDRDAEAleAAAAELRAAGGRA--LAVAADVTDE-AAVEALVAA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       78 IFDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVP 149
Cdd:COG1028  77 AVAAFGRLDILVNNAGItppgpleeLTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGG---RIVNISSIAGLRGSPGQA 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1B16_A      150 VYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHtfnSWLDVEPRVAELLLSHP 210
Cdd:COG1028 154 AYAASKAAVVGLTRSLALeLAP-RGIRVNAVAPGPIDTPMTR---ALLGAEEVREALAARIP 211
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
 1-191 5.24e-31

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 114.89  E-value: 5.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVIL-DRveNPTALAELKA-INPkvNITFHTYDVTVPvAESKKLLKKI 78
Cdd:COG4221   1 MSDKGKVALITGASSGIGAATARALAAAGAR--VVLaAR--RAERLEALAAeLGG--RALAVPLDVTDE-AAVEAAVAAA 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       79 FDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPV 150
Cdd:COG4221  74 VAEFGRLDVLVNNAGVallgpleeLDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSG---HIVNISSIAGLRPYPGGAV 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1B16_A      151 YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHT 191
Cdd:COG4221 151 YAATKAAVRGLSESLRAeLRP-TGIRVTVIEPGAVDTEFLDS 191
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
 1-193 3.64e-25

3-ketoacyl-(acyl-carrier-protein) reductase; Validated


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 99.50  E-value: 3.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKAINPKVNITFHTYDVTVPVAES-KKLLKKIF 79
Cdd:PRK05557   1 MSLEGKVALVTGASRGIGRAIAERLAAQGAN--VVINYASSEAGAEALVAEIGALGGKALAVQGDVSDAESvERAVDEAK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDfwDKRKGGPGGIIaNICSVTGF-NAIHQVPv 150
Cdd:PRK05557  79 AEFGGVDILVNNAGITRDNLLmrmkeedwDRVIDTNLTGVFNLTKAVAR--PMMKQRSGRII-NISSVVGLmGNPGQAN- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
1B16_A       151 YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHTFN 193
Cdd:PRK05557 155 YAASKAGVIGFTKSLAReLAS-RGITVNAVAPGFIETDMTDALP 197
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
 13-229 1.50e-24

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 97.70  E-value: 1.50e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       13 ALGGIGLDTSRELVKRNLKnFVILDRveNPTALAELKAINPKVNITFHTY--DVTVPvAESKKLLKKIFDQLKTVDILIN 90
Cdd:cd05339   7 GGSGIGRLLALEFAKRGAK-VVILDI--NEKGAEETANNVRKAGGKVHYYkcDVSKR-EEVYEAAKKIKKEVGDVTILIN 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       91 GAGI--------LDDHQIERTIAINFTGLVNTTTAIL-DFWDKRKGGpggiIANICSVTGFNAIHQVPVYSASKAAVVSF 161
Cdd:cd05339  83 NAGVvsgkklleLPDEEIEKTFEVNTLAHFWTTKAFLpDMLERNHGH----IVTIASVAGLISPAGLADYCASKAAAVGF 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1B16_A      162 TNSLA---KLAPITGVTAYSINPGITRTPLVHtfnswlDVEPRVAELLlshPTQTSEQCGQNFVKAIEANK 229
Cdd:cd05339 159 HESLRlelKAYGKPGIKTTLVCPYFINTGMFQ------GVKTPRPLLA---PILEPEYVAEKIVRAILTNQ 220
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
5-189 2.04e-23

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 94.83  E-value: 2.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         5 NKNVIFVAALGGIGLDTSRELVKRNLKnfVIL-DRVENPTALA-ELKAINPKVNITFHTYDVTvPVAESKKLLKKIFDQL 82
Cdd:PRK12824   2 KKIALVTGAKRGIGSAIARELLNDGYR--VIAtYFSGNDCAKDwFEEYGFTEDQVRLKELDVT-DTEECAEALAEIEEEE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        83 KTVDILINGAGILDDHQIERT--------IAINFTGLVNTTTAILDfwDKRKGGPGGIIaNICSVTGFNAIHQVPVYSAS 154
Cdd:PRK12824  79 GPVDILVNNAGITRDSVFKRMshqewndvINTNLNSVFNVTQPLFA--AMCEQGYGRII-NISSVNGLKGQFGQTNYSAA 155

                        170       180       190
                 ....*....|....*....|....*....|....*
1B16_A       155 KAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK12824 156 KAGMIGFTKALASEGARYGITVNCIAPGYIATPMV 190
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-187 7.73e-23

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 93.39  E-value: 7.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKAINP--KVNITFHTYDVTVPvAESKKLLKKI 78
Cdd:PRK12825   2 GSLMGRVALVTGAARGLGRAIALRLARAGAD--VVVHYRSDEEAAEELVEAVEalGRRAQAVQADVTDK-AALEAAVAAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDfwDKRKGGPGGIIaNICSVTGFNA-IHQVP 149
Cdd:PRK12825  79 VERFGRIDILVNNAGIfedkpladMSDDEWDEVIDVNLSGVFHLLRAVVP--PMRKQRGGRIV-NISSVAGLPGwPGRSN 155

                        170       180       190
                 ....*....|....*....|....*....|....*....
1B16_A       150 vYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTP 187
Cdd:PRK12825 156 -YAAAKAGLVGLTKALAReLAE-YGITVNMVAPGDIDTD 192
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
 1-229 1.93e-22

classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka Tyrosine-dependent oxidoreductases) are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 91.98  E-value: 1.93e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        1 MDLTNKNVIFVAALGGIGLDTSRELVKRNlkNFVIL-DRveNPTALAELKAINPKVnitfHTYDVTVPVAES-KKLLKKI 78
Cdd:cd05370   1 MKLTGNTVLITGGTSGIGLALARKFLEAG--NTVIItGR--REERLAEAKKELPNI----HTIVLDVGDAESvEALAEAL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       79 FDQLKTVDILINGAGILDDHQI----------ERTIAINFTGLVNTTTAILDFWDKRkggPGGIIANICSVTGFNAIHQV 148
Cdd:cd05370  73 LSEYPNLDILINNAGIQRPIDLrdpasdldkaDTEIDTNLIGPIRLIKAFLPHLKKQ---PEATIVNVSSGLAFVPMAAN 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      149 PVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLvhtfnswldVEPRVAELLLSHPTQTSEQCGQNFVKAIEAN 228
Cdd:cd05370 150 PVYCATKAALHSYTLALRHQLKDTGVEVVEIVPPAVDTEL---------HEERRNPDGGTPRKMPLDEFVDEVVAGLERG 220


                .
1B16_A      229 K 229
Cdd:cd05370 221 R 221
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-193 2.23e-22

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 92.21  E-value: 2.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTA--LAELKAINpkVNITFHTYDVTVPvAESKKLLKKI 78
Cdd:PRK05565   1 MKLMGKVAIVTGASGGIGRAIAELLAKEGAKVVIAYDINEEAAQelLEEIKEEG--GDAIAVKADVSSE-EDVENLVEQI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFN-AIHQVP 149
Cdd:PRK05565  78 VEKFGKIDILVNNAGIsnfglvtdMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSG---VIVNISSIWGLIgASCEVL 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
1B16_A       150 vYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHTFN 193
Cdd:PRK05565 155 -YSASKGAVNAFTKALAKeLAP-SGIRVNAVAPGAIDTEMWSSFS 197
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
 1-165 3.80e-22

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 91.38  E-value: 3.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        1 MDLTNKNVIFVAALGGIGLDTSRELVKRNlkNFVIL-DRveNPTALAELKAINPkvNITFHTYDVTVPvAESKKLLKKIF 79
Cdd:COG3967   1 MKLTGNTILITGGTSGIGLALAKRLHARG--NTVIItGR--REEKLEEAAAANP--GLHTIVLDVADP-ASIAALAEQVT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       80 DQLKTVDILINGAGIL----------DDHQIERTIAINFTGLVNTTTAILDFWDKRkggPGGIIANICSVTGFNAIHQVP 149
Cdd:COG3967  74 AEFPDLNVLINNAGIMraedlldeaeDLADAEREITTNLLGPIRLTAAFLPHLKAQ---PEAAIVNVSSGLAFVPLAVTP 150

                       170
                ....*....|....*.
1B16_A      150 VYSASKAAVVSFTNSL 165
Cdd:COG3967 151 TYSATKAALHSYTQSL 166
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
 6-230 5.38e-22

3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These proteins include members identified as KDSR, ribitol type dehydrogenase, and others. The group shows strong conservation of the active site tetrad and glycine rich NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 91.16  E-value: 5.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNLKNFVI---LDRVENPTALAELKAINPKVNITFHTYDVTVPVaESKKLLKKIFDQL 82
Cdd:cd08939   2 KHVLITGGSSGIGKALAKELVKEGANVIIVarsESKLEEAVEEIEAEANASGQKVSYISADLSDYE-EVEQAFAQAVEKG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       83 KTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSAS 154
Cdd:cd08939  81 GPPDLVVNCAGIsipglfedLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPG---HIVFVSSQAALVGIYGYSAYCPS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      155 KAAVVSFTNSLA---KLAPITGVTAYsinPGITRTPLVHTFNSwldVEPRVAELL-LSHPTQTSEQCGQNFVKAIEANKN 230
Cdd:cd08939 158 KFALRGLAESLRqelKPYNIRVSVVY---PPDTDTPGFEEENK---TKPEETKAIeGSSGPITPEEAARIIVKGLDRGYD 231
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
1-187 6.44e-22

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 90.99  E-value: 6.44e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVeNPTALAELKAINPK--VNITFHTYDVTVPvAESKKLLKKI 78
Cdd:PRK05653   1 MSLQGKTALVTGASRGIGRAIALRLAADGAK--VVIYDS-NEEAAEALAAELRAagGEARVLVFDVSDE-AAVRALIEAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGILDDHQIE--------RTIAINFTGLVNTT-TAILDFWDKRKGGpggiIANICSVTGFNA-IHQV 148
Cdd:PRK05653  77 VEAFGALDILVNNAGITRDALLPrmseedwdRVIDVNLTGTFNVVrAALPPMIKARYGR----IVNISSVSGVTGnPGQT 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
1B16_A       149 PvYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTP 187
Cdd:PRK05653 153 N-YSAAKAGVIGFTKALALeLAS-RGITVNAVAPGFIDTD 190
PRK12829 PRK12829
short chain dehydrogenase; Provisional
 2-187 4.09e-21

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 89.35  E-value: 4.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQ 81
Cdd:PRK12829   8 PLDGLRVLVTGGASGIGRAIAEAFAEAG-ARVHVCDV--SEAALAATAARLPGAKVTATVADVADP-AQVERVFDTAVER 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        82 LKTVDILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIANICSVTGFNAIHQVPVYS 152
Cdd:PRK12829  84 FGGLDVLVNNAGIagptggideITPEQWEQTLAVNLNGQFYFARAAVPLL--KASGHGGVIIALSSVAGRLGYPGRTPYA 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
1B16_A       153 ASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTP 187
Cdd:PRK12829 162 ASKWAVVGLVKSLAIeLGP-LGIRVNAILPGIVRGP 196
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
 7-229 2.05e-20

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 86.90  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        7 NVIFV-AALGGIGLDTSRELVKRnlknfviLDRV----ENPTALAELKAINPkVNITFHTYDVTVPvAESKKLLKKIFDQ 81
Cdd:cd05374   1 KVVLItGCSSGIGLALALALAAQ-------GYRViataRNPDKLESLGELLN-DNLEVLELDVTDE-ESIKAAVKEVIER 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       82 LKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSA 153
Cdd:cd05374  72 FGRIDVLVNNAGYglfgpleeTSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSG---RIVNVSSVAGLVPTPFLGPYCA 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      154 SKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLVHTFNSWLDVEPRVAE------------LLLSHPTQTSEQCGQN 220
Cdd:cd05374 149 SKAALEALSESLRLeLAP-FGIKVTIIEPGPVRTGFADNAAGSALEDPEISPyaperkeikenaAGVGSNPGDPEKVADV 227


                ....*....
1B16_A      221 FVKAIEANK 229
Cdd:cd05374 228 IVKALTSES 236
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 8.79e-20

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 85.01  E-value: 8.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVI-LDrvenptalaelKAINPKVNITFHTY--DVTVPvaeskklLKK 77
Cdd:PRK06550   1 QEFMTKTVLITGAASGIGLAQARAFLAQGAQ--VYgVD-----------KQDKPDLSGNFHFLqlDLSDD-------LEP 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        78 IFDQLKTVDILINGAGILDDHQ---------IERTIAINFTGLVNTTTAILDFWDKRKggpGGIIANICSVTGFNAIHQV 148
Cdd:PRK06550  61 LFDWVPSVDILCNTAGILDDYKplldtsleeWQHIFDTNLTSTFLLTRAYLPQMLERK---SGIIINMCSIASFVAGGGG 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
1B16_A       149 PVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06550 138 AAYTASKHALAGFTKQLALDYAKDGIQVFGIAPGAVKTPM 177
FabG-like PRK07231
SDR family oxidoreductase;
1-192 1.46e-19

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 84.50  E-value: 1.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAEL-KAINPKVNITFHTYDVTVPvAESKKLLKKIF 79
Cdd:PRK07231   1 MRLEGKVAIVTGASSGIGEGIARRFAAEG-ARVVVTDR--NEEAAERVaAEILAGGRAIAVAADVSDE-ADVEAAVAAAL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGfnaIHQVP- 149
Cdd:PRK07231  77 ERFGSVDILVNNAGTthrngplldVDEAEFDRIFAVNVKSPYLWTQAAVPAMRGEGGG---AIVNVASTAG---LRPRPg 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
1B16_A       150 --VYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHTF 192
Cdd:PRK07231 151 lgWYNASKGAVITLTKALAaELGP-DKIRVNAVAPVVVETGLLEAF 195
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 16-186 1.68e-19

Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 83.83  E-value: 1.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       16 GIGLDTSRELVKRNlKNFVIL-----DRVEnpTALAELKaiNPKVNITFHTYDVTVPvaES-KKLLKKIFDQLKTVDILI 89
Cdd:cd05324  11 GIGFEIVRQLAKSG-PGTVILtardvERGQ--AAVEKLR--AEGLSVRFHQLDVTDD--ASiEAAADFVEEKYGGLDILV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       90 NGAGILDDH---------QIERTIAINFTGLVNTTTAILDfwdKRKGGPGGIIANICSVTGfnaiHQVPVYSASKAAVVS 160
Cdd:cd05324  84 NNAGIAFKGfddstptreQARETMKTNFFGTVDVTQALLP---LLKKSPAGRIVNVSSGLG----SLTSAYGVSKAALNA 156

                       170       180
                ....*....|....*....|....*.
1B16_A      161 FTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:cd05324 157 LTRILAKELKETGIKVNACCPGWVKT 182
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 2-188 4.42e-19

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 83.66  E-value: 4.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDR----VENptALAELKAINPKVniTFHTYDVtVPVAESKKLLKK 77
Cdd:cd08935   2 SLKNKVAVITGGTGVLGGAMARALAQAGAK-VAALGRnqekGDK--VAKEITALGGRA--IALAADV-LDRASLERAREE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       78 IFDQLKTVDILINGAGI----------------------LDDHQIERTIAINFTGlvnTTTAILDFWDKRKGGPGGIIAN 135
Cdd:cd08935  76 IVAQFGTVDILINGAGGnhpdattdpehyepeteqnffdLDEEGWEFVFDLNLNG---SFLPSQVFGKDMLEQKGGSIIN 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
1B16_A      136 ICSVTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:cd08935 153 ISSMNAFSPLTKVPAYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTPQ 205
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
 5-239 7.42e-19

d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, catalyzes the interconversion of D-3-hydroxybutyrate and acetoacetate. It is a classical SDR, with the canonical NAD-binding motif and active site tetrad. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 82.88  E-value: 7.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        5 NKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPT---ALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQ 81
Cdd:cd08940   2 GKVALVTGSTSGIGLGIARALAAAGAN--IVLNGFGDAAeieAVRAGLAAKHGVKVLYHGADLSKP-AAIEDMVAYAQRQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       82 LKTVDILINGAGILDDHQIE--------RTIAINFTGLVNTTTAILDFWDKRkgGPGGIIaNICSVTGFNAIHQVPVYSA 153
Cdd:cd08940  79 FGGVDILVNNAGIQHVAPIEdfptekwdAIIALNLSAVFHTTRLALPHMKKQ--GWGRII-NIASVHGLVASANKSAYVA 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      154 SKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVH------TFNSWLDVEPRVAELLLS-HPTQ---TSEQCGQNFV- 222
Cdd:cd08940 156 AKHGVVGLTKVVALETAGTGVTCNAICPGWVLTPLVEkqisalAQKNGVPQEQAARELLLEkQPSKqfvTPEQLGDTAVf 235

                       250
                ....*....|....*....
1B16_A      223 KAIEANK--NGAIWKLDLG 239
Cdd:cd08940 236 LASDAASqiTGTAVSVDGG 254
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
 13-189 2.56e-18

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 81.05  E-value: 2.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       13 ALGGIGLDTSRELVKRNLKnFVILDRVENPTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQLKTVDILINGA 92
Cdd:cd05333   8 ASRGIGRAIALRLAAEGAK-VAVTDRSEEAAAETVEEIKALGGNAAALEADVSDR-EAVEALVEKVEAEFGPVDILVNNA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       93 GI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGF-NAIHQVPvYSASKAAVVSFTN 163
Cdd:cd05333  86 GItrdnllmrMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGR---IINISSVVGLiGNPGQAN-YAASKAGVIGFTK 161

                       170       180
                ....*....|....*....|....*..
1B16_A      164 SLAK-LAPiTGVTAYSINPGITRTPLV 189
Cdd:cd05333 162 SLAKeLAS-RGITVNAVAPGFIDTDMT 187
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
 2-192 4.59e-18

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 80.50  E-value: 4.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKNFV--ILDRVENPTAlAELKAinpkvNITFHTYDVTVPvAESKKLLKKIF 79
Cdd:cd05341   2 RLKGKVAIVTGGARGLGLAHARLLVAEGAKVVLsdILDEEGQAAA-AELGD-----AARFFHLDVTDE-DGWTAVVDTAR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       80 DQLKTVDILINGAGILDDHQIE--------RTIAINFTGLVNTTTAILDfwDKRKGGPGGIIaNICSVTGFNAIHQVPVY 151
Cdd:cd05341  75 EAFGRLDVLVNNAGILTGGTVEtttleewrRLLDINLTGVFLGTRAVIP--PMKEAGGGSII-NMSSIEGLVGDPALAAY 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
1B16_A      152 SASKAAVVSFTNSLA-KLAPIT-GVTAYSINPGITRTPLVHTF 192
Cdd:cd05341 152 NASKGAVRGLTKSAAlECATQGyGIRVNSVHPGYIYTPMTDEL 194
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 2-196 5.75e-18

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 80.48  E-value: 5.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        2 DLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQ 81
Cdd:cd05347   2 SLKGKVALVTGASRGIGFGIASGLAEAG-ANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDE-EAIKAAVEAIEED 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       82 LKTVDILINGAGILDDHQIER--------TIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPVYSA 153
Cdd:cd05347  80 FGKIDILVNNAGIIRRHPAEEfpeaewrdVIDVNLNGVFFVSQAVARHMIKQGHGK---IINICSLLSELGGPPVPAYAA 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1B16_A      154 SKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV------HTFNSWL 196
Cdd:cd05347 157 SKGGVAGLTKALATEWARHGIQVNAIAPGYFATEMTeavvadPEFNDDI 205
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
 16-188 1.22e-17

