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Conserved domains on  [gi|21450325|ref|NP_659172|]