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 79.64  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       16 GIGLDTSRELVKRNLKnFVILDRVENPtALAELKAINpkvNITFHTYDVTvPVAESKKLLKKIFDQLKTVDILINGAGI- 94
Cdd:cd05371  13 GLGLATVERLLAQGAK-VVILDLPNSP-GETVAKLGD---NCRFVPVDVT-SEKDVKAALALAKAKFGRLDIVVNCAGIa 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       95 ---------------LDDHQieRTIAINFTGLVNTTTAILDFWDKRK---GGPGGIIANICSVTGFNAIHQVPVYSASKA 156
Cdd:cd05371  87 vaaktynkkgqqphsLELFQ--RVINVNLIGTFNVIRLAAGAMGKNEpdqGGERGVIINTASVAAFEGQIGQAAYSASKG 164

                       170       180       190
                ....*....|....*....|....*....|...
1B16_A      157 AVVSFTNSLAK-LAPItGVTAYSINPGITRTPL 188
Cdd:cd05371 165 GIVGMTLPIARdLAPQ-GIRVVTIAPGLFDTPL 196
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 6-229 1.45e-17

retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) OxidoReductase (LPOR) and related proteins, classical (c) SDRs; Classical SDR subgroup containing retinol-DHs, LPORs, and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Pchlide reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14, dehydrogenase/reductase SDR family member (DHRS)-12 , -13 and -X (a DHRS on chromosome X), and WWOX (WW domain-containing oxidoreductase), as well as a Neurospora crassa SDR encoded by the blue light inducible bli-4 gene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 79.58  E-value: 1.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNLKnFVILDRVENP--TALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQLK 83
Cdd:cd05327   2 KVVVITGANSGIGKETARELAKRGAH-VIIACRNEEKgeEAAAEIKKETGNAKVEVIQLDLSSL-ASVRQFAEEFLARFP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       84 TVDILINGAGI------LDDHQIERTIAINFTGLVNTTTAILDfwDKRKGGPGGIIaNICSVT--------------GFN 143
Cdd:cd05327  80 RLDILINNAGImapprrLTKDGFELQFAVNYLGHFLLTNLLLP--VLKASAPSRIV-NVSSIAhragpidfndldleNNK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      144 AIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTfNSWLDVEPRVAELLLshpTQTSEQCGQNFVK 223
Cdd:cd05327 157 EYSPYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTELLRR-NGSFFLLYKLLRPFL---KKSPEQGAQTALY 232


                ....*.
1B16_A      224 AIEANK 229
Cdd:cd05327 233 AATSPE 238
PRK07825 PRK07825
short chain dehydrogenase; Provisional
 1-189 1.57e-17

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 79.60  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVI--LDRVENPTALAELKainpkvNITFHTYDVTVPvAESKKLLKKI 78
Cdd:PRK07825   1 DDLRGKVVAITGGARGIGLATARALAALGAR-VAIgdLDEALAKETAAELG------LVVGGPLDVTDP-ASFAAFLDAV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDfwDKRKGGPGGIIaNICSVTGFNAIHQVPV 150
Cdd:PRK07825  73 EADLGPIDVLVNNAGVMpvgpfldePDAVTRRILDVNVYGVILGSKLAAP--RMVPRGRGHVV-NVASLAGKIPVPGMAT 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
1B16_A       151 YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLV 189
Cdd:PRK07825 150 YCASKHAVVGFTDAARLeLRG-TGVHVSVVLPSFVNTELI 188
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 1-213 2.36e-17

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 78.68  E-value: 2.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRVENPT--ALAELKAINPKVNitfhTYDVTVPVAeSKKLLKKI 78
Cdd:PRK12828   3 HSLQGKVVAITGGFGGLGRATAAWLAARGAR-VALIGRGAAPLsqTLPGVPADALRIG----GIDLVDPQA-ARRAVDEV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKrkgGPGGIIANICSVTGFNAIHQVPV 150
Cdd:PRK12828  77 NRQFGRLDALVNIAGAfvwgtiadGDADTWDRMYGVNVKTTLNASKAALPALTA---SGGGRIVNIGAGAALKAGPGMGA 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1B16_A       151 YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHT------FNSWLDVE--PRVAELLLSHPTQT 213
Cdd:PRK12828 154 YAAAKAGVARLTEALAAELLDRGITVNAVLPSIIDTPPNRAdmpdadFSRWVTPEqiAAVIAFLLSDEAQA 224
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
 5-206 8.01e-17

meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases (BDHs) catalyze the NAD+ dependent conversion of 2,3-butanediol to acetonin; BDHs are classified into types according to their stereospecificity as to substrates and products. Included in this subgroup are Klebsiella pneumonia meso-BDH which catalyzes meso-2,3-butanediol to D(-)-acetonin, and Corynebacterium glutamicum L-BDH which catalyzes lX+)-2,3-butanediol to L(+)-acetonin. This subgroup is comprised of classical SDRs with the characteristic catalytic triad and NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 77.42  E-value: 8.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        5 NKNVIFVAALGGIGLDTSRELVKRNLkNFVILDRVENPTALAELKAINPK-VNITFHTYDVTVPvAESKKLLKKIFDQLK 83
Cdd:cd05366   2 SKVAIITGAAQGIGRAIAERLAADGF-NIVLADLNLEEAAKSTIQEISEAgYNAVAVGADVTDK-DDVEALIDQAVEKFG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       84 TVDILINGAGI-----LDD---HQIERTIAINFTGLVNTTTAILDFWDKRKGGpgGIIANICSVTGFNAIHQVPVYSASK 155
Cdd:cd05366  80 SFDVMVNNAGIapitpLLTiteEDLKKVYAVNVFGVLFGIQAAARQFKKLGHG--GKIINASSIAGVQGFPNLGAYSASK 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
1B16_A      156 AAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLvhtfnsWLDVEPRVAELL 206
Cdd:cd05366 158 FAVRGLTQTAAQeLAP-KGITVNAYAPGIVKTEM------WDYIDEEVGEIA 202
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
 6-186 8.68e-17

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 76.94  E-value: 8.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNLKnfVIL--DRVENPTALA-ELKAINPKVNITFhTYDVTVPvAESKKLLKKIFDQL 82
Cdd:cd05346   1 KTVLITGASSGIGEATARRFAKAGAK--LILtgRRAERLQELAdELGAKFPVKVLPL-QLDVSDR-ESIEAALENLPEEF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       83 KTVDILINGAGI-----------LDDhqIERTIAINFTGLVNTTTAILDFWDKRKggpGGIIANICSVTGFNAIHQVPVY 151
Cdd:cd05346  77 RDIDILVNNAGLalgldpaqeadLED--WETMIDTNVKGLLNVTRLILPIMIARN---QGHIINLGSIAGRYPYAGGNVY 151

                       170       180       190
                ....*....|....*....|....*....|....*
1B16_A      152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:cd05346 152 CATKAAVRQFSLNLRKDLIGTGIRVTNIEPGLVET 186
PRK12826 PRK12826
SDR family oxidoreductase;
2-187 9.30e-17

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 76.88  E-value: 9.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVI-LDRVENPTALAELKAINPKVnitfHTY--DVTVPvAESKKLLKKI 78
Cdd:PRK12826   3 DLEGRVALVTGAARGIGRAIAVRLAADGAEVIVVdICGDDAAATAELVEAAGGKA----RARqvDVRDR-AALKAAVAAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDfWDKRKGGpgGIIANICSVTGF-----NAI 145
Cdd:PRK12826  78 VEDFGRLDILVANAGIfpltpfaeMDDEQWERVIDVNLTGTFLLTQAALP-ALIRAGG--GRIVLTSSVAGPrvgypGLA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
1B16_A       146 HqvpvYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTP 187
Cdd:PRK12826 155 H----YAASKAGLVGFTRALALeLAA-RNITVNSVHPGGVDTP 192
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 8-212 1.57e-16

2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 dihydrozybenzoate dehydrogenase shares the characteristics of the classical SDRs. This subgroup includes Escherichai coli EntA which catalyzes the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoate to 2,3-dihydroxybenzoate during biosynthesis of the siderophore Enterobactin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 76.35  E-value: 1.57e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        8 VIFVAALGGIGLDTSRELVKRNLK------NFVILDRVENPTALAELkainpkvnitfhtyDVTVPvAESKKLLKKIFDQ 81
Cdd:cd05331   1 VIVTGAAQGIGRAVARHLLQAGATvialdlPFVLLLEYGDPLRLTPL--------------DVADA-AAVREVCSRLLAE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       82 LKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILD-FWDKRkggpGGIIANICSvtgfNAIHQ----V 148
Cdd:cd05331  66 HGPIDALVNCAGVLrpgatdplSTEDWEQTFAVNVTGVFNLLQAVAPhMKDRR----TGAIVTVAS----NAAHVprisM 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1B16_A      149 PVYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHTfnSWLDvEPRVAELLLSHPTQ 212
Cdd:cd05331 138 AAYGASKAALASLSKCLGlELAP-YGVRCNVVSPGSTDTAMQRT--LWHD-EDGAAQVIAGVPEQ 198
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
 3-189 1.85e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 76.46  E-value: 1.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVkRNLKNFVILDRVENPTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQL 82
Cdd:PRK12429   2 LKGKVALVTGAASGIGLEIALALA-KEGAKVVIADLNDEAAAAAAEALQKAGGKAIGVAMDVTDE-EAINAGIDYAVETF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        83 KTVDILINGAGI-----LDDHQIER---TIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSAS 154
Cdd:PRK12429  80 GGVDILVNNAGIqhvapIEDFPTEKwkkMIAIMLDGAFLTTKAALPIMKAQGGG---RIINMASVHGLVGSAGKAAYVSA 156

                        170       180       190
                 ....*....|....*....|....*....|....*
1B16_A       155 KAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK12429 157 KHGLIGLTKVVALEGATHGVTVNAICPGYVDTPLV 191
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
 8-229 3.05e-16

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 75.44  E-value: 3.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        8 VIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTAL-AELKAINPKVNItfHTYDVTVPvAESKKLLKKIFDQLKTVD 86
Cdd:cd05350   1 VLITGASSGIGRALAREFAKAGYNVALAARRTDRLDELkAELLNPNPSVEV--EILDVTDE-ERNQLVIAELEAELGGLD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       87 ILINGAGI-----LDDHQIE---RTIAINFTGLVNTTTAILD-FWDKRKGGpggiIANICSVTGFNAIHQVPVYSASKAA 157
Cdd:cd05350  78 LVIINAGVgkgtsLGDLSFKafrETIDTNLLGAAAILEAALPqFRAKGRGH----LVLISSVAALRGLPGAAAYSASKAA 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1B16_A      158 VVSFTNSL-AKLAPiTGVTAYSINPGITRTPLvhTFNSwldveprvaellLSHPTQTS-EQCGQNFVKAIEANK 229
Cdd:cd05350 154 LSSLAESLrYDVKK-RGIRVTVINPGFIDTPL--TANM------------FTMPFLMSvEQAAKRIYKAIKKGA 212
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 1-188 4.33e-16

2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 75.31  E-value: 4.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVI-LDRVENPTAlaelkainpkvNITFHTYDVTVPVAES-KKLLKKI 78
Cdd:PRK08220   4 MDFSGKTVWVTGAAQGIGYAVALAFVEAGAK--VIgFDQAFLTQE-----------DYPFATFVLDVSDAAAvAQVCQRL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggiiaNICSVtGFNAIHqVP- 149
Cdd:PRK08220  71 LAETGPLDVLVNAAGILrmgatdslSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSG------AIVTV-GSNAAH-VPr 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
1B16_A       150 ----VYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPL 188
Cdd:PRK08220 143 igmaAYGASKAALTSLAKCVGlELAP-YGVRCNVVSPGSTDTDM 185
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
 2-189 5.98e-16

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 74.93  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPT--ALAELKAINPKVniTFHTYDVTVPvAESKKLLKKIF 79
Cdd:PRK13394   4 NLNGKTAVVTGAASGIGKEIALELARAG-AAVAIADLNQDGAnaVADEINKAGGKA--IGVAMDVTNE-DAVNAGIDKVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGILDDHQIE--------RTIAINFTGLVNTTTAILDFWDKRKGGpgGIIANICSVTGFNAIHQVPVY 151
Cdd:PRK13394  80 ERFGSVDILVSNAGIQIVNPIEnysfadwkKMQAIHVDGAFLTTKAALKHMYKDDRG--GVVIYMGSVHSHEASPLKSAY 157

                        170       180       190
                 ....*....|....*....|....*....|....*...
1B16_A       152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK13394 158 VTAKHGLLGLARVLAKEGAKHNVRSHVVCPGFVRTPLV 195
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
 4-188 6.49e-16

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 74.88  E-value: 6.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        4 TNKNVIFVA-ALGGIGLDTSRELVKRNLKNFVILDRVEN-PTALAELKAINPKVNITfhTYDVTVPvAESKKLLKKIFDQ 81
Cdd:cd08945   1 QDSEVALVTgATSGIGLAIARRLGKEGLRVFVCARGEEGlATTVKELREAGVEADGR--TCDVRSV-PEIEALVAAAVAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       82 LKTVDILINGAG--------ILDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIaNICSVTGFNA-IHQVPvYS 152
Cdd:cd08945  78 YGPIDVLVNNAGrsgggataELADELWLDVVETNLTGVFRVTKEVLKAGGMLERGTGRII-NIASTGGKQGvVHAAP-YS 155

                       170       180       190
                ....*....|....*....|....*....|....*..
1B16_A      153 ASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPL 188
Cdd:cd08945 156 ASKHGVVGFTKALGlELAR-TGITVNAVCPGFVETPM 191
PRK07201 PRK07201
SDR family oxidoreductase;
3-225 1.47e-15

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 75.76  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVEnptALAELKA-INPKvNITFHTY--DVTVPvAESKKLLKKIF 79
Cdd:PRK07201 369 LVGKVVLITGASSGIGRATAIKVAEAGATVFLVARNGE---ALDELVAeIRAK-GGTAHAYtcDLTDS-AAVDHTVKDIL 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAG------ILDD----HQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVtG-------F 142
Cdd:PRK07201 444 AEHGHVDYLVNNAGrsirrsVENStdrfHDYERTMAVNYFGAVRLILGLLPHMRERRFGH---VVNVSSI-GvqtnaprF 519

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       143 NAihqvpvYSASKAAVVSFTNSLAKLAPITGVTAYSINpgitrTPLVHTfnswldvePRVA--ELLLSHPTQTSEQCGQN 220
Cdd:PRK07201 520 SA------YVASKAALDAFSDVAASETLSDGITFTTIH-----MPLVRT--------PMIAptKRYNNVPTISPEEAADM 580


                 ....*
1B16_A       221 FVKAI 225
Cdd:PRK07201 581 VVRAI 585
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-184 3.14e-15

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 72.80  E-value: 3.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLkNFVILDRVE---NPTAlAELKAInpKVNITFHTYDVTVpVAESKKLLKK 77
Cdd:PRK07666   3 QSLQGKNALITGAGRGIGRAVAIALAKEGV-NVGLLARTEenlKAVA-EEVEAY--GVKVVIATADVSD-YEEVTAAIEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        78 IFDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVP 149
Cdd:PRK07666  78 LKNELGSIDILINNAGIskfgkfleLDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGD---IINISSTAGQKGAAVTS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
1B16_A       150 VYSASKAAVVSFTNSLAK-----------LAPITGVTAYSINPGIT 184
Cdd:PRK07666 155 AYSASKFGVLGLTESLMQevrkhnirvtaLTPSTVATDMAVDLGLT 200
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
 2-188 3.46e-15

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 72.75  E-value: 3.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRveNPTALAELKAINPKVNITFHTYDVTVPVAES-KKLLKKIFD 80
Cdd:cd05352   5 SLKGKVAIVTGGSRGIGLAIARALAEAGADVAIIYNS--APRAEEKAEELAKKYGVKTKAYKCDVSSQESvEKTFKQIQK 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       81 QLKTVDILINGAGI------LDD--HQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIAnICSVTGFNA---IHQVP 149
Cdd:cd05352  83 DFGKIDILIANAGItvhkpaLDYtyEQWNKVIDVNLNGVFNCAQAAAKIF--KKQGKGSLII-TASMSGTIVnrpQPQAA 159

                       170       180       190
                ....*....|....*....|....*....|....*....
1B16_A      150 vYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:cd05352 160 -YNASKAAVIHLAKSLAVEWAKYFIRVNSISPGYIDTDL 197
PRK08267 PRK08267
SDR family oxidoreductase;
6-189 3.47e-15

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 72.66  E-value: 3.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         6 KNVIFVAALGGIGLDTSRELVKRNLknFV-ILDRveNPTALAELKAINPKVNITFHTYDVTVPVAESKKLlkKIFDQL-- 82
Cdd:PRK08267   2 KSIFITGAASGIGRATALLFAAEGW--RVgAYDI--NEAGLAALAAELGAGNAWTGALDVTDRAAWDAAL--ADFAAAtg 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        83 KTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWdkrKGGPGGIIANICSVTGFNAIHQVPVYSAS 154
Cdd:PRK08267  76 GRLDVLFNNAGILrggpfediPLEAHDRVIDINVKGVLNGAHAALPYL---KATPGARVINTSSASAIYGQPGLAVYSAT 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
1B16_A       155 KAAVVSFTNSL----AKLapitGVTAYSINPGITRTPLV 189
Cdd:PRK08267 153 KFAVRGLTEALdlewRRH----GIRVADVMPLFVDTAML 187
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 16-206 6.67e-15

carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl reductase of the classical SDR family. Studies in Drosophila melanogaster implicate Sniffer in the prevention of neurodegeneration due to aging and oxidative-stress. This subgroup also includes Rhodococcus sp. AD45 IsoH, which is an NAD-dependent 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase involved in isoprene metabolism, Aspergillus nidulans StcE encoded by a gene which is part of a proposed sterigmatocystin biosynthesis gene cluster, Bacillus circulans SANK 72073 BtrF encoded by a gene found in the butirosin biosynthesis gene cluster, and Aspergillus parasiticus nor-1 involved in the biosynthesis of aflatoxins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 71.56  E-value: 6.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       16 GIGLDTSRELVKRnlKNFVILDRVENPTALAELKAINPK-VNITFHTYDVTVPVAESKKLLKKIFDQLKtVDILINGAGI 94
Cdd:cd05325   9 GIGLELVRQLLAR--GNNTVIATCRDPSAATELAALGAShSRLHILELDVTDEIAESAEAVAERLGDAG-LDVLINNAGI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       95 L---------DDHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGgIIANICSVTG---FNAIHQVPVYSASKAAVVSFT 162
Cdd:cd05325  86 LhsygpasevDSEDLLEVFQVNVLGPLLLTQAFLPLL--LKGARA-KIINISSRVGsigDNTSGGWYSYRASKAALNMLT 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
1B16_A      163 NSLAKLAPITGVTAYSINPGITRTPL---VHTFNSWLDVEPRVAELL 206
Cdd:cd05325 163 KSLAVELKRDGITVVSLHPGWVRTDMggpFAKNKGPITPEESVAGLL 209
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 11-189 1.24e-14

Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) reductases.


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 70.92  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         11 VAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQLKTVDILIN 90
Cdd:pfam13561   2 AANESGIGWAIARALAEEG-AEVVLTDL--NEALAKRVEELAEELGAAVLPCDVTDE-EQVEALVAAAVEKFGRLDILVN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         91 GAGILDDHQI----------ERTIAINFTGLVNTTTAILdfwdkRKGGPGGIIANICSVTGFNAIHQVPVYSASKAAVVS 160
Cdd:pfam13561  78 NAGFAPKLKGpfldtsredfDRALDVNLYSLFLLAKAAL-----PLMKEGGSIVNLSSIGAERVVPNYNAYGAAKAALEA 152

                         170       180       190
                  ....*....|....*....|....*....|
1B16_A        161 FTNSLAK-LAPiTGVTAYSINPGITRTPLV 189
Cdd:pfam13561 153 LTRYLAVeLGP-RGIRVNAISPGPIKTLAA 181
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
 5-187 1.58e-14

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 70.77  E-value: 1.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        5 NKNVIFVAALGGIGLDTSRELVK---------RNLKNfviLDRvenptALAELKAINPKVNITfhTYDVTVPvAESKKLL 75
Cdd:cd05344   1 GKVALVTAASSGIGLAIARALARegarvaicaRNREN---LER-----AASELRAGGAGVLAV--VADLTDP-EDIDRLV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       76 KKIFDQLKTVDILINGAG--------ILDDHQIERTIAINFTGLVNTTTAILDFWDKRKggpGGIIANICSVTGFNAIHQ 147
Cdd:cd05344  70 EKAGDAFGRVDILVNNAGgpppgpfaELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERG---WGRIVNISSLTVKEPEPN 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
1B16_A      148 VPVYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTP 187
Cdd:cd05344 147 LVLSNVARAGLIGLVKTLSReLAP-DGVTVNSVLPGYIDTE 186
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
 3-188 1.58e-14

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 70.64  E-value: 1.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALA-ELKAINPKVNITfhTYDVTvPVAESKKLLKKIFDQ 81
Cdd:cd08934   1 LQGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDRLEALAdELEAEGGKALVL--ELDVT-DEQQVDAAVERTVEA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       82 LKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPVYSA 153
Cdd:cd08934  78 LGRLDILVNNAGIMllgpvedaDTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGT---IVNISSVAGRVAVRNSAVYNA 154

                       170       180       190
                ....*....|....*....|....*....|....*
1B16_A      154 SKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:cd08934 155 TKFGVNAFSEGLRQEVTERGVRVVVIEPGTVDTEL 189
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
 3-190 2.07e-14

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 70.13  E-value: 2.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKNfvILDRVENPTALAELKAINPKvNITFHTYDVTVPvaESkklLKKIFDQL 82
Cdd:cd05354   1 IKDKTVLVTGANRGIGKAFVESLLAHGAKK--VYAAVRDPGSAAHLVAKYGD-KVVPLRLDVTDP--ES---IKAAAAQA 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       83 KTVDILINGAGIL---------DDHQIERTIAINFTGLVNTTTAildFWDKRKGGPGGIIANICSVTGFNAIHQVPVYSA 153
Cdd:cd05354  73 KDVDVVINNAGVLkpatlleegALEALKQEMDVNVFGLLRLAQA---FAPVLKANGGGAIVNLNSVASLKNFPAMGTYSA 149

                       170       180       190
                ....*....|....*....|....*....|....*...
1B16_A      154 SKAAVVSFTNSL-AKLAPiTGVTAYSINPGITRTPLVH 190
Cdd:cd05354 150 SKSAAYSLTQGLrAELAA-QGTLVLSVHPGPIDTRMAA 186
PRK07060 PRK07060
short chain dehydrogenase; Provisional
 1-210 3.69e-14

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 69.74  E-value: 3.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKAinpKVNITFHTYDVTVPVAeskklLKKIFD 80
Cdd:PRK07060   5 FDFSGKSVLVTGASSGIGRACAVALAQRG-ARVVAAAR--NAAALDRLAG---ETGCEPLRLDVGDDAA-----IRAALA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGILD--------DHQIERTIAINFTGLVNTTTAildFWDKR-KGGPGGIIANICSVTGFNAIHQVPVY 151
Cdd:PRK07060  74 AAGAFDGLVNCAGIASlesaldmtAEGFDRVMAVNARGAALVARH---VARAMiAAGRGGSIVNVSSQAALVGLPDHLAY 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       152 SASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPLvHTFnSWLDVEPRvAELLLSHP 210
Cdd:PRK07060 151 CASKAALDAITRVLCVeLGP-HGIRVNSVNPTVTLTPM-AAE-AWSDPQKS-GPMLAAIP 206
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
 13-186 5.78e-14

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 69.17  E-value: 5.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       13 ALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELKAINPKVNITFHTYDVTVpvaeSKKLLKKIFDQLKTVDI--LIN 90
Cdd:cd05356   9 ATDGIGKAYAEELAKRGFNVILISRTQEKLDAVAKEIEEKYGVETKTIAADFSA----GDDIYERIEKELEGLDIgiLVN 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       91 GAGI----------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSASKAAVVS 160
Cdd:cd05356  85 NVGIshsipeyfleTPEDELQDIINVNVMATLKMTRLILPGMVKRKKG---AIVNISSFAGLIPTPLLATYSASKAFLDF 161

                       170       180
                ....*....|....*....|....*.
1B16_A      161 FTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:cd05356 162 FSRALYEEYKSQGIDVQSLLPYLVAT 187
PRK08264 PRK08264
SDR family oxidoreductase;
1-190 1.25e-13

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 67.99  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNfvILDRVENPTALAELkaiNPKVnITFHTyDVTVP--VAESKkllkki 78
Cdd:PRK08264   2 MDIKGKVVLVTGANRGIGRAFVEQLLARGAAK--VYAAARDPESVTDL---GPRV-VPLQL-DVTDPasVAAAA------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 fDQLKTVDILINGAGI------LDDHQIE---RTIAINFTGLVNTTTA---ILdfwdKRKGGpgGIIANICSVTGFNAIH 146
Cdd:PRK08264  69 -EAASDVTILVNNAGIfrtgslLLEGDEDalrAEMETNYFGPLAMARAfapVL----AANGG--GAIVNVLSVLSWVNFP 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
1B16_A       147 QVPVYSASKAAVVSFTNSL-AKLAPiTGVTAYSINPGITRTPLVH 190
Cdd:PRK08264 142 NLGTYSASKAAAWSLTQALrAELAP-QGTRVLGVHPGPIDTDMAA 185
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
 4-182 1.56e-13

classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad and domain size of the classical SDRs, but has an atypical NAD-binding motif ([ST]G[GA]XGXXG). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 68.13  E-value: 1.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        4 TNKNVIFVAALGGIGldtsRELVKRNLKN---FVILDR-VENPTALAELKAINPKVNITFHTYDVTVPvaES-KKLLKKI 78
Cdd:cd08930   1 EDKIILITGAAGLIG----KAFCKALLSAgarLILADInAPALEQLKEELTNLYKNRVIALELDITSK--ESiKELIESY 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       79 FDQLKTVDILINGAGI-----------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNA--- 144
Cdd:cd08930  75 LEKFGRIDILINNAYPspkvwgsrfeeFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKG---SIINIASIYGVIApdf 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1B16_A      145 -IHQVP------VYSASKAAVVSFTNSLAKLAPITGVTAYSINPG 182
Cdd:cd08930 152 rIYENTqmyspvEYSVIKAGIIHLTKYLAKYYADTGIRVNAISPG 196
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 6-188 1.67e-13

HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC 7120 HetN, a putative oxidoreductase involved in heterocyst differentiation, and related proteins. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 67.77  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNlknfvilDRV----ENPTALAELKAINPKVNItfHTYDVTVPVAES--KKLLKKIF 79
Cdd:cd08932   1 KVALVTGASRGIGIEIARALARDG-------YRVslglRNPEDLAALSASGGDVEA--VPYDARDPEDARalVDALRDRF 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       80 DQlktVDILINGAGILD--------DHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIaNICSVTG-----FNAih 146
Cdd:cd08932  72 GR---IDVLVHNAGIGRpttlregsDAELEAHFSINVIAPAELTRALLPAL--REAGSGRVV-FLNSLSGkrvlaGNA-- 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1B16_A      147 qvpVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:cd08932 144 ---GYSASKFALRALAHALRQEGWDHGVRVSAVCPGFVDTPM 182
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
 3-189 1.90e-13

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 67.72  E-value: 1.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRveNPTALAELKAINPKVNITFHTYDVTVPVA---ESKKLLKKIF 79
Cdd:PRK12935   4 LNGKVAIVTGGAKGIGKAITVALAQEGAK--VVINY--NSSKEAAENLVNELGKEGHDVYAVQADVSkveDANRLVEEAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPVY 151
Cdd:PRK12935  80 NHFGKVDILVNNAGITRDRTFkklnredwERVIDVNLSSVFNTTSAVLPYITEAEEGR---IISISSIIGQAGGFGQTNY 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
1B16_A       152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK12935 157 SAAKAGMLGFTKSLALELAKTNVTVNAICPGFIDTEMV 194
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
3-189 2.25e-13

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 67.90  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTALAElKAINPKVNITFHTYDVTVP--VAESKKLLKKIFD 80
Cdd:PRK08226   4 LTGKTALITGALQGIGEGIARVFARHG-ANLILLDISPEIEKLAD-ELCGRGHRCTAVVADVRDPasVAAAIKRAKEKEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLktvDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTG-FNAIHQVPVY 151
Cdd:PRK08226  82 RI---DILVNNAGVcrlgsfldMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGR---IVMMSSVTGdMVADPGETAY 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
1B16_A       152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK08226 156 ALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMA 193
PRK07454 PRK07454
SDR family oxidoreductase;
6-188 2.67e-13

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 67.29  E-value: 2.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         6 KNVIFVAALGGIGLDTSRELVKRNLkNFVILDRveNPTALAELKA--INPKVNITFHTYDVTVPvAESKKLLKKIFDQLK 83
Cdd:PRK07454   7 PRALITGASSGIGKATALAFAKAGW-DLALVAR--SQDALEALAAelRSTGVKAAAYSIDLSNP-EAIAPGIAELLEQFG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        84 TVDILINGAGI----------LDDHQieRTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSA 153
Cdd:PRK07454  83 CPDVLINNAGMaytgpllempLSDWQ--WVIQLNLTSVFQCCSAVLPGMRARGGG---LIINVSSIAARNAFPQWGAYCV 157

                        170       180       190
                 ....*....|....*....|....*....|....*
1B16_A       154 SKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK07454 158 SKAALAAFTKCLAEEERSHGIRVCTITLGAVNTPL 192
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
 4-187 3.35e-13

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 67.11  E-value: 3.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        4 TNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVeNPTALAELKAINpkvNITFHTYDVTvpvaeSKKLLKKIFDQLK 83
Cdd:cd05368   1 DGKVALITAAAQGIGRAIALAFAREGAN--VIATDI-NEEKLKELERGP---GITTRVLDVT-----DKEQVAALAKEEG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       84 TVDILINGAG------ILD--DHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGfnAIHQVP---VYS 152
Cdd:cd05368  70 RIDVLFNCAGfvhhgsILDceDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGS---IINMSSVAS--SIKGVPnrfVYS 144

                       170       180       190
                ....*....|....*....|....*....|....*
1B16_A      153 ASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTP 187
Cdd:cd05368 145 TTKAAVIGLTKSVAADFAQQGIRCNAICPGTVDTP 179
PRK09072 PRK09072
SDR family oxidoreductase;
1-194 3.83e-13

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 67.27  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRveNPTALAELKAINPK-VNITFHTYDVTVPvAESKKLLKKIf 79
Cdd:PRK09072   1 MDLKDKRVLLTGASGGIGQALAEALAAAGAR-LLLVGR--NAEKLEALAARLPYpGRHRWVVADLTSE-AGREAVLARA- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDfWDKRKggPGGIIANICSVtgFNAIhQVP-- 149
Cdd:PRK09072  76 REMGGINVLINNAGVnhfalledQDPEAIERLLALNLTAPMQLTRALLP-LLRAQ--PSAMVVNVGST--FGSI-GYPgy 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
1B16_A       150 -VYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTplvhTFNS 194
Cdd:PRK09072 150 aSYCASKFALRGFSEALRReLAD-TGVRVLYLAPRATRT----AMNS 191
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
 3-186 4.05e-13

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 66.84  E-value: 4.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnfVIL-----DRVEN-PTALAELKAINPKVnITFhtyDVTVPvAESKKLLK 76
Cdd:cd05332   1 LQGKVVIITGASSGIGEELAYHLARLGAR--LVLsarreERLEEvKSECLELGAPSPHV-VPL---DMSDL-EDAEQVVE 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       77 KIFDQLKTVDILINGAGI-----LDDHQIERT---IAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQV 148
Cdd:cd05332  74 EALKLFGGLDILINNAGIsmrslFHDTSIDVDrkiMEVNYFGPVALTKAALPHLIERSQG---SIVVVSSIAGKIGVPFR 150

                       170       180       190
                ....*....|....*....|....*....|....*....
1B16_A      149 PVYSASKAAVVSFTNSL-AKLAPiTGVTAYSINPGITRT 186
Cdd:cd05332 151 TAYAASKHALQGFFDSLrAELSE-PNISVTVVCPGLIDT 188
PRK05872 PRK05872
short chain dehydrogenase; Provisional
 2-226 5.35e-13

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 67.30  E-value: 5.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRveNPTALAELKAINPKVNITFH-TYDVTVPVAeSKKLLKKIFD 80
Cdd:PRK05872   6 SLAGKVVVVTGAARGIGAELARRLHARGAK-LALVDL--EEAELAALAAELGGDDRVLTvVADVTDLAA-MQAAAEEAVE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGgpggIIANICSVTGFNAIHQVPVYS 152
Cdd:PRK05872  82 RFGGIDVVVANAGIAsggsvaqvDPDAFRRVIDVNLLGVFHTVRATLPALIERRG----YVLQVSSLAAFAAAPGMAAYC 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       153 ASKAAVVSFTNSL-AKLAPiTGVTAYSINPGITRTPLVhtfNSWLDVEPRVAELLLSHP-----TQTSEQCGQNFVKAIE 226
Cdd:PRK05872 158 ASKAGVEAFANALrLEVAH-HGVTVGSAYLSWIDTDLV---RDADADLPAFRELRARLPwplrrTTSVEKCAAAFVDGIE 233
PRK06484 PRK06484
short chain dehydrogenase; Validated
 8-189 6.67e-13

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 67.57  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         8 VIFVAALGGIGLDTSRELVkRNLKNFVILDR-VENPTALAElkainpKVNITFHTYDVTVPV-AESKKLLKKIFDQLKTV 85
Cdd:PRK06484   8 VLVTGAAGGIGRAACQRFA-RAGDQVVVADRnVERARERAD------SLGPDHHALAMDVSDeAQIREGFEQLHREFGRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        86 DILINGAGILDD----------HQIERTIAINFTGLVNTTTAILDFwdKRKGGPGGIIANICSVTGFNAIHQVPVYSASK 155
Cdd:PRK06484  81 DVLVNNAGVTDPtmtatldttlEEFARLQAINLTGAYLVAREALRL--MIEQGHGAAIVNVASGAGLVALPKRTAYSASK 158

                        170       180       190
                 ....*....|....*....|....*....|....*
1B16_A       156 AAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLV 189
Cdd:PRK06484 159 AAVISLTRSLAcEWAA-KGIRVNAVLPGYVRTQMV 192
PRK07069 PRK07069
short chain dehydrogenase; Validated
 13-205 9.42e-13

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 65.89  E-value: 9.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        13 ALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKA-IN----PKVNITFhTYDVTvPVAESKKLLKKIFDQLKTVDI 87
Cdd:PRK07069   7 AAGGLGRAIARRMAEQGAK--VFLTDINDAAGLDAFAAeINaahgEGVAFAA-VQDVT-DEAQWQALLAQAADAMGGLSV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        88 LINGAGILDDHQIE--------RTIAINFTGLVNTTTAILDFWdkRKGGPGGIIaNICSVTGFNAIHQVPVYSASKAAVV 159
Cdd:PRK07069  83 LVNNAGVGSFGAIEqieldewrRVMAINVESIFLGCKHALPYL--RASQPASIV-NISSVAAFKAEPDYTAYNASKAAVA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
1B16_A       160 SFTNSLAKLAPITG--VTAYSINPGITRTPLVHTFNSWLDVEPRVAEL 205
Cdd:PRK07069 160 SLTKSIALDCARRGldVRCNSIHPTFIRTGIVDPIFQRLGEEEATRKL 207
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 8-189 1.33e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 65.51  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         8 VIFVA-ALGGIGLDTSRELVKRNlKNFVILDRvENPTALAELKAINPKV-----NITFHTYDVTvPVAESKKLLKKIFDQ 81
Cdd:PRK12827   8 RVLITgGSGGLGRAIAVRLAADG-ADVIVLDI-HPMRGRAEADAVAAGIeaaggKALGLAFDVR-DFAATRAALDAGVEE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        82 LKTVDILINGAGILDD--------HQIERTIAINFTGLVNTTTAILDFWDKRKGGpgGIIANICSVTGFNAIH-QVPvYS 152
Cdd:PRK12827  85 FGRLDILVNNAGIATDaafaelsiEEWDDVIDVNLDGFFNVTQAALPPMIRARRG--GRIVNIASVAGVRGNRgQVN-YA 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
1B16_A       153 ASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLV 189
Cdd:PRK12827 162 ASKAGLIGLTKTLAnELAP-RGITVNAVAPGAINTPMA 198
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
 6-189 1.58e-12

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 64.78  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNLknFVILDRVeNPTALAELKAINPKVNITFHTYDVTVPVAESKKLLKKIFDQLKTV 85
Cdd:cd08931   1 KAIFITGAASGIGRETALLFARNGW--FVGLYDI-DEDGLAALAAELGAENVVAGALDVTDRAAWAAALADFAAATGGRL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       86 DILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWdkrKGGPGGIIANICSVTGFNAIHQVPVYSASKAA 157
Cdd:cd08931  78 DALFNNAGVGrggpfedvPLAAHDRMVDINVKGVLNGAYAALPYL---KATPGARVINTASSSAIYGQPDLAVYSATKFA 154

                       170       180       190
                ....*....|....*....|....*....|..
1B16_A      158 VVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:cd08931 155 VRGLTEALDVEWARHGIRVADVWPWFVDTPIL 186
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 59-186 4.00e-12

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 64.22  E-value: 4.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        59 FHTYDVTVPVAeskklLKKIFDQ----LKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILdfwdKR- 125
Cdd:PRK12939  60 AIAADLADPAS-----VQRFFDAaaaaLGGLDGLVNNAGItnsksateLDIDTWDAVMNVNVRGTFLMLRAAL----PHl 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
1B16_A       126 KGGPGGIIANICSVTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK12939 131 RDSGRGRIVNLASDTALWGAPKLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTAT 191
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
 3-188 6.39e-12

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 63.56  E-value: 6.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKAI--NPKVNITFHTYDVTVPvAESKKLLKKIFD 80
Cdd:cd05358   1 LKGKVALVTGASSGIGKAIAIRLATAGAN--VVVNYRSKEDAAEEVVEEikAVGGKAIAVQADVSKE-EDVVALFQSAIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       81 QLKTVDILINGAGI----------LDDHQieRTIAINFTG-LVNTTTAILDFWDKRKGGpggIIANICSVtgfnaiHQV- 148
Cdd:cd05358  78 EFGTLDILVNNAGLqgdasshemtLEDWN--KVIDVNLTGqFLCAREAIKRFRKSKIKG---KIINMSSV------HEKi 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
1B16_A      149 --PV---YSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPL 188
Cdd:cd05358 147 pwPGhvnYAASKGGVKMMTKTLAqEYAP-KGIRVNAIAPGAINTPI 191
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
 3-188 6.85e-12

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 63.58  E-value: 6.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSrELVKRNLKNFVILDR-VEN--PTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIF 79
Cdd:cd05364   1 LSGKVAIITGSSSGIGAGTA-ILFARLGARLALTGRdAERleETRQSCLQAGVSEKKILLVVADLTEE-EGQDRIISTTL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       80 DQLKTVDILINGAGIL-----DDHQIE---RTIAINFTGLVNTTTAILDFWDKRKGGpggiIANICSVTGFNAIHQVPVY 151
Cdd:cd05364  79 AKFGRLDILVNNAGILakgggEDQDIEeydKVMNLNLRAVIYLTKLAVPHLIKTKGE----IVNVSSVAGGRSFPGVLYY 154

                       170       180       190
                ....*....|....*....|....*....|....*...
1B16_A      152 SASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPL 188
Cdd:cd05364 155 CISKAALDQFTRCTAlELAP-KGVRVNSVSPGVIVTGF 191
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
 8-202 8.09e-12

classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a canonical active site triad (and also active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 63.17  E-value: 8.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        8 VIFVAALGGIGLDTSRELVKRNLKnFVILDRveNPTALAELKAinpKVNITFH-----TYDVTVPvAESKKLLKKIFDQL 82
Cdd:cd05360   3 VVITGASSGIGRATALAFAERGAK-VVLAAR--SAEALHELAR---EVRELGGeaiavVADVADA-AQVERAADTAVERF 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       83 KTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIaNICSVTGFNAIHQVPVYSAS 154
Cdd:cd05360  76 GRIDTWVNNAGVavfgrfedVTPEEFRRVFDVNYLGHVYGTLAALPHL--RRRGGGALI-NVGSLLGYRSAPLQAAYSAS 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
1B16_A      155 KAAVVSFTNSL-AKLA----PITgVTaySINPGITRTPLVHTFNSWLDVEPRV 202
Cdd:cd05360 153 KHAVRGFTESLrAELAhdgaPIS-VT--LVQPTAMNTPFFGHARSYMGKKPKP 202
PRK06398 PRK06398
aldose dehydrogenase; Validated
 2-189 8.16e-12

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 63.31  E-value: 8.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTalaelkainpKVNITFHTYDVTVPvAESKKLLKKIFDQ 81
Cdd:PRK06398   3 GLKDKVAIVTGGSQGIGKAVVNRLKEEGSN--VINFDIKEPS----------YNDVDYFKVDVSNK-EQVIKGIDYVISK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        82 LKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKggpGGIIANICSVTGFNAIHQVPVYSA 153
Cdd:PRK06398  70 YGRIDILVNNAGIesygaihaVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQD---KGVIINIASVQSFAVTRNAAAYVT 146

                        170       180       190
                 ....*....|....*....|....*....|....*..
1B16_A       154 SKAAVVSFTNSLA-KLAPItgVTAYSINPGITRTPLV 189
Cdd:PRK06398 147 SKHAVLGLTRSIAvDYAPT--IRCVAVCPGSIRTPLL 181
PRK07831 PRK07831
SDR family oxidoreductase;
3-187 8.91e-12

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 63.13  E-value: 8.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALG-GIGLDTSRELVKRNLKnFVILDRVEN--PTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIF 79
Cdd:PRK07831  15 LAGKVVLVTAAAGtGIGSATARRALEEGAR-VVISDIHERrlGETADELAAELGLGRVEAVVCDVTSE-AQVDALIDAAV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRkgGPGGIIANICSVTGFNAIHQVPVY 151
Cdd:PRK07831  93 ERLGRLDVLVNNAGLggqtpvvdMTDDEWSRVLDVTLTGTFRATRAALRYMRAR--GHGGVIVNNASVLGWRAQHGQAHY 170

                        170       180       190
                 ....*....|....*....|....*....|....*.
1B16_A       152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTP 187
Cdd:PRK07831 171 AAAKAGVMALTRCSALEAAEYGVRINAVAPSIAMHP 206
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
 3-189 1.15e-11

cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol reductases,including (6R)-2,2,6-trimethyl-1,4-cyclohexanedione (levodione) reductase of Corynebacterium aquaticum, catalyze the reversible oxidoreduction of hydroxycyclohexanone derivatives. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 62.92  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRVEN--PTALAELKAINPKVNITFHTYDVTvPVAESKKLLKKIFD 80
Cdd:cd05330   1 FKDKVVLITGGGSGLGLATAVRLAKEGAK-LSLVDLNEEglEAAKAALLEIAPDAEVLLIKADVS-DEAQVEAYVDATVE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       81 QLKTVDILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVY 151
Cdd:cd05330  79 QFGRIDGFFNNAGIegkqnltedFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSG---MIVNTASVGGIRGVGNQSGY 155

                       170       180       190
                ....*....|....*....|....*....|....*...
1B16_A      152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:cd05330 156 AAAKHGVVGLTRNSAVEYGQYGIRINAIAPGAILTPMV 193
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
 1-187 1.21e-11

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 63.11  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKrNLKNFVILDRVENptalaELKAinpkVNITFHTYDVTVPvAESKKLLKKIFD 80
Cdd:PRK06171   5 LNLQGKIIIVTGGSSGIGLAIVKELLA-NGANVVNADIHGG-----DGQH----ENYQFVPTDVSSA-EEVNHTVAEIIE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGI-----------------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFN 143
Cdd:PRK06171  74 KFGRIDGLVNNAGIniprllvdekdpagkyeLNEAAFDKMFNINQKGVFLMSQAVARQMVKQHDG---VIVNMSSEAGLE 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       144 AIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGIT-----RTP 187
Cdd:PRK06171 151 GSEGQSCYAATKAALNSFTRSWAKELGKHNIRVVGVAPGILeatglRTP 199
PRK06181 PRK06181
SDR family oxidoreductase;
5-186 1.38e-11

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 62.69  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         5 NKNVIFVAALGGIGLDTSRELVKRNLkNFVILDRveNPTALA----ELKAINPKVnITFHTyDVTVPvAESKKLLKKIFD 80
Cdd:PRK06181   1 GKVVIITGASEGIGRALAVRLARAGA-QLVLAAR--NETRLAslaqELADHGGEA-LVVPT-DVSDA-EACERLIEAAVA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGI--------LDDHQI-ERTIAINFTGLVNTTTAILDFWDKRKggpGGIIAnICSVTGFNAIHQVPVY 151
Cdd:PRK06181  75 RFGGIDILVNNAGItmwsrfdeLTDLSVfERVMRVNYLGAVYCTHAALPHLKASR---GQIVV-VSSLAGLTGVPTRSGY 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
1B16_A       152 SASKAAVVSFTNSL-AKLAPiTGVTAYSINPGITRT 186
Cdd:PRK06181 151 AASKHALHGFFDSLrIELAD-DGVAVTVVCPGFVAT 185
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 72-189 1.45e-11

classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 62.69  E-value: 1.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       72 KKLLKKIFDQLKTVDILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILDFWDkrkggPGGIIANICSVTGF 142
Cdd:cd05355  93 RDLVKEVVKEFGKLDILVNNAAYqhpqesiedITTEQLEKTFRTNIFSMFYLTKAALPHLK-----KGSSIINTTSVTAY 167

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1B16_A      143 NAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:cd05355 168 KGSPHLLDYAATKGAIVAFTRGLSLQLAEKGIRVNAVAPGPIWTPLI 214
PRK06484 PRK06484
short chain dehydrogenase; Validated
 34-189 1.93e-11

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 63.33  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        34 VILDR-VENPTALAEL---KAINPKVNITfhtydvtvPVAESKKLLKKIFDQLKTVDILINGAGILDD---------HQI 100
Cdd:PRK06484 297 LIIDRdAEGAKKLAEAlgdEHLSVQADIT--------DEAAVESAFAQIQARWGRLDVLVNNAGIAEVfkpsleqsaEDF 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       101 ERTIAINFTGLVNTTTAILdfwdkRKGGPGGIIANICSVTGFNAIHQVPVYSASKAAVVSFTNSLA-KLAPItGVTAYSI 179
Cdd:PRK06484 369 TRVYDVNLSGAFACARAAA-----RLMSQGGVIVNLGSIASLLALPPRNAYCASKAAVTMLSRSLAcEWAPA-GIRVNTV 442

                        170
                 ....*....|
1B16_A       180 NPGITRTPLV 189
Cdd:PRK06484 443 APGYIETPAV 452
PRK06841 PRK06841
short chain dehydrogenase; Provisional
 2-188 2.14e-11

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 61.98  E-value: 2.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRVEnptALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQ 81
Cdd:PRK06841  12 DLSGKVAVVTGGASGIGHAIAELFAAKGAR-VALLDRSE---DVAEVAAQLLGGNAKGLVCDVSDS-QSVEAAVAAVISA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        82 LKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPVYSA 153
Cdd:PRK06841  87 FGRIDILVNSAGVallapaedVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGK---IVNLASQAGVVALERHVAYCA 163

                        170       180       190
                 ....*....|....*....|....*....|....*.
1B16_A       154 SKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPL 188
Cdd:PRK06841 164 SKAGVVGMTKVLAlEWGP-YGITVNAISPTVVLTEL 198
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 72-188 2.26e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 62.05  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        72 KKLLKKIFDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAIldfwdKRKGGPGGIIANICSVTGFN 143
Cdd:PRK06077  72 ETLAKATIDRYGVADILVNNAGLglfspflnVDDKLIDKHISTDFKSVIYCSQEL-----AKEMREGGAIVNIASVAGIR 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
1B16_A       144 AIHQVPVYSASKAAVVSFTNSLA-KLAPITGVTAysINPGITRTPL 188
Cdd:PRK06077 147 PAYGLSIYGAMKAAVINLTKYLAlELAPKIRVNA--IAPGFVKTKL 190
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
 16-187 2.95e-11

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 61.53  E-value: 2.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       16 GIGLDTSRELVKRNLKNFVI-LDRVENPtaLAELKA-INPKVNITFHTYDVTVPvAESKKLLKKIFDQLKTVDILINGAG 93
Cdd:cd05367  10 GIGRALAEELLKRGSPSVVVlLARSEEP--LQELKEeLRPGLRVTTVKADLSDA-AGVEQLLEAIRKLDGERDLLINNAG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       94 IL---------DDHQIERTIAINFTGLVNTTTAILDfwDKRKGGPGGIIANICSVTGFNAIHQVPVYSASKAAVVSFTNS 164
Cdd:cd05367  87 SLgpvskiefiDLDELQKYFDLNLTSPVCLTSTLLR--AFKKRGLKKTVVNVSSGAAVNPFKGWGLYCSSKAARDMFFRV 164

                       170       180
                ....*....|....*....|...
1B16_A      165 LAKLAPitGVTAYSINPGITRTP 187
Cdd:cd05367 165 LAAEEP--DVRVLSYAPGVVDTD 185
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 63-188 3.59e-11

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 61.97  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        63 DVTVPvAESKKLLKKIFDQLKTVDILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILDFWdkrkgGPGGII 133
Cdd:PRK06701 104 DVSDE-AFCKDAVEETVRELGRLDILVNNAAFqypqqsledITAEQLDKTFKTNIYSYFHMTKAALPHL-----KQGSAI 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
1B16_A       134 ANICSVTGFNAIHQVPVYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPL 188
Cdd:PRK06701 178 INTGSITGYEGNETLIDYSATKGAIHAFTRSLAQsLVQ-KGIRVNAVAPGPIWTPL 232
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 2-182 4.59e-11

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 61.45  E-value: 4.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDR-VENPTALA-ELKAiNPKVNITFHTyDVTvPVAESKKLLKKIF 79
Cdd:PRK08277   7 SLKGKVAVITGGGGVLGGAMAKELARAGAK-VAILDRnQEKAEAVVaEIKA-AGGEALAVKA-DVL-DKESLEQARQQIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAG------ILDDHQ-----------------IERTIAINFTGLVNTTtaiLDFWDKRKGGPGGIIANI 136
Cdd:PRK08277  83 EDFGPCDILINGAGgnhpkaTTDNEFhelieptktffdldeegFEFVFDLNLLGTLLPT---QVFAKDMVGRKGGNIINI 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
1B16_A       137 CSVTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPG 182
Cdd:PRK08277 160 SSMNAFTPLTKVPAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPG 205
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
76-189 4.97e-11

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 61.18  E-value: 4.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        76 KKIFDQLKT----VDILINGAGILDD---HQIERT-----IAINFTGLVNTTTAILDFWDKRkgGPGGIIaNICSVTGFN 143
Cdd:PRK12938  69 KAAFDKVKAevgeIDVLVNNAGITRDvvfRKMTREdwtavIDTNLTSLFNVTKQVIDGMVER--GWGRII-NISSVNGQK 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
1B16_A       144 AIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK12938 146 GQFGQTNYSTAKAGIHGFTMSLAQEVATKGVTVNTVSPGYIGTDMV 191
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-189 5.76e-11

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 60.74  E-value: 5.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVI-LDRVENPTALAELKAINPKVniTFHTYDVTVPvAESKKLLKKIF 79
Cdd:PRK08217   1 MDLKDKVIVITGGAQGLGRAMAEYLAQKGAKLALIdLNQEKLEEAVAECGALGTEV--RGYAANVTDE-EDVEATFAQIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGILDD-----------------HQIERTIAINFTG--LVNTTTAILDFwdkrKGGPGGIIANICSVT 140
Cdd:PRK08217  78 EDFGQLNGLINNAGILRDgllvkakdgkvtskmslEQFQSVIDVNLTGvfLCGREAAAKMI----ESGSKGVIINISSIA 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       141 GFNAIHQVPvYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK08217 154 RAGNMGQTN-YSASKAGVAAMTVTWAKELARYGIRVAAIAPGVIETEMT 201
PRK05855 PRK05855
SDR family oxidoreductase;
8-191 5.77e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 61.92  E-value: 5.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         8 VIFVAALGGIGLDTSRELVKRNLKnFVILDRVE---NPTAlAELKAINPKVnitfHTYDVTVPVAES-KKLLKKIFDQLK 83
Cdd:PRK05855 318 VVVTGAGSGIGRETALAFAREGAE-VVASDIDEaaaERTA-ELIRAAGAVA----HAYRVDVSDADAmEAFAEWVRAEHG 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        84 TVDILINGAGI------LD--DHQIERTIAINFTGLVNTTTAildfWDKR--KGGPGGIIANICSVTGFNAIHQVPVYSA 153
Cdd:PRK05855 392 VPDIVVNNAGIgmaggfLDtsAEDWDRVLDVNLWGVIHGCRL----FGRQmvERGTGGHIVNVASAAAYAPSRSLPAYAT 467

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
1B16_A       154 SKAAVVSFTNSL-AKLAP--ItGVTAysINPGITRTPLVHT 191
Cdd:PRK05855 468 SKAAVLMLSECLrAELAAagI-GVTA--ICPGFVDTNIVAT 505
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
5-204 7.78e-11

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 60.51  E-value: 7.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         5 NKNVIFVAALG-GIGLDTSRELVKRNLKnFVILDRVENpTALAELKAINPKVNITFHtydVTVPVAESKKL---LKKIFD 80
Cdd:PRK08643   1 MSKVALVTGAGqGIGFAIAKRLVEDGFK-VAIVDYNEE-TAQAAADKLSKDGGKAIA---VKADVSDRDQVfaaVRQVVD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGI-----LDD---HQIERTIAINFTGLV-NTTTAILDFwdkRKGGPGGIIANICSVTGFNAIHQVPVY 151
Cdd:PRK08643  76 TFGDLNVVVNNAGVapttpIETiteEQFDKVYNINVGGVIwGIQAAQEAF---KKLGHGGKIINATSQAGVVGNPELAVY 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
1B16_A       152 SASKAAVVSFTNSLAK-LAP--ITgVTAYSinPGITRTPLvhtfnsWLDVEPRVAE 204
Cdd:PRK08643 153 SSTKFAVRGLTQTAARdLASegIT-VNAYA--PGIVKTPM------MFDIAHQVGE 199
PRK07074 PRK07074
SDR family oxidoreductase;
4-203 8.72e-11

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 60.55  E-value: 8.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         4 TNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKAINPKVNITFHTYDVTVPVAESKKLLKKIFDQlK 83
Cdd:PRK07074   1 TKRTALVTGAAGGIGQALARRFLAAG-DRVLALDI--DAAALAAFADALGDARFVPVACDLTDAASLAAALANAAAER-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        84 TVDILINGAGI-----LDDHQIE---RTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAI-HqvPVYSAS 154
Cdd:PRK07074  77 PVDVLVANAGAaraasLHDTTPAswrADNALNLEAAYLCVEAVLEGMLKRSRGA---VVNIGSVNGMAALgH--PAYSAA 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       155 KAAVVSFTNSLAKLAPITGVTAYSINPGITRTPlvhtfnSWldvEPRVA 203
Cdd:PRK07074 152 KAGLIHYTKLLAVEYGRFGIRANAVAPGTVKTQ------AW---EARVA 191
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 39-186 1.61e-10

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 59.93  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        39 VENPTALAELKAINPKvNITFHTYDVTVPvAESKKLLKKIFDQLKTVDILINGAGI--------LDDHQIERTIAINFTG 110
Cdd:PRK06180  35 VRSEAARADFEALHPD-RALARLLDVTDF-DAIDAVVADAEATFGPIDVLVNNAGYghegaieeSPLAEMRRQFEVNVFG 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1B16_A       111 LVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSASKAAVVSFTNSLAK-LAPI-TGVTAysINPGITRT 186
Cdd:PRK06180 113 AVAMTKAVLPGMRARRRG---HIVNITSMGGLITMPGIGYYCGSKFALEGISESLAKeVAPFgIHVTA--VEPGSFRT 185
PRK06179 PRK06179
short chain dehydrogenase; Provisional
 4-188 1.70e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 59.53  E-value: 1.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         4 TNKNVIFV-AALGGIGLDTSRELVKRNLKNFvilDRVENPTALAelkainPKVNITFHTYDVT--VPVAeskKLLKKIFD 80
Cdd:PRK06179   2 SNSKVALVtGASSGIGRATAEKLARAGYRVF---GTSRNPARAA------PIPGVELLELDVTddASVQ---AAVDEVIA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGI-----LDDHQIERTIAI---NFTGLVNTTTAILDFwdKRKGGPGGIIaNICSVTGFnaihqVP--- 149
Cdd:PRK06179  70 RAGRIDVLVNNAGVglagaAEESSIAQAQALfdtNVFGILRMTRAVLPH--MRAQGSGRII-NISSVLGF-----LPapy 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
1B16_A       150 --VYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06179 142 maLYAASKHAVEGYSESLDHEVRQFGIRVSLVEPAYTKTNF 182
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
 1-193 1.89e-10

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 59.16  E-value: 1.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAelKAINPKVNItfhtydvtVPV-----AESKKLL 75
Cdd:PRK12936   2 FDLSGRKALVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALA--AELGERVKI--------FPAnlsdrDEVKALG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        76 KKIFDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQ 147
Cdd:PRK12936  72 QKAEADLEGVDILVNNAGItkdglfvrMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGR---IINITSVVGVTGNPG 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
1B16_A       148 VPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFN 193
Cdd:PRK12936 149 QANYCASKAGMIGFSKSLAQEIATRNVTVNCVAPGFIESAMTGKLN 194
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
1-187 1.92e-10

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 59.27  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDR-VENPTALAELkainpkvnITFHTYDVTVPVAES---KKLLK 76
Cdd:PRK07067   2 MRLQGKVALLTGAASGIGEAVAERYLAEGAR-VVIADIkPARARLAALE--------IGPAAIAVSLDVTRQdsiDRIVA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        77 KIFDQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDFWDKRkgGPGGIIANICSVTGFNAIHQV 148
Cdd:PRK07067  73 AAVERFGGIDILFNNAALFDMAPIldisrdsyDRLFAVNVKGLFFLMQAVARHMVEQ--GRGGKIINMASQAGRRGEALV 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
1B16_A       149 PVYSASKAAVVSFTNSlAKLAPIT-GVTAYSINPGITRTP 187
Cdd:PRK07067 151 SHYCATKAAVISYTQS-AALALIRhGINVNAIAPGVVDTP 189
PRK07024 PRK07024
SDR family oxidoreductase;
43-188 2.10e-10

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 59.17  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        43 TALAELKAINPKvNITFHTYDVTVPVAESKKLLKKIF-DQLKTVDILINGAGIL---------DDHQIERTIAINFTGLV 112
Cdd:PRK07024  37 DALQAFAARLPK-AARVSVYAADVRDADALAAAAADFiAAHGLPDVVIANAGISvgtlteereDLAVFREVMDTNYFGMV 115

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1B16_A       113 NTttaILDFWDKRKGGPGGIIANICSVTGFNAIHQVPVYSASKAAVVSFTNSL-AKLAPiTGVTAYSINPGITRTPL 188
Cdd:PRK07024 116 AT---FQPFIAPMRAARRGTLVGIASVAGVRGLPGAGAYSASKAAAIKYLESLrVELRP-AGVRVVTIAPGYIRTPM 188
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
 1-192 2.46e-10

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 58.94  E-value: 2.46e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRveNPTAlAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFD 80
Cdd:cd05345   1 MRLEGKVAIVTGAGSGFGEGIARRFAQEGAR-VVIADI--NADG-AERVAADIGEAAIAIQADVTKR-ADVEAMVEAALS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       81 QLKTVDILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILDFWdkrKGGPGGIIANICSVTGFNAIHQVPVY 151
Cdd:cd05345  76 KFGRLDILVNNAGIthrnkpmleVDEEEFDRVFAVNVKSIYLSAQALVPHM---EEQGGGVIINIASTAGLRPRPGLTWY 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1B16_A      152 SASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHTF 192
Cdd:cd05345 153 NASKGWVVTATKAMAvELAP-RNIRVNCLCPVAGETPLLSMF 193
PRK06125 PRK06125
short chain dehydrogenase; Provisional
 1-210 2.60e-10

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 58.90  E-value: 2.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSR---------ELVKRNLknfvilDRVEnpTALAELKAINPkVNITFHTYDVTVPVAes 71
Cdd:PRK06125   3 LHLAGKRVLITGASKGIGAAAAEafaaegchlHLVARDA------DALE--ALAADLRAAHG-VDVAVHALDLSSPEA-- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        72 kklLKKIFDQLKTVDILINGAG--------ILDDHQIERTIAINFTGLVNTTTAildFWDKRKGGPGGIIANICSVTGFN 143
Cdd:PRK06125  72 ---REQLAAEAGDIDILVNNAGaipgggldDVDDAAWRAGWELKVFGYIDLTRL---AYPRMKARGSGVIVNVIGAAGEN 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1B16_A       144 AIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTF-----NSWLDVEPRVAELLLSHP 210
Cdd:PRK06125 146 PDADYICGSAGNAALMAFTRALGGKSLDDGVRVVGVNPGPVATDRMLTLlkgraRAELGDESRWQELLAGLP 217
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 3-191 4.37e-10

tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6,8-tetrahydroxynaphthalene reductase (4HNR) of Magnaporthe grisea and the related 1,3,8-trihydroxynaphthalene reductase (3HNR) are typical members of the SDR family containing the canonical glycine rich NAD(P)-binding site and active site tetrad, and function in fungal melanin biosynthesis. This subgroup also includes an SDR from Norway spruce that may function to protect against both biotic and abitoic stress. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 58.06  E-value: 4.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKAINPKVNITFHTY--DVTVPVAeskklLKKIFD 80
Cdd:cd05362   1 LAGKVALVTGASRGIGRAIAKRLARDGAS--VVVNYASSKAAAEEVVAEIEAAGGKAIAVqaDVSDPSQ-----VARLFD 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       81 QLKT----VDILINGAGILDDHQIERTIAINF--TGLVNTTTAildFWDKRKG----GPGGIIANICSVTGFNAIHQVPV 150
Cdd:cd05362  74 AAEKafggVDILVNNAGVMLKKPIAETSEEEFdrMFTVNTKGA---FFVLQEAakrlRDGGRIINISSSLTAAYTPNYGA 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
1B16_A      151 YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHT 191
Cdd:cd05362 151 YAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFYA 191
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 6-196 5.52e-10

retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup containing retinol-DHs and related proteins. Retinol is processed by a medium chain alcohol dehydrogenase followed by retinol-DHs. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. This subgroup includes the human proteins: retinol dehydrogenase -12, -13 ,and -14. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 58.25  E-value: 5.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNLKnfVIL---DRVENPTALAELKAINPKVNITFHTYDVTvPVAESKKLLKKIFDQL 82
Cdd:cd09807   2 KTVIITGANTGIGKETARELARRGAR--VIMacrDMAKCEEAAAEIRRDTLNHEVIVRHLDLA-SLKSIRAFAAEFLAEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       83 KTVDILINGAGIL------DDHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIaNICSVT-----------GFNAI 145
Cdd:cd09807  79 DRLDVLINNAGVMrcpyskTEDGFEMQFGVNHLGHFLLTNLLLDLL--KKSAPSRIV-NVSSLAhkagkinfddlNSEKS 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
1B16_A      146 HQVPV-YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL---VHTFNSWL 196
Cdd:cd09807 156 YNTGFaYCQSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELgrhTGIHHLFL 210
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
 3-187 1.20e-09

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 57.24  E-value: 1.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELkaINPkvnitfHTYDVTVPV---AESKKLLKKIF 79
Cdd:cd05363   1 LDGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAE--IGP------AACAISLDVtdqASIDRCVAALV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       80 DQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILdfwdKR--KGGPGGIIANICSVTGFNAIHQVP 149
Cdd:cd05363  73 DRWGSIDILVNNAALFDLAPIvditresyDRLFAINVSGTLFMMQAVA----RAmiAQGRGGKIINMASQAGRRGEALVG 148

                       170       180       190
                ....*....|....*....|....*....|....*....
1B16_A      150 VYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTP 187
Cdd:cd05363 149 VYCATKAAVISLTQSAGlNLIR-HGINVNAIAPGVVDGE 186
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 16-188 1.36e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 56.89  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        16 GIGLDTSRELVKRNLkNFVILDRVENPT---ALAELKAINPKVniTFHTYDVTvPVAESKKLLKKIFDQLKTVDILINGA 92
Cdd:PRK12745  13 GIGLGIARALAAAGF-DLAINDRPDDEElaaTQQELRALGVEV--IFFPADVA-DLSAHEAMLDAAQAAWGRIDCLVNNA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        93 GI-------LDDHQIE---RTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPV---YSASKAAVV 159
Cdd:PRK12745  89 GVgvkvrgdLLDLTPEsfdRVLAINLRGPFFLTQAVAKRMLAQPEPEELPHRSIVFVSSVNAIMVSPNrgeYCISKAGLS 168

                        170       180       190
                 ....*....|....*....|....*....|
1B16_A       160 SFTNSLA-KLAPiTGVTAYSINPGITRTPL 188
Cdd:PRK12745 169 MAAQLFAaRLAE-EGIGVYEVRPGLIKTDM 197
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
 3-189 1.56e-09

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 56.70  E-value: 1.56e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKAINPKVNITFHTyDVTVPvAESKKLLKKIFDQL 82
Cdd:cd05326   2 LDGKVAIITGGASGIGEATARLFAKHGAR--VVIADIDDDAGQAVAAELGDPDISFVHC-DVTVE-ADVRAAVDTAVARF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       83 KTVDILINGAGIL----------DDHQIERTIAIN----FTGLVNTTTAIldfwdkRKGGPGGIIaNICSVTGFNAIHQV 148
Cdd:cd05326  78 GRLDIMFNNAGVLgapcysiletSLEEFERVLDVNvygaFLGTKHAARVM------IPAKKGSIV-SVASVAGVVGGLGP 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1B16_A      149 PVYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLV 189
Cdd:cd05326 151 HAYTASKHAVLGLTRSAAtELGE-HGIRVNCVSPYGVATPLL 191
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
8-181 2.11e-09

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 57.55  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         8 VIFVA-ALGGIGLDTSRELVKRNlKNFVILDRveNPTALAELKA-INPKVNITFHTYDVTVPVAeskklLKKIFDQLKT- 84
Cdd:PRK08324 424 VALVTgAAGGIGKATAKRLAAEG-ACVVLADL--DEEAAEAAAAeLGGPDRALGVACDVTDEAA-----VQAAFEEAALa 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        85 ---VDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIANICSVTGFNAIHQVPVYSA 153
Cdd:PRK08324 496 fggVDIVVSNAGIaisgpieeTSDEDWRRSFDVNATGHFLVAREAVRIM--KAQGLGGSIVFIASKNAVNPGPNFGAYGA 573

                        170       180
                 ....*....|....*....|....*....
1B16_A       154 SKAAVVSFTNSLAK-LAPItGVTAYSINP 181
Cdd:PRK08324 574 AKAAELHLVRQLALeLGPD-GIRVNGVNP 601
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
 44-182 4.45e-09

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 55.34  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        44 ALAELKAINpkvnITFHTY--DVTVPvAESKKLLKKIFDQLKTVDILINGAGI-----LDDHQIE---RTIAINFTGLVN 113
Cdd:PRK08213  52 AAAHLEALG----IDALWIaaDVADE-ADIERLAEETLERFGHVDILVNNAGAtwgapAEDHPVEawdKVMNLNVRGLFL 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1B16_A       114 TTTAILDFWDKRKGGpgGIIANICSVTGFNAIH----QVPVYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPG 182
Cdd:PRK08213 127 LSQAVAKRSMIPRGY--GRIINVASVAGLGGNPpevmDTIAYNTSKGAVINFTRALAaEWGP-HGIRVNAIAPG 197
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 1-188 4.52e-09

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 55.56  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENptalaELKAINPKVNITFHTyDVTvPVAESKKLLKKIFD 80
Cdd:PRK06463   3 MRFKGKVALITGGTRGIGRAIAEAFLREGAKVAVLYNSAEN-----EAKELREKGVFTIKC-DVG-NRDQVKKSKEVVEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWDKRKggpGGIIANICSVTGF-NAIHQVPVY 151
Cdd:PRK06463  76 EFGRVDVLVNNAGIMylmpfeefDEEKYNKMIKINLNGAIYTTYEFLPLLKLSK---NGAIVNIASNAGIgTAAEGTTFY 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
1B16_A       152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06463 153 AITKAGIIILTRRLAFELGKYGIRVNAVAPGWVETDM 189
PRK06114 PRK06114
SDR family oxidoreductase;
81-188 6.27e-09

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 55.17  E-value: 6.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTG------FNAIH 146
Cdd:PRK06114  83 ELGALTLAVNAAGIananpaeeMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGS---IVNIASMSGiivnrgLLQAH 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
1B16_A       147 qvpvYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06114 160 ----YNASKAGVIHLSKSLAMEWVGRGIRVNSISPGYTATPM 197
PRK08589 PRK08589
SDR family oxidoreductase;
3-189 9.86e-09

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 54.40  E-value: 9.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKrnlknfvildrvENPTALAelKAINPKVNITF----------HTYDVTVPVAES- 71
Cdd:PRK08589   4 LENKVAVITGASTGIGQASAIALAQ------------EGAYVLA--VDIAEAVSETVdkiksnggkaKAYHVDISDEQQv 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        72 KKLLKKIFDQLKTVDILINGAGI------LDDHQIE---RTIAINFTGLVNTTTAILDFWDKRkggpGGIIANICSVTGF 142
Cdd:PRK08589  70 KDFASEIKEQFGRVDVLFNNAGVdnaagrIHEYPVDvfdKIMAVDMRGTFLMTKMLLPLMMEQ----GGSIINTSSFSGQ 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
1B16_A       143 NAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK08589 146 AADLYRSGYNAAKGAVINFTKSIAIEYGRDGIRANAIAPGTIETPLV 192
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
 86-187 9.94e-09

Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase (KR) domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 53.67  E-value: 9.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       86 DILINGAGILDD--------HQIERTIAINFTGLVNTTTAILDFWDKRkgGPGGIIaNICSVTGFNAIHQVPVYSASKAA 157
Cdd:cd02266  33 DVVVHNAAILDDgrlidltgSRIERAIRANVVGTRRLLEAARELMKAK--RLGRFI-LISSVAGLFGAPGLGGYAASKAA 109

                        90       100       110
                ....*....|....*....|....*....|
1B16_A      158 VVSFTNSLAKLAPITGVTAYSINPGITRTP 187
Cdd:cd02266 110 LDGLAQQWASEGWGNGLPATAVACGTWAGS 139
PRK05867 PRK05867
SDR family oxidoreductase;
2-202 1.26e-08

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 54.27  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNL------KNFVILDRVENPTALAELKAINPKVnitfhtyDVTVPvAESKKLL 75
Cdd:PRK05867   6 DLHGKRALITGASTGIGKRVALAYVEAGAqvaiaaRHLDALEKLADEIGTSGGKVVPVCC-------DVSQH-QQVTSML 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        76 KKIFDQLKTVDILINGAGILDDH--------QIERTIAINFTGLVNTTTAILDFWDKRkgGPGGIIANICSVTG--FNAI 145
Cdd:PRK05867  78 DQVTAELGGIDIAVCNAGIITVTpmldmpleEFQRLQNTNVTGVFLTAQAAAKAMVKQ--GQGGVIINTASMSGhiINVP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
1B16_A       146 HQVPVYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHTFNSWLDV-EPRV 202
Cdd:PRK05867 156 QQVSHYCASKAAVIHLTKAMAvELAP-HKIRVNSVSPGYILTELVEPYTEYQPLwEPKI 213
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
 68-182 1.29e-08

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 53.87  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       68 VAESKKLLKKIFDQLKTVDILINGAGILDDHQIERT--------IAINFTGLVNTTTAILDFWDKRKggpGGIIANICSV 139
Cdd:cd05353  72 VEDGEKIVKTAIDAFGRVDILVNNAGILRDRSFAKMseedwdlvMRVHLKGSFKVTRAAWPYMRKQK---FGRIINTSSA 148

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
1B16_A      140 TG-FNAIHQVPvYSASKAAVVSFTNSLAKLAPITGVTAYSINPG 182
Cdd:cd05353 149 AGlYGNFGQAN-YSAAKLGLLGLSNTLAIEGAKYNITCNTIAPA 191
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
57-186 1.41e-08

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 53.97  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        57 ITFHTYDVTVPvAESKKLLKKIFDQLKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGG 128
Cdd:PRK06935  65 VTFVQVDLTKP-ESAEKVVKEALEEFGKIDILVNNAGTIrraplleyKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSG 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
1B16_A       129 PggiIANICSVTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK06935 144 K---IINIASMLSFQGGKFVPAYTASKHGVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
PRK07063 PRK07063
SDR family oxidoreductase;
3-210 1.44e-08

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 53.90  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKRNLKNFVI-LDRVENPTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFDQ 81
Cdd:PRK07063   5 LAGKVALVTGAAQGIGAAIARAFAREGAAVALAdLDAALAERAAAAIARDVAGARVLAVPADVTDA-ASVAAAVAAAEEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        82 LKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKggpGGIIANICSVTGFNAI-HQVPvYS 152
Cdd:PRK07063  84 FGPLDVLVNNAGInvfadplaMTDEDWRRCFAVDLDGAWNGCRAVLPGMVERG---RGSIVNIASTHAFKIIpGCFP-YP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       153 ASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHT-FNSWLDVEPRVAELLLSHP 210
Cdd:PRK07063 160 VAKHGLLGLTRALGiEYAA-RNVRVNAIAPGYIETQLTEDwWNAQPDPAAARAETLALQP 218
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
2-186 2.85e-08

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 52.98  E-value: 2.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTALAELKAINPKvnitFHTydVTVPVAESKKL---LKKI 78
Cdd:PRK12481   5 DLNGKVAIITGCNTGLGQGMAIGLAKAG-ADIVGVGVAEAPETQAQVEALGRK----FHF--ITADLIQQKDIdsiVSQA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGIlddhqIERTIAINFT-----GLVNTTTAILDFWDKR------KGGPGGIIANICSVTGFNAIHQ 147
Cdd:PRK12481  78 VEVMGHIDILINNAGI-----IRRQDLLEFGnkdwdDVININQKTVFFLSQAvakqfvKQGNGGKIINIASMLSFQGGIR 152

                        170       180       190
                 ....*....|....*....|....*....|....*....
1B16_A       148 VPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK12481 153 VPSYTASKSAVMGLTRALATELSQYNINVNAIAPGYMAT 191
PRK12937 PRK12937
short chain dehydrogenase; Provisional
 75-188 3.62e-08

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 52.82  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        75 LKKIFD----QLKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILdfwdkRKGGPGGIIANI-CSVTG 141
Cdd:PRK12937  70 VTRLFDaaetAFGRIDVLVNNAGVMplgtiadfDLEDFDRTIATNLRGAFVVLREAA-----RHLGQGGRIINLsTSVIA 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
1B16_A       142 FnAIHQVPVYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTPL 188
Cdd:PRK12937 145 L-PLPGYGPYAASKAAVEGLVHVLANeLRG-RGITVNAVAPGPVATEL 190
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
 72-183 4.77e-08

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 52.20  E-value: 4.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       72 KKLLKKIFDQLKTVDILINGAG--------ILDDHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIANIC---SVT 140
Cdd:cd05369  69 EAAVDETLKEFGKIDILINNAAgnflapaeSLSPNGFKTVIDIDLNGTFNTTKAVGKRL--IEAKHGGSILNISatyAYT 146

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
1B16_A      141 GFNAihQVPVySASKAAVVSFTNSLA-KLAPiTGVTAYSINPGI 183
Cdd:cd05369 147 GSPF--QVHS-AAAKAGVDALTRSLAvEWGP-YGIRVNAIAPGP 186
PRK07109 PRK07109
short chain dehydrogenase; Provisional
 1-201 5.60e-08

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 52.62  E-value: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRveNPTALAELKA-INPKVNitfHTYDVTVPVAESKKLLK--- 76
Cdd:PRK07109   4 KPIGRQVVVITGASAGVGRATARAFARRGAK-VVLLAR--GEEGLEALAAeIRAAGG---EALAVVADVADAEAVQAaad 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        77 KIFDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWdKRKGGpgGIIANICSVTGFNAIHQV 148
Cdd:PRK07109  78 RAEEELGPIDTWVNNAMVtvfgpfedVTPEEFRRVTEVTYLGVVHGTLAALRHM-RPRDR--GAIIQVGSALAYRSIPLQ 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
1B16_A       149 PVYSASKAAVVSFTNSL-AKL----APITgVTaySINPGITRTPLVHTFNSWLDVEPR 201
Cdd:PRK07109 155 SAYCAAKHAIRGFTDSLrCELlhdgSPVS-VT--MVQPPAVNTPQFDWARSRLPVEPQ 209
PRK06194 PRK06194
hypothetical protein; Provisional
 2-232 6.21e-08

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 52.33  E-value: 6.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENP---TALAELKAINPKVnITFHTyDVTVPvAESKKLLKKI 78
Cdd:PRK06194   3 DFAGKVAVITGAASGFGLAFARIGAALGMK--LVLADVQQDaldRAVAELRAQGAEV-LGVRT-DVSDA-AQVEALADAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGI-----LDDHQI---ERTIAINFTGLVNTT---TAILDFWDKRKGGPGGIIANICSVTGFNAIHQ 147
Cdd:PRK06194  78 LERFGAVHLLFNNAGVgagglVWENSLadwEWVLGVNLWGVIHGVrafTPLMLAAAEKDPAYEGHIVNTASMAGLLAPPA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       148 VPVYSASKAAVVSFTNSL-AKLAPITG-VTAYSINPGITRTPLVHtfnSWLDvepRVAELLLSHPTQTSEQCGQNFV-KA 224
Cdd:PRK06194 158 MGIYNVSKHAVVSLTETLyQDLSLVTDqVGASVLCPYFVPTGIWQ---SERN---RPADLANTAPPTRSQLIAQAMSqKA 231


                 ....*...
1B16_A       225 IEANKNGA 232
Cdd:PRK06194 232 VGSGKVTA 239
PRK05650 PRK05650
SDR family oxidoreductase;
73-194 6.22e-08

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 52.35  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        73 KLLKKIFDQLKTVDILINGAGI-----LDDHQIER---TIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNA 144
Cdd:PRK05650  66 ALAQACEEKWGGIDVIVNNAGVasggfFEELSLEDwdwQIAINLMGVVKGCKAFLPLFKRQKSGR---IVNIASMAGLMQ 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
1B16_A       145 IHQVPVYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHTFNS 194
Cdd:PRK05650 143 GPAMSSYNVAKAGVVALSETLLvELAD-DEIGVHVVCPSFFQTNLLDSFRG 192
PRK07035 PRK07035
SDR family oxidoreductase;
78-209 6.72e-08

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 51.94  E-value: 6.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        78 IFDQLKT----VDILINGAG-------ILDDHQI--ERTIAINFTG--LVNTTTAILdfwdKRKGGpGGIIANICSVTGF 142
Cdd:PRK07035  75 LFAHIRErhgrLDILVNNAAanpyfghILDTDLGafQKTVDVNIRGyfFMSVEAGKL----MKEQG-GGSIVNVASVNGV 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1B16_A       143 NAIHQVPVYSASKAAVVSFTNSLAK-LAPItGVTAYSINPGITRTplvhTFNSWLDVEPRVAELLLSH 209
Cdd:PRK07035 150 SPGDFQGIYSITKAAVISMTKAFAKeCAPF-GIRVNALLPGLTDT----KFASALFKNDAILKQALAH 212
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
 3-208 6.82e-08

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 52.13  E-value: 6.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTAL-AELKAINpkvNITFHTYDVTVPVAES-KKLLKKIFD 80
Cdd:cd05343   4 WRGRVALVTGASVGIGAAVARALVQHGMKVVGCARRVDKIEALaAECQSAG---YPTLFPYQCDLSNEEQiLSMFSAIRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       81 QLKTVDILINGAGIL--------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIaNICSVTGfnaiHQVP--- 149
Cdd:cd05343  81 QHQGVDVCINNAGLArpepllsgKTEGWKEMFDVNVLALSICTREAYQSMKERNVDDGHII-NINSMSG----HRVPpvs 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1B16_A      150 ---VYSASKAAVVSFTNSL------AKlapiTGVTAYSINPGITRTPLVHTFNswlDVEPRVAELLLS 208
Cdd:cd05343 156 vfhFYAATKHAVTALTEGLrqelreAK----THIRATSISPGLVETEFAFKLH---DNDPEKAAATYE 216
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
 88-224 7.51e-08

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 51.89  E-value: 7.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       88 LINGAGIL-----------DDHQieRTIAINFTGLVNTTTAILDFWDKRKGGpggiIANICSVTGFNAIHQVPVYSASKA 156
Cdd:cd09805  82 LVNNAGILgfggdeellpmDDYR--KCMEVNLFGTVEVTKAFLPLLRRAKGR----VVNVSSMGGRVPFPAGGAYCASKA 155

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      157 AVVSFTNSLAK-LAPItGVTAYSINPGITRTPLVHTFNSWLdvepRVAELLLSH-PTQTSEQCGQNFVKA 224
Cdd:cd09805 156 AVEAFSDSLRReLQPW-GVKVSIIEPGNFKTGITGNSELWE----KQAKKLWERlPPEVKKDYGEDYIDE 220
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
 3-197 9.22e-08

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 51.77  E-value: 9.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVEN-PTALAELKAINPKVNITFhtydVTVPVAESK-KLLKKIFD 80
Cdd:cd08936   8 LANKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNvDRAVATLQGEGLSVTGTV----CHVGKAEDReRLVATAVN 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       81 QLKTVDILINGAG-------ILD--DHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIAnicSVTGFNAIHQVPVY 151
Cdd:cd08936  84 LHGGVDILVSNAAvnpffgnILDstEEVWDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVS---SVAAFHPFPGLGPY 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
1B16_A      152 SASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHTFnsWLD 197
Cdd:cd08936 161 NVSKTALLGLTKNLApELAP-RNIRVNCLAPGLIKTSFSSAL--WMD 204
PRK07326 PRK07326
SDR family oxidoreductase;
1-165 1.14e-07

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 51.16  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRVENPTALAeLKAINPKVNITFHTYDVTVPVAEsKKLLKKIFD 80
Cdd:PRK07326   2 MSLKGKVALITGGSKGIGFAIAEALLAEGYK-VAITARDQKELEEA-AAELNNKGNVLGLAADVRDEADV-QRAVDAIVA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRkggpGGIIANICSVTGFNAIHQVPVYS 152
Cdd:PRK07326  79 AFGGLDVLIANAGVghfapveeLTPEEWRLVIDTNLTGAFYTIKAAVPALKRG----GGYIINISSLAGTNFFAGGAAYN 154

                        170
                 ....*....|...
1B16_A       153 ASKAAVVSFTNSL 165
Cdd:PRK07326 155 ASKFGLVGFSEAA 167
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
 70-189 1.28e-07

tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup includes TR-I and TR-II; these proteins are members of the SDR family. TRs catalyze the NADPH-dependent reductions of the 3-carbonyl group of tropinone, to a beta-hydroxyl group. TR-I and TR-II produce different stereoisomers from tropinone, TR-I produces tropine (3alpha-hydroxytropane), and TR-II, produces pseudotropine (sigma-tropine, 3beta-hydroxytropane). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 51.30  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       70 ESKKLLKKIFDQL-KTVDILINGAGIL----------DDHQIerTIAINFTGLVNTTTAildFWDKRKGGPGGIIANICS 138
Cdd:cd05329  69 ERQELMDTVASHFgGKLNILVNNAGTNirkeakdyteEDYSL--IMSTNFEAAYHLSRL---AHPLLKASGNGNIVFISS 143

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
1B16_A      139 VTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:cd05329 144 VAGVIAVPSGAPYGATKGALNQLTRSLACEWAKDNIRVNAVAPWVIATPLV 194
PRK06198 PRK06198
short chain dehydrogenase; Provisional
 2-187 1.51e-07

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 51.16  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENP--TALAELKAINPKVniTFHTYDVTvPVAESKKLLKKIF 79
Cdd:PRK06198   3 RLDGKVALVTGGTQGLGAAIARAFAERGAAGLVICGRNAEKgeAQAAELEALGAKA--VFVQADLS-DVEDCRRVVAAAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGILDDHQI--------ERTIAINFTG---LVNTTTAILdfwdKRKGGPGGIIaNICSVTGFNAIHQV 148
Cdd:PRK06198  80 EAFGRLDALVNAAGLTDRGTIldtspelfDRHFAVNVRApffLMQEAIKLM----RRRKAEGTIV-NIGSMSAHGGQPFL 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       149 PVYSASKAAvvsftnslakLAPITGVTAYS----------INPGITRTP 187
Cdd:PRK06198 155 AAYCASKGA----------LATLTRNAAYAllrnrirvngLNIGWMATE 193
PRK06138 PRK06138
SDR family oxidoreductase;
1-188 1.95e-07

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 50.54  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLknFVILDRVENPTALAELKAINPKVNITFHTYDVTVPvAESKKLLKKIFD 80
Cdd:PRK06138   1 MRLAGRVAIVTGAGSGIGRATAKLFAREGA--RVVVADRDAEAAERVAAAIAAGGRAFARQGDVGSA-EAVEALVDFVAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYS 152
Cdd:PRK06138  78 RWGRLDVLVNNAGFgcggtvvtTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGG---SIVNTASQLALAGGRGRAAYV 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
1B16_A       153 ASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06138 155 ASKGAIASLTRAMALDHATDGIRVNAVAPGTIDTPY 190
PRK09242 PRK09242
SDR family oxidoreductase;
3-188 2.03e-07

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 50.52  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSREL---------VKRNLKNfviLDRVENptalaELKAINPKVNITFHTYDVTVPVaESKK 73
Cdd:PRK09242   7 LDGQTALITGASKGIGLAIAREFlglgadvliVARDADA---LAQARD-----ELAEEFPEREVHGLAADVSDDE-DRRA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        74 LLKKIFDQLKTVDILINGAGI------LDDHQIE--RTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAI 145
Cdd:PRK09242  78 ILDWVEDHWDGLHILVNNAGGnirkaaIDYTEDEwrGIFETNLFSAFELSRYAHPLLKQHASSA---IVNIGSVSGLTHV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
1B16_A       146 HQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK09242 155 RSGAPYGMTKAALLQMTRNLAVEWAEDGIRVNAVAPWYIRTPL 197
PRK06172 PRK06172
SDR family oxidoreductase;
1-210 2.09e-07

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 50.52  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVI-LDRVENPTALAELKAINPKVniTFHTYDVTVPvAESKKLLKKIF 79
Cdd:PRK06172   3 MTFSGKVALVTGGAAGIGRATALAFAREGAKVVVAdRDAAGGEETVALIREAGGEA--LFVACDVTRD-AEVKALVEQTI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGI------LDDH---QIERTIAINFTG----LVNTTTAILdfwdkrKGGpGGIIANICSVTGFNAIH 146
Cdd:PRK06172  80 AAYGRLDYAFNNAGIeieqgrLAEGseaEFDAIMGVNVKGvwlcMKYQIPLML------AQG-GGAIVNTASVAGLGAAP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
1B16_A       147 QVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFnswLDVEPRVAELLLS-HP 210
Cdd:PRK06172 153 KMSIYAASKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTDMFRRA---YEADPRKAEFAAAmHP 214
PRK05866 PRK05866
SDR family oxidoreductase;
2-189 2.42e-07

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 50.51  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAElkainpkvNIT-------FHTYDVTVPVAeSKKL 74
Cdd:PRK05866  37 DLTGKRILLTGASSGIGEAAAEQFARRGATVVAVARREDLLDAVAD--------RITraggdamAVPCDLSDLDA-VDAL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        75 LKKIFDQLKTVDILINGAG---------ILDD-HQIERTIAINFTGLVNTTTAILDFWDKRKGGpggiiaNICSVTGFNA 144
Cdd:PRK05866 108 VADVEKRIGGVDILINNAGrsirrplaeSLDRwHDVERTMVLNYYAPLRLIRGLAPGMLERGDG------HIINVATWGV 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       145 IHQVP----VYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLV 189
Cdd:PRK05866 182 LSEASplfsVYNASKAALSAVSRVIETEWGDRGVHSTTLYYPLVATPMI 230
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 63-186 3.75e-07

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 49.78  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        63 DVTVPVAeSKKLLKKIFDQLKTVDILINGA--------GILDDHQIERTIAINFTGlvnTTTAILDFWDKRKGGPGGIIA 134
Cdd:PRK12859  76 DLTQNDA-PKELLNKVTEQLGYPHILVNNAaystnndfSNLTAEELDKHYMVNVRA---TTLLSSQFARGFDKKSGGRII 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
1B16_A       135 NICSVTGFNAIHQVPVYSASKAAVVSFTNSLA-KLAPItGVTAYSINPGITRT 186
Cdd:PRK12859 152 NMTSGQFQGPMVGELAYAATKGAIDALTSSLAaEVAHL-GITVNAINPGPTDT 203
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
74-186 4.18e-07

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 49.49  E-value: 4.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        74 LLKKIFDQLKTVDILINGAGIlddhqIERTIAINFT-----GLVNTTTAILDFWDKR------KGGPGGIIANICSVTGF 142
Cdd:PRK08993  75 LLERAVAEFGHIDILVNNAGL-----IRREDAIEFSekdwdDVMNLNIKSVFFMSQAaakhfiAQGNGGKIINIASMLSF 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
1B16_A       143 NAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK08993 150 QGGIRVPSYTASKSGVMGVTRLMANEWAKHNINVNAIAPGYMAT 193
PRK06123 PRK06123
SDR family oxidoreductase;
73-186 5.38e-07

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 49.39  E-value: 5.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        73 KLLKKIFDQLKTVDILINGAGIL---------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTG-F 142
Cdd:PRK06123  69 RLFEAVDRELGRLDALVNNAGILeaqmrleqmDAARLTRIFATNVVGSFLCAREAVKRMSTRHGGRGGAIVNVSSMAArL 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
1B16_A       143 NAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK06123 149 GSPGEYIDYAASKGAIDTMTIGLAKEVAAEGIRVNAVRPGVIYT 192
PRK06949 PRK06949
SDR family oxidoreductase;
84-190 7.77e-07

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 48.99  E-value: 7.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        84 TVDILINGAGILDDHQIERTIAINFTGLVNTTTAILDFWDK--------RKGG-----PGGIIANICSVTGFNAIHQVPV 150
Cdd:PRK06949  86 TIDILVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQevakrmiaRAKGagntkPGGRIINIASVAGLRVLPQIGL 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
1B16_A       151 YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVH 190
Cdd:PRK06949 166 YCMSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTEINH 205
PRK06057 PRK06057
short chain dehydrogenase; Provisional
 3-188 1.36e-06

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 48.19  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTAlaelKAINPKVNITFHTYDVTVPVAeSKKLLKKIFDQL 82
Cdd:PRK06057   5 LAGRVAVITGGGSGIGLATARRLAAEGAT--VVVGDIDPEAG----KAAADEVGGLFVPTDVTDEDA-VNALFDTAAETY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        83 KTVDILINGAGIL--DDHQIE--------RTIAINFTGLVNTTTAILDFwdKRKGGPGGII--ANICSVTGfNAIHQVPv 150
Cdd:PRK06057  78 GSVDIAFNNAGISppEDDSILntgldawqRVQDVNLTSVYLCCKAALPH--MVRQGKGSIIntASFVAVMG-SATSQIS- 153

                        170       180       190
                 ....*....|....*....|....*....|....*...
1B16_A       151 YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06057 154 YTASKGGVLAMSRELGVQFARQGIRVNALCPGPVNTPL 191
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 2-181 1.41e-06

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 48.24  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTA---LAELKAINPKVniTFHTYDVTVpvAESKKLLKKI 78
Cdd:PRK07792   9 DLSGKVAVVTGAAAGLGRAEALGLARLG-ATVVVNDVASALDAsdvLDEIRAAGAKA--VAVAGDISQ--RATADELVAT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        79 FDQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDFW-DKRKGGPG---GIIANICSVTGFNAIH 146
Cdd:PRK07792  84 AVGLGGLDIVVNNAGITRDRMLfnmsdeewDAVIAVHLRGHFLLTRNAAAYWrAKAKAAGGpvyGRIVNTSSEAGLVGPV 163

                        170       180       190
                 ....*....|....*....|....*....|....*
1B16_A       147 QVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINP 181
Cdd:PRK07792 164 GQANYGAAKAGITALTLSAARALGRYGVRANAICP 198
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
 85-229 1.54e-06

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 47.84  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       85 VDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPVYSASKA 156
Cdd:cd09806  80 VDVLVCNAGVgllgpleaLSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGR---ILVTSSVGGLQGLPFNDVYCASKF 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      157 AVVSFTNSLAKLAPITGVTAYSINPGitrtPlVHT------FNSWLDVEPRVAE---------LLLSHPTQTSEQCGQN- 220
Cdd:cd09806 157 ALEGLCESLAVQLLPFNVHLSLIECG----P-VHTafmekvLGSPEEVLDRTADdittfhffyQYLAHSKQVFREAAQNp 231

                       170
                ....*....|....*
1B16_A      221 ------FVKAIEANK 229
Cdd:cd09806 232 eevaevFLTAIRAPK 246
PRK06128 PRK06128
SDR family oxidoreductase;
72-188 2.41e-06

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 47.55  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        72 KKLLKKIFDQLKTVDILINGAGI---------LDDHQIERTIAINFTGLvntttaildFWDKRKG----GPGGIIANICS 138
Cdd:PRK06128 122 RQLVERAVKELGGLDILVNIAGKqtavkdiadITTEQFDATFKTNVYAM---------FWLCKAAiphlPPGASIINTGS 192

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
1B16_A       139 VTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06128 193 IQSYQPSPTLLDYASTKAAIVAFTKALAKQVAEKGIRVNAVAPGPVWTPL 242
PRK07577 PRK07577
SDR family oxidoreductase;
85-188 2.75e-06

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 47.03  E-value: 2.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        85 VDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAildFWDKRKGGPGGIIANICSVTGFNAIHQVPvYSASKA 156
Cdd:PRK07577  69 VDAIVNNVGIalpqplgkIDLAALQDVYDLNVRAAVQVTQA---FLEGMKLREQGRIVNICSRAIFGALDRTS-YSAAKS 144

                         90       100       110
                 ....*....|....*....|....*....|...
1B16_A       157 AVVSFTNSLA-KLAPiTGVTAYSINPGITRTPL 188
Cdd:PRK07577 145 ALVGCTRTWAlELAE-YGITVNAVAPGPIETEL 176
PRK06182 PRK06182
short chain dehydrogenase; Validated
 4-187 3.33e-06

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 46.88  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         4 TNKNVIFV-AALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELKAINPKVnitfhtyDVTVPvAESKKLLKKIFDQL 82
Cdd:PRK06182   1 MQKKVALVtGASSGIGKATARRLAAQGYTVYGAARRVDKMEDLASLGVHPLSL-------DVTDE-ASIKAAVDTIIAEE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        83 KTVDILINGAGI-----LDDHQIE---RTIAINFTGLVNTTTAILDFwdKRKGGPGGIIaNICSVTGfnAIHQvPV---Y 151
Cdd:PRK06182  73 GRIDVLVNNAGYgsygaIEDVPIDearRQFEVNLFGAARLTQLVLPH--MRAQRSGRII-NISSMGG--KIYT-PLgawY 146

                        170       180       190
                 ....*....|....*....|....*....|....*..
1B16_A       152 SASKAAVVSFTNSL-AKLAPItGVTAYSINPGITRTP 187
Cdd:PRK06182 147 HATKFALEGFSDALrLEVAPF-GIDVVVIEPGGIKTE 182
PRK06500 PRK06500
SDR family oxidoreductase;
3-188 3.36e-06

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 46.87  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRveNPTALAELKAI--NPKVNITFHTYDVtvpvAESKKLLKKIFD 80
Cdd:PRK06500   4 LQGKTALITGGTSGIGLETARQFLAEGAR-VAITGR--DPASLEAARAElgESALVIRADAGDV----AAQKALAQALAE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGILDDHQIE--------RTIAINFTGLVNTTTAILDFWDKrkggPGGIIANicsvTGFNAIHQVP--- 149
Cdd:PRK06500  77 AFGRLDAVFINAGVAKFAPLEdwdeamfdRSFNTNVKGPYFLIQALLPLLAN----PASIVLN----GSINAHIGMPnss 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
1B16_A       150 VYSASKAAVVSFTNSL-AKLAPiTGVTAYSINPGITRTPL 188
Cdd:PRK06500 149 VYAASKAALLSLAKTLsGELLP-RGIRVNAVSPGPVQTPL 187
PRK08265 PRK08265
short chain dehydrogenase; Provisional
 2-189 3.74e-06

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 46.93  E-value: 3.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDR-VENPTALAElkAINPkvNITFHTYDVTVPvAESKKLLKKIFD 80
Cdd:PRK08265   3 GLAGKVAIVTGGATLIGAAVARALVAAGAR-VAIVDIdADNGAAVAA--SLGE--RARFIATDITDD-AAIERAVATVVA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGILDDHQIE-------RTIAINftgLVNTTTAILDFWDKRKGGpGGIIANICSVTGFNAIHQVPVYSA 153
Cdd:PRK08265  77 RFGRVDILVNLACTYLDDGLAssradwlAALDVN---LVSAAMLAQAAHPHLARG-GGAIVNFTSISAKFAQTGRWLYPA 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
1B16_A       154 SKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLV 189
Cdd:PRK08265 153 SKAAIRQLTRSMAmDLAP-DGIRVNSVSPGWTWSRVM 188
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
 3-187 4.12e-06

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 46.75  E-value: 4.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRVENPTALA-ELKAINPKvnITFHTYDVTvPVAESKKLLKKIFDQ 81
Cdd:cd08937   2 FEGKVVVVTGAAQGIGRGVAERLAGEGAR-VLLVDRSELVHEVLaEILAAGDA--AHVHTADLE-TYAGAQGVVRAAVER 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       82 LKTVDILIN--GAGIL-------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNaIHQVPvYS 152
Cdd:cd08937  78 FGRVDVLINnvGGTIWakpyehyEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQG---VIVNVSSIATRG-IYRIP-YS 152

                       170       180       190
                ....*....|....*....|....*....|....*
1B16_A      153 ASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTP 187
Cdd:cd08937 153 AAKGGVNALTASLAFEHARDGIRVNAVAPGGTEAP 187
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
 16-186 4.37e-06

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 46.69  E-value: 4.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       16 GIGLDTSRELVKRNLkNFVILDRVEnPTALAELKAINPKVNITFHTYDVTV-PVAESKKLLKKIFDQLKTVDILINGAGI 94
Cdd:cd05337  12 GIGRAIATELAARGF-DIAINDLPD-DDQATEVVAEVLAAGRRAIYFQADIgELSDHEALLDQAWEDFGRLDCLVNNAGI 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       95 ----------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVP---VYSASKAAVVSF 161
Cdd:cd05337  90 avrprgdlldLTEDSFDRLIAINLRGPFFLTQAVARRMVEQPDRFDGPHRSIIFVTSINAYLVSPnrgEYCISKAGLSMA 169

                       170       180
                ....*....|....*....|....*.
1B16_A      162 TNSLA-KLAPiTGVTAYSINPGITRT 186
Cdd:cd05337 170 TRLLAyRLAD-EGIAVHEIRPGLIHT 194
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 3-213 4.93e-06

classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site tetrad and glycine-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 46.33  E-value: 4.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        3 LTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRVENPTALAELKAINPkvnitfHTYDVTVPVAES---KKLLKKIF 79
Cdd:cd08944   1 LEGKVAIVTGAGAGIGAACAARLAREGAR--VVVADIDGGAAQAVVAQIAG------GALALRVDVTDEqqvAALFERAV 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       80 DQLKTVDILINGAGILD-DHQIE--------RTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPV 150
Cdd:cd08944  73 EEFGGLDLLVNNAGAMHlTPAIIdtdlavwdQTMAINLRGTFLCCRHAAPRMIARGGGS---IVNLSSIAGQSGDPGYGA 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1B16_A      151 YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHT-FNSWLDVEPRVAELLLSHPTQT 213
Cdd:cd08944 150 YGASKAAIRNLTRTLAAELRHAGIRCNALAPGLIDTPLLLAkLAGFEGALGPGGFHLLIHQLQG 213
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
 2-197 5.73e-06

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 46.30  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLKnfVILDRvENPTALAELKAINPKVNITFHT--YDVTVPvAESKKLLKKIF 79
Cdd:PRK07523   7 DLTGRRALVTGSSQGIGYALAEGLAQAGAE--VILNG-RDPAKLAAAAESLKGQGLSAHAlaFDVTDH-DAVRAAIDAFE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        80 DQLKTVDILINGAGI-----LDDHQI---ERTIAINFTGLVNTTTAILDFWDKRkgGPGGIIaNICSVTGFNAIHQVPVY 151
Cdd:PRK07523  83 AEIGPIDILVNNAGMqfrtpLEDFPAdafERLLRTNISSVFYVGQAVARHMIAR--GAGKII-NIASVQSALARPGIAPY 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
1B16_A       152 SASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVH------TFNSWLD 197
Cdd:PRK07523 160 TATKGAVGNLTKGMATDWAKHGLQCNAIAPGYFDTPLNAalvadpEFSAWLE 211
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
 5-182 6.22e-06

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 46.03  E-value: 6.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        5 NKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRVENPTALAElKAINPkvNITFHTYDVTvPVAESKKLLKKIFDQLKT 84
Cdd:cd09761   1 GKVAIVTGGGHGIGKQICLDFLEAGDK-VVFADIDEERGADFA-EAEGP--NLFFVHGDVA-DETLVKFVVYAMLEKLGR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       85 VDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDFWdkRKGGpgGIIANICSVTGFNAIHQVPVYSASKA 156
Cdd:cd09761  76 IDVLVNNAARGSKGILssllleewDRILSVNLTGPYELSRYCRDEL--IKNK--GRIINIASTRAFQSEPDSEAYAASKG 151

                       170       180
                ....*....|....*....|....*..
1B16_A      157 AVVSFTNSLA-KLAPITGVTAysINPG 182
Cdd:cd09761 152 GLVALTHALAmSLGPDIRVNC--ISPG 176
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 42-182 6.74e-06

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 46.75  E-value: 6.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        42 PTALAELKAINPKVNITFHTYDVTVPVAeSKKLLKKIFDQLKTVDILINGAGI--------LDDHQIERTIAINFTGLVN 113
Cdd:PRK08261 243 PAAGEALAAVANRVGGTALALDITAPDA-PARIAEHLAERHGGLDIVVHNAGItrdktlanMDEARWDSVLAVNLLAPLR 321

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1B16_A       114 TTTAILdfwDKRKGGPGGIIANICSVTGF-------NaihqvpvYSASKAAVVSFTNSLAKLAPITGVTAYSINPG 182
Cdd:PRK08261 322 ITEALL---AAGALGDGGRIVGVSSISGIagnrgqtN-------YAASKAGVIGLVQALAPLLAERGITINAVAPG 387
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
 3-196 1.06e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 45.52  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         3 LTNKNVIFVAALGGIGLDTSRELVKRN---LKNFVILDRVENptALAELKAinpkVNITFHT--YDVTVPvAESKKLLKK 77
Cdd:PRK08085   7 LAGKNILITGSAQGIGFLLATGLAEYGaeiIINDITAERAEL--AVAKLRQ----EGIKAHAapFNVTHK-QEVEAAIEH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        78 IFDQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVP 149
Cdd:PRK08085  80 IEKDIGPIDVLINNAGIQRRHPFtefpeqewNDVIAVNQTAVFLVSQAVARYMVKRQAGK---IINICSMQSELGRDTIT 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
1B16_A       150 VYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHT------FNSWL 196
Cdd:PRK08085 157 PYAASKGAVKMLTRGMCVELARHNIQVNGIAPGYFKTEMTKAlvedeaFTAWL 209
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
 1-186 1.25e-05

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 45.15  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        1 MDLTNKNVIFVAALGGIGLDTSRELVKRNLKnFVILDRveNPTALAELKAINPkvnitfHTYDVTVPVA---ESKKLLKK 77
Cdd:cd05351   3 LDFAGKRALVTGAGKGIGRATVKALAKAGAR-VVAVSR--TQADLDSLVRECP------GIEPVCVDLSdwdATEEALGS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       78 IFdqlkTVDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAIL-DFWDKrkgGPGGIIANICSVTGFNAIHQV 148
Cdd:cd05351  74 VG----PVDLLVNNAAVailqpfleVTKEAFDRSFDVNVRAVIHVSQIVArGMIAR---GVPGSIVNVSSQASQRALTNH 146

                       170       180       190
                ....*....|....*....|....*....|....*....
1B16_A      149 PVYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRT 186
Cdd:cd05351 147 TVYCSTKAALDMLTKVMAlELGP-HKIRVNSVNPTVVMT 184
PRK07856 PRK07856
SDR family oxidoreductase;
1-192 1.27e-05

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 45.31  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVEnPTALAELKAinpkvniTFHTYDVTVPvAESKKLLKKIFD 80
Cdd:PRK07856   2 LDLTGRVVLVTGGTRGIGAGIARAFLAAG-ATVVVCGRRA-PETVDGRPA-------EFHAADVRDP-DQVAALVDAIVE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAG-----ILDD-----HqiERTIAINFTGLVNTTTAILDFWDKRKGGpgGIIANICSVTGFNAIHQVPV 150
Cdd:PRK07856  72 RHGRLDVLVNNAGgspyaLAAEasprfH--EKIVELNLLAPLLVAQAANAVMQQQPGG--GSIVNIGSVSGRRPSPGTAA 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
1B16_A       151 YSASKAAVVSFTNSLA-KLAPITGVTAysINPGITRTPLVHTF 192
Cdd:PRK07856 148 YGAAKAGLLNLTRSLAvEWAPKVRVNA--VVVGLVRTEQSELH 188
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 72-186 1.55e-05

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 45.07  E-value: 1.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        72 KKLLKKIFDQLKTVDILINGA--------GILDDHQIERTIAINFTGLVNTTTAildFWDKRKGGPGGIIANICSvtgfn 143
Cdd:PRK12748  83 NRVFYAVSERLGDPSILINNAaysthtrlEELTAEQLDKHYAVNVRATMLLSSA---FAKQYDGKAGGRIINLTS----- 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
1B16_A       144 AIHQVPV-----YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK12748 155 GQSLGPMpdelaYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT 202
PRK09730 PRK09730
SDR family oxidoreductase;
81-186 1.70e-05

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 44.84  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        81 QLKTVDILINGAGIL---------DDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTG-FNAIHQVPV 150
Cdd:PRK09730  76 HDEPLAALVNNAGILftqctvenlTAERINRVLSTNVTGYFLCCREAVKRMALKHGGSGGAIVNVSSAASrLGAPGEYVD 155

                         90       100       110
                 ....*....|....*....|....*....|....*.
1B16_A       151 YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK09730 156 YAASKGAIDTLTTGLSLEVAAQGIRVNCVRPGFIYT 191
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
 61-187 1.94e-05

haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. Haloalcohol dehalogenase show low sequence similarity to short-chain dehydrogenases/reductases (SDRs). Like the SDRs, haloalcohol dehalogenases have a conserved catalytic triad (Ser-Tyr-Lys/Arg), and form a Rossmann fold. However, the normal classical SDR NAD(P)-binding motif (TGXXGXG) and NAD-binding function is replaced with a halide binding site, allowing the enzyme to catalyze a dehalogenation reaction. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 44.49  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       61 TYDVTVPVAESK--KLLKKIFDQLKTVDILIN------------GAGILDDHQIERTIAINFTGLVNTTTAILdfwdkRK 126
Cdd:cd05361  47 ENPGTKALSEQKpeELVDAVLQAGGAIDVLVSndyiprpmnpidGTSEADIRQAFEALSIFPFALLQAAIAQM-----KK 121

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1B16_A      127 GGPGGIIAnICSVTGFNAIHQVPVYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTP 187
Cdd:cd05361 122 AGGGSIIF-ITSAVPKKPLAYNSLYGPARAAAVALAESLAKeLSR-DNILVYAIGPNFFNSP 181
PRK07832 PRK07832
SDR family oxidoreductase;
6-229 2.36e-05

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 44.65  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         6 KNVIFVAALGGIGLDTSRELVKRNLKNFvILDRVENPTAL--AELKAINPKVnITFHTYDVTvPVAESKKLLKKIFDQLK 83
Cdd:PRK07832   1 KRCFVTGAASGIGRATALRLAAQGAELF-LTDRDADGLAQtvADARALGGTV-PEHRALDIS-DYDAVAAFAADIHAAHG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        84 TVDILINGAGI--------LDDHQIERTIAINFTGLVNTttaILDFWDKR-KGGPGGIIANICSVTGFNAIHQVPVYSAS 154
Cdd:PRK07832  78 SMDVVMNIAGIsawgtvdrLTHEQWRRMVDVNLMGPIHV---IETFVPPMvAAGRGGHLVNVSSAAGLVALPWHAAYSAS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       155 KAAVVSFTNSLA-KLAPI-TGVTAysINPGITRTPLVHT------------FNSWLDVEPRVAelllshptQTSEQCGQN 220
Cdd:PRK07832 155 KFGLRGLSEVLRfDLARHgIGVSV--VVPGAVKTPLVNTveiagvdredprVQKWVDRFRGHA--------VTPEKAAEK 224


                 ....*....
1B16_A       221 FVKAIEANK 229
Cdd:PRK07832 225 ILAGVEKNR 233
PRK08219 PRK08219
SDR family oxidoreductase;
13-188 2.48e-05

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 44.15  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        13 ALGGIGLDTSRELVKRNlkNFVILDRveNPTALAELKAINPKVnITFHTyDVTVPVAESKKllkkiFDQLKTVDILINGA 92
Cdd:PRK08219  11 ASRGIGAAIARELAPTH--TLLLGGR--PAERLDELAAELPGA-TPFPV-DLTDPEAIAAA-----VEQLGRLDVLVHNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        93 GILDDHQIE--------RTIAINFTGLVNTTTAILdfwdkrkggP-----GGIIANICSVTGFNAIHQVPVYSASKAAVV 159
Cdd:PRK08219  80 GVADLGPVAestvdewrATLEVNVVAPAELTRLLL---------PalraaHGHVVFINSGAGLRANPGWGSYAASKFALR 150

                        170       180       190
                 ....*....|....*....|....*....|
1B16_A       160 SFTNSL-AKLAPITGVTaySINPGITRTPL 188
Cdd:PRK08219 151 ALADALrEEEPGNVRVT--SVHPGRTDTDM 178
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
 131-230 3.08e-05

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This subgroup includes human DHRS1 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 43.97  E-value: 3.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      131 GIIANICSVTGFNAIHQVPvYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLVHTF-----NSWLDVEPRVAE 204
Cdd:cd09763 141 GLIVIISSTGGLEYLFNVA-YGVGKAAIDRMAADMAhELKP-HGVAVVSLWPGFVRTELVLEMpeddeGSWHAKERDAFL 218

                        90       100
                ....*....|....*....|....*.
1B16_A      205 lllshPTQTSEQCGQNFVkAIEANKN 230
Cdd:cd09763 219 -----NGETTEYSGRCVV-ALAADPD 238
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 1-188 3.10e-05

2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 44.18  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDLTNKNVIFVAALGGIGldtsRELVKRnlknFV-------ILDRveNPTALAELKAINPKVNITFHTyDVTVpVAESKK 73
Cdd:PRK06200   2 GWLHGQVALITGGGSGIG----RALVER----FLaegarvaVLER--SAEKLASLRQRFGDHVLVVEG-DVTS-YADNQR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        74 LLKKIFDQLKTVDILINGAGILD---------DHQIERT----IAINFTGLVNTTTAILDfwdKRKGGPGGIIANIcSVT 140
Cdd:PRK06200  70 AVDQTVDAFGKLDCFVGNAGIWDyntslvdipAETLDTAfdeiFNVNVKGYLLGAKAALP---ALKASGGSMIFTL-SNS 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       141 GFNAIHQVPVYSASKAAVVSFTNSLA-KLAPITGVTAysINPGITRTPL 188
Cdd:PRK06200 146 SFYPGGGGPLYTASKHAVVGLVRQLAyELAPKIRVNG--VAPGGTVTDL 192
PRK08251 PRK08251
SDR family oxidoreductase;
4-232 4.10e-05

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 43.77  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         4 TNKNVIFVAALGGIGLDTSRELVKRNlKNFVI----LDRVEnptAL-AELKAINPKVNITFHTYDVT----VPvaeskkl 74
Cdd:PRK08251   1 TRQKILITGASSGLGAGMAREFAAKG-RDLALcarrTDRLE---ELkAELLARYPGIKVAVAALDVNdhdqVF------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        75 lkKIFDQLKT----VDILINGAGILDDHQI--------ERTIAINFTG-LVNTTTAILDFwdkRKGGPGGIIAnICSVTg 141
Cdd:PRK08251  70 --EVFAEFRDelggLDRVIVNAGIGKGARLgtgkfwanKATAETNFVAaLAQCEAAMEIF---REQGSGHLVL-ISSVS- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       142 fnAIHQVP----VYSASKAAVVSFTNSL-AKLA--PITgVTaySINPGITRTplvhtfnswlDVEPRVAELLLSHPTQTS 214
Cdd:PRK08251 143 --AVRGLPgvkaAYAASKAGVASLGEGLrAELAktPIK-VS--TIEPGYIRS----------EMNAKAKSTPFMVDTETG 207

                        250
                 ....*....|....*...
1B16_A       215 eqCgQNFVKAIEANKNGA 232
Cdd:PRK08251 208 --V-KALVKAIEKEPGRA 222
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 6-208 4.93e-05

dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an NAD-binding protein related to the SDRs. It converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamines synthesis. Dihydropteridine reductase has the YXXXK of these tyrosine-dependent oxidoreductases, but lacks the typical upstream Asn and Ser catalytic residues. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 43.08  E-value: 4.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        6 KNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENPTALAelkainpkvNITFHtyDVTVPVAESKKLLKKIFDQLKTV 85
Cdd:cd05334   2 RVVLVYGGRGALGSAVVQAFKSRG-WWVASIDLAENEEADA---------SIIVL--DSDSFTEQAKQVVASVARLSGKV 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       86 DILINGAG------ILDDHQIE---RTIAINftglVNTTTAILDFWDKRkGGPGGIIANICSVTGFNAIHQVPVYSASKA 156
Cdd:cd05334  70 DALICVAGgwaggsAKSKSFVKnwdLMWKQN----LWTSFIASHLATKH-LLSGGLLVLTGAKAALEPTPGMIGYGAAKA 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      157 AVVSFTNSLA--KLAPITGVTAYSINPGITRTPLVHT------FNSWLDVEpRVAELLLS 208
Cdd:cd05334 145 AVHQLTQSLAaeNSGLPAGSTANAILPVTLDTPANRKampdadFSSWTPLE-FIAELILF 203
PRK07985 PRK07985
SDR family oxidoreductase;
71-188 7.92e-05

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 43.06  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        71 SKKLLKKIFDQLKTVDILINGAGI---------LDDHQIERTIAINFTGLvntttaildFWDKRKGGP----GGIIANIC 137
Cdd:PRK07985 115 ARSLVHEAHKALGGLDIMALVAGKqvaipdiadLTSEQFQKTFAINVFAL---------FWLTQEAIPllpkGASIITTS 185

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
1B16_A       138 SVTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK07985 186 SIQAYQPSPHLLDYAATKAAILNYSRGLAKQVAEKGIRVNIVAPGPIWTAL 236
PRK08263 PRK08263
short chain dehydrogenase; Provisional
 85-182 8.19e-05

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 42.72  E-value: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        85 VDILINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWdkRKGGPGGIIaNICSVTGFNAIHQVPVYSASKA 156
Cdd:PRK08263  78 LDIVVNNAGYglfgmieeVTESEARAQIDTNFFGALWVTQAVLPYL--REQRSGHII-QISSIGGISAFPMSGIYHASKW 154

                         90       100
                 ....*....|....*....|....*.
1B16_A       157 AVVSFTNSLAKLAPITGVTAYSINPG 182
Cdd:PRK08263 155 ALEGMSEALAQEVAEFGIKVTLVEPG 180
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
 2-187 8.44e-05

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 42.74  E-value: 8.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         2 DLTNKNVIFVAALGGIGLDTSRELVKRNLK---NFVILDRVENptALAELKainpKVNITFHTY--DVTVPVaESKKLLK 76
Cdd:PRK07097   7 SLKGKIALITGASYGIGFAIAKAYAKAGATivfNDINQELVDK--GLAAYR----ELGIEAHGYvcDVTDED-GVQAMVS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        77 KIFDQLKTVDILINGAGIlddhqIERT-------------IAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFN 143
Cdd:PRK07097  80 QIEKEVGVIDILVNNAGI-----IKRIpmlemsaedfrqvIDIDLNAPFIVSKAVIPSMIKKGHGK---IINICSMMSEL 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
1B16_A       144 AIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTP 187
Cdd:PRK07097 152 GRETVSAYAAAKGGLKMLTKNIASEYGEANIQCNGIGPGYIATP 195
PRK05693 PRK05693
SDR family oxidoreductase;
63-182 8.91e-05

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 42.86  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        63 DVTVPvAESKKLLKKIFDQLKTVDILINGAG------ILDD--HQIERTIAINFTGLVNTTTAILDFWDKRKGgpggIIA 134
Cdd:PRK05693  52 DVNDG-AALARLAEELEAEHGGLDVLINNAGygamgpLLDGgvEAMRRQFETNVFAVVGVTRALFPLLRRSRG----LVV 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       135 NICSVTGFNAIHQVPVYSASKAAVVSFTNSL-AKLAPItGVTAYSINPG 182
Cdd:PRK05693 127 NIGSVSGVLVTPFAGAYCASKAAVHALSDALrLELAPF-GVQVMEVQPG 174
PRK07775 PRK07775
SDR family oxidoreductase;
8-186 1.03e-04

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 42.43  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         8 VIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELKAINPKVNITFHtYDVTVPvAESKKLLKKIFDQLKTVDI 87
Cdd:PRK07775  13 ALVAGASSGIGAATAIELAAAGFPVALGARRVEKCEELVDKIRADGGEAVAFP-LDVTDP-DSVKSFVAQAEEALGEIEV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        88 LINGAGIL--------DDHQIERTIAINFTGLVNTTTAIL-DFWDKRKGgpggiiaNICSVTGFNAIHQVP---VYSASK 155
Cdd:PRK07775  91 LVSGAGDTyfgklheiSTEQFESQVQIHLVGANRLATAVLpGMIERRRG-------DLIFVGSDVALRQRPhmgAYGAAK 163

                        170       180       190
                 ....*....|....*....|....*....|.
1B16_A       156 AAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK07775 164 AGLEAMVTNLQMELEGTGVRASIVHPGPTLT 194
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
 13-181 1.04e-04

rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has bifunctional proteins with an N-terminal aldolase and a C-terminal classical SDR domain. One member is identified as a rhamnulose-1-phosphate aldolase/alcohol dehydrogenase. The SDR domain has a canonical SDR glycine-rich NAD(P) binding motif and a match to the characteristic active site triad. However, it lacks an upstream active site Asn typical of SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 42.38  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       13 ALGGIGLDTSRELVKRNlKNFVILDRVENPTALAELKAINPKVNITFhTYDVTvPVAESKKLLKKIFDQLKTVDILINGA 92
Cdd:cd08943   9 GASGIGLAIAKRLAAEG-AAVVVADIDPEIAEKVAEAAQGGPRALGV-QCDVT-SEAQVQSAFEQAVLEFGGLDIVVSNA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       93 GILDDHQIE--------RTIAINFTGlvNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPVYSASKAAVVSFTNS 164
Cdd:cd08943  86 GIATSSPIAetsledwnRSMDINLTG--HFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLARC 163

                       170
                ....*....|....*..
1B16_A      165 LAKLAPITGVTAYSINP 181
Cdd:cd08943 164 LALEGGEDGIRVNTVNP 180
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
6-166 1.31e-04

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 41.98  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         6 KNVIFVAALGGIGLDTSRELVKRNlKNFVILDRVENP--TALAELKaiNPKvnITFHTYDVTvPVAESKKLLKKIFDQLK 83
Cdd:PRK06924   2 RYVIITGTSQGLGEAIANQLLEKG-THVISISRTENKelTKLAEQY--NSN--LTFHSLDLQ-DVHELETNFNEILSSIQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        84 TVDI----LINGAGILD---------DHQIERTIAINFTG---LVNTTTAILDFWDKRKggpggIIANICSVTGFNAIHQ 147
Cdd:PRK06924  76 EDNVssihLINNAGMVApikpiekaeSEELITNVHLNLLApmiLTSTFMKHTKDWKVDK-----RVINISSGAAKNPYFG 150

                        170
                 ....*....|....*....
1B16_A       148 VPVYSASKAAVVSFTNSLA 166
Cdd:PRK06924 151 WSAYCSSKAGLDMFTQTVA 169
PRK07102 PRK07102
SDR family oxidoreductase;
102-236 1.34e-04

SDR family oxidoreductase;


Pssm-ID: 180838 [Multi-domain]  Cd Length: 243  Bit Score: 42.22  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       102 RTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFNAIHQVPVYSASKAAVVSFTNSL-AKLAPiTGVTAYSIN 180
Cdd:PRK07102 102 REFRTNFEGPIALLTLLANRFEARGSG---TIVGISSVAGDRGRASNYVYGSAKAALTAFLSGLrNRLFK-SGVHVLTVK 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
1B16_A       181 PGITRTPLVHTFN--SWLDVEPrvaelllshptqtsEQCGQNFVKAIEANKNGA----IWKL 236
Cdd:PRK07102 178 PGFVRTPMTAGLKlpGPLTAQP--------------EEVAKDIFRAIEKGKDVIytpwFWRL 225
PRK06101 PRK06101
SDR family oxidoreductase;
5-188 1.49e-04

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 41.78  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         5 NKNVIFVAALGGIGLDTSRELVKRNLKnfvILDRVENPTALAELKAINPkvNITFHTYDVTvpvaeSKKLLKKIFDQLKT 84
Cdd:PRK06101   1 MTAVLITGATSGIGKQLALDYAKQGWQ---VIACGRNQSVLDELHTQSA--NIFTLAFDVT-----DHPGTKAALSQLPF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        85 V-DILINGAG--------ILDDHQIERTIAINFTGLVNTTTAILDFWDkrkggPGGIIANICSVTGFNAIHQVPVYSASK 155
Cdd:PRK06101  71 IpELWIFNAGdceymddgKVDATLMARVFNVNVLGVANCIEGIQPHLS-----CGHRVVIVGSIASELALPRAEAYGASK 145

                        170       180       190
                 ....*....|....*....|....*....|...
1B16_A       156 AAVVSFTNSLAKLAPITGVTAYSINPGITRTPL 188
Cdd:PRK06101 146 AAVAYFARTLQLDLRPKGIEVVTVFPGFVATPL 178
PRK08177 PRK08177
SDR family oxidoreductase;
6-186 2.11e-04

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 41.55  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         6 KNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELkainPKVNItfHTYDVTVPVAeSKKLLKKIFDQlkTV 85
Cdd:PRK08177   2 RTALIIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQAL----PGVHI--EKLDMNDPAS-LDQLLQRLQGQ--RF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        86 DILINGAGILD-DHQIERTIAINFTGLVNTTTAILD------FWDKRKGGPGgIIANICSVTG---FNAIHQVPVYSASK 155
Cdd:PRK08177  73 DLLFVNAGISGpAHQSAADATAAEIGQLFLTNAIAPirlarrLLGQVRPGQG-VLAFMSSQLGsveLPDGGEMPLYKASK 151

                        170       180       190
                 ....*....|....*....|....*....|.
1B16_A       156 AAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:PRK08177 152 AALNSMTRSFVAELGEPTLTVLSMHPGWVKT 182
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
 73-184 2.25e-04

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 41.49  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       73 KLLKKIFDQLKTVDILINGAGILDDHQIERTIAINFTGL--VNTTTA---ILDFWDKRKGGPGGIIANICS--VTGFNAI 145
Cdd:cd05357  67 DLVAAAFRAFGRCDVLVNNASAFYPTPLGQGSEDAWAELfgINLKAPyllIQAFARRLAGSRNGSIINIIDamTDRPLTG 146

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1B16_A      146 HqvPVYSASKAAVVSFTNSLA-KLAPITGVTAysINPGIT 184
Cdd:cd05357 147 Y--FAYCMSKAALEGLTRSAAlELAPNIRVNG--IAPGLI 182
PKS_KR smart00822
This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step ...
 13-97 3.61e-04

This enzymatic domain is part of bacterial polyketide synthases; It catalyses the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 214833 [Multi-domain]  Cd Length: 180  Bit Score: 40.16  E-value: 3.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A          13 ALGGIGLDTSRELVKRNLKNFVILDRVENPTA-----LAELKAINPKVniTFHTYDVTVPVAeSKKLLKKIFDQLKTVDI 87
Cdd:smart00822   8 GLGGLGRALARWLAERGARRLVLLSRSGPDAPgaaalLAELEAAGARV--TVVACDVADRDA-LAAVLAAIPAVEGPLTG 84

                           90
                   ....*....|
1B16_A          88 LINGAGILDD 97
Cdd:smart00822  85 VIHAAGVLDD 94
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
 74-182 3.99e-04

RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is an SDR-family beta-ketoacyl reductase involved in Rhamnolipid biosynthesis. RhlG is similar to but distinct from the FabG family of beta-ketoacyl-acyl carrier protein (ACP) of type II fatty acid synthesis. RhlG and related proteins are classical SDRs, with a canonical active site tetrad and glycine-rich NAD(P)-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 40.54  E-value: 3.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       74 LLKKIFDQLKTVDILINGAGI-----LDDHQI---ERTIAINFTGLVNTTTAILDFWDKRK--GGPGGIIaNICSVTGFN 143
Cdd:cd08942  72 LVARVAERSDRLDVLVNNAGAtwgapLEAFPEsgwDKVMDINVKSVFFLTQALLPLLRAAAtaENPARVI-NIGSIAGIV 150

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
1B16_A      144 AI-HQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPG 182
Cdd:cd08942 151 VSgLENYSYGASKAAVHQLTRKLAKELAGEHITVNAIAPG 190
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
 63-182 6.32e-04

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 40.02  E-value: 6.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        63 DVTVPvAESKKLLKKIFDQLKTVDILINGAGILDDHQI--------ERTIAINFTGLVNTTTAILDFWDKRkgGPGGIIA 134
Cdd:PRK12384  61 DATSE-QSVLALSRGVDEIFGRVDLLVYNAGIAKAAFItdfqlgdfDRSLQVNLVGYFLCAREFSRLMIRD--GIQGRII 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
1B16_A       135 NICSVTGFNAIHQVPVYSASKAAVVSFTNSLA-KLAPiTGVTAYSINPG 182
Cdd:PRK12384 138 QINSKSGKVGSKHNSGYSAAKFGGVGLTQSLAlDLAE-YGITVHSLMLG 185
PRK06523 PRK06523
short chain dehydrogenase; Provisional
 56-187 6.95e-04

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 39.89  E-value: 6.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        56 NITFHTYDVTVPvAESKKLLKKIFDQLKTVDILINGAG----------ILDDHQIERTIAINFTGLVNTTTAILDfwDKR 125
Cdd:PRK06523  50 GVEFVAADLTTA-EGCAAVARAVLERLGGVDILVHVLGgssapaggfaALTDEEWQDELNLNLLAAVRLDRALLP--GMI 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1B16_A       126 KGGPGGIIaNICSVTgfnaiHQVPV------YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRTP 187
Cdd:PRK06523 127 ARGSGVII-HVTSIQ-----RRLPLpesttaYAAAKAALSTYSKSLSKeVAP-KGVRVNTVSPGWIETE 188
PRK06947 PRK06947
SDR family oxidoreductase;
78-186 7.24e-04

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 39.79  E-value: 7.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        78 IFDQLKT----VDILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTG-FN 143
Cdd:PRK06947  70 MFDAVQSafgrLDALVNNAGIvapsmpladMDAARLRRMFDTNVLGAYLCAREAARRLSTDRGGRGGAIVNVSSIASrLG 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
1B16_A       144 AIHQVPVYSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRT 186
Cdd:PRK06947 150 SPNEYVDYAGSKGAVDTLTLGLAKeLGP-HGVRVNAVRPGLIET 192
PLN02780 PLN02780
ketoreductase/ oxidoreductase
 16-165 9.34e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 39.85  E-value: 9.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        16 GIGLDTSRELVKRNLkNFVILDRveNPTALAEL-KAINPK---VNITFHTYDVTVPVAESKKLLKKIFDQLKtVDILING 91
Cdd:PLN02780  64 GIGKGFAFQLARKGL-NLVLVAR--NPDKLKDVsDSIQSKyskTQIKTVVVDFSGDIDEGVKRIKETIEGLD-VGVLINN 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        92 AGI----------LDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANIcsvtGFNAIHQVP------VYSASK 155
Cdd:PLN02780 140 VGVsypyarffheVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGA---IINI----GSGAAIVIPsdplyaVYAATK 212

                        170
                 ....*....|
1B16_A       156 AAVVSFTNSL 165
Cdd:PLN02780 213 AYIDQFSRCL 222
PRK08628 PRK08628
SDR family oxidoreductase;
1-197 1.05e-03

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 39.56  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         1 MDL--TNKNVIFVAALGGIGLDTSRELVKRNLKNfVILDRVENPTALA-ELKAINPKVniTFHTYDVTVPvAESKKLLKK 77
Cdd:PRK08628   1 MDLnlKDKVVIVTGGASGIGAAISLRLAEEGAIP-VIFGRSAPDDEFAeELRALQPRA--EFVQVDLTDD-AQCRDAVEQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        78 IFDQLKTVDILINGAGILDD-------HQIERTIAINFTGLVNTTTAILDFWDKRKGGpggiIANICSVTGFNAIHQVPV 150
Cdd:PRK08628  77 TVAKFGRIDGLVNNAGVNDGvgleagrEAFVASLERNLIHYYVMAHYCLPHLKASRGA----IVNISSKTALTGQGGTSG 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
1B16_A       151 YSASKAAVVSFTNSLA-KLAPiTGVTAYSINPGITRTPLvhtFNSWLD 197
Cdd:PRK08628 153 YAAAKGAQLALTREWAvALAK-DGVRVNAVIPAEVMTPL---YENWIA 196
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
 5-188 1.33e-03

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 39.26  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        5 NKNVIFVAAlGGIGLdtSRELVKRnlknFV-------ILDRveNPTALAELKAINpKVNITFHTYDVTVpVAESKKLLKK 77
Cdd:cd05348   3 KGEVALITG-GGSGL--GRALVER----FVaegakvaVLDR--SAEKVAELRADF-GDAVVGVEGDVRS-LADNERAVAR 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       78 IFDQLKTVDILINGAGILD-------------DHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANIcSVTGFNA 144
Cdd:cd05348  72 CVERFGKLDCFIGNAGIWDystslvdipeeklDEAFDELFHINVKGYILGAKAALPALYATEGS---VIFTV-SNAGFYP 147

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1B16_A      145 IHQVPVYSASKAAVVSFTNSLA-KLAPITGVTAysINPGITRTPL 188
Cdd:cd05348 148 GGGGPLYTASKHAVVGLVKQLAyELAPHIRVNG--VAPGGMVTDL 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
 72-186 2.38e-03

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 38.21  E-value: 2.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       72 KKLLKKIFDQLKTVDILINGAGI-----------LDDHQIERTIA-INFT--GLVNTTTAILDFWDKRKGGPggiIANIC 137
Cdd:cd05349  63 QAMIEEAKNHFGPVDTIVNNALIdfpfdpdqrktFDTIDWEDYQQqLEGAvkGALNLLQAVLPDFKERGSGR---VINIG 139

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1B16_A      138 SvtgfnAIHQVPV-----YSASKAAVVSFTNSLAK-LAPiTGVTAYSINPGITRT 186
Cdd:cd05349 140 T-----NLFQNPVvpyhdYTTAKAALLGFTRNMAKeLGP-YGITVNMVSGGLLKV 188
PRK09291 PRK09291
SDR family oxidoreductase;
85-202 2.85e-03

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 38.06  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        85 VDILINGAGI-----LDDHQIE---RTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPVYSASKA 156
Cdd:PRK09291  74 VDVLLNNAGIgeagaVVDIPVElvrELFETNVFGPLELTQGFVRKMVARGKGK---VVFTSSMAGLITGPFTGAYCASKH 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
1B16_A       157 AVVSFTNSL-AKLAPItGVTAYSINPGITRT----PLVHTFNSWLDVEPRV 202
Cdd:PRK09291 151 ALEAIAEAMhAELKPF-GIQVATVNPGPYLTgfndTMAETPKRWYDPARNF 200
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
 8-183 4.03e-03

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 37.81  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A         8 VIFV-AALGGIGLDTSRELVKRNLKNFVILDRVENptaLAELKAinpKVNITFHTYDVTV-PVAESKKLLKKIFDQLKTV 85
Cdd:PRK10538   2 IVLVtGATAGFGECITRRFIQQGHKVIATGRRQER---LQELKD---ELGDNLYIAQLDVrNRAAIEEMLASLPAEWRNI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        86 DILINGAGI-----------LDDHqiERTIAINFTGLVNTTTAILDFWDKRKGGPggiIANICSVTGFNAIHQVPVYSAS 154
Cdd:PRK10538  76 DVLVNNAGLalglepahkasVEDW--ETMIDTNNKGLVYMTRAVLPGMVERNHGH---IINIGSTAGSWPYAGGNVYGAT 150

                        170       180
                 ....*....|....*....|....*....
1B16_A       155 KAAVVSFTNSLAKLAPITGVTAYSINPGI 183
Cdd:PRK10538 151 KAFVRQFSLNLRTDLHGTAVRVTDIEPGL 179
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
 73-186 4.43e-03

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 37.55  E-value: 4.43e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       73 KLLKKIFDQLKTVDILINGAG---------ILDDHQIERTIAINFTGLVNTTTAILDFWDKRKGGpggIIANICSVTGFN 143
Cdd:cd05365  65 AVVKATVSQFGGITILVNNAGgggpkpfdmPMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGG---AILNISSMSSEN 141

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1B16_A      144 AIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRT 186
Cdd:cd05365 142 KNVRIAAYGSSKAAVNHMTRNLAFDLGPKGIRVNAVAPGAVKT 184
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 69-182 5.86e-03

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 37.06  E-value: 5.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       69 AESKKLLKKIFDQLKTVDILINGAGILDDHQI--------ERTIAINFTG--LVNTTTAILDFwdkRKGGPGGIIaNICS 138
Cdd:cd05322  65 QSVIALSKGVDEIFKRVDLLVYSAGIAKSAKItdfelgdfDRSLQVNLVGyfLCAREFSKLMI---RDGIQGRII-QINS 140

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
1B16_A      139 VTGFNAIHQVPVYSASKAAVVSFTNSLAKLAPITGVTAYSINPG 182
Cdd:cd05322 141 KSGKVGSKHNSGYSAAKFGGVGLTQSLALDLAEHGITVNSLMLG 184
PRK07023 PRK07023
SDR family oxidoreductase;
87-186 5.96e-03

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 36.91  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        87 ILINGAGI---------LDDHQIERTIAINFTGLVNTTTAILdfwdkrKGGPGGI---IANICSVTGFNAIHQVPVYSAS 154
Cdd:PRK07023  80 LLINNAGTvepigplatLDAAAIARAVGLNVAAPLMLTAALA------QAASDAAerrILHISSGAARNAYAGWSVYCAT 153

                         90       100       110
                 ....*....|....*....|....*....|..
1B16_A       155 KAAVVSFTNSLAKLAPiTGVTAYSINPGITRT 186
Cdd:PRK07023 154 KAALDHHARAVALDAN-RALRIVSLAPGVVDT 184
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
 13-102 6.12e-03

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 37.35  E-value: 6.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       13 ALGGIGLDTSRELVKRNLKNFVILDRV-------ENPTALAELKAinPKVNITFHTYDVTVPVAeSKKLLKKIFDQLKTV 85
Cdd:cd08953 213 GAGGIGRALARALARRYGARLVLLGRSplppeeeWKAQTLAALEA--LGARVLYISADVTDAAA-VRRLLEKVRERYGAI 289

                        90
                ....*....|....*..
1B16_A       86 DILINGAGILDDHQIER 102
Cdd:cd08953 290 DGVIHAAGVLRDALLAQ 306
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 8-237 6.34e-03

Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a classical SDR, it contains a glycine-rich motif similar to the canonical motif of the SDR NAD(P)-binding site. However, the typical SDR active site residues are absent in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 36.79  E-value: 6.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A        8 VIFVAALGGIGLDTSRELVKRNlknfvildrvenptalAELkainpkVNITFHTYDVTVPVaESKKLLKKIFDQLKTVDI 87
Cdd:cd11731   1 IIVIGATGTIGLAVAQLLSAHG----------------HEV------ITAGRSSGDYQVDI-TDEASIKALFEKVGHFDA 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A       88 LINGAGI--------LDDHQIERTIAINFTGLVNTTTAILDFWdkRKGGpggiiaNICSVTGFNAIHQVP---VYSASKA 156
Cdd:cd11731  58 IVSTAGDaefaplaeLTDADFQRGLNSKLLGQINLVRHGLPYL--NDGG------SITLTSGILAQRPIPggaAAATVNG 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1B16_A      157 AVVSFTNSLAkLAPITGVTAYSINPGITRTplvhtfnSWLDVEPRVAElllsHPTQTSEQCGQNFVKAIEANKNGAIWKL 236
Cdd:cd11731 130 ALEGFVRAAA-IELPRGIRINAVSPGVVEE-------SLEAYGDFFPG----FEPVPAEDVAKAYVRSVEGAFTGQVLHV 197


                .
1B16_A      237 D 237
Cdd:cd11731 198 D 198
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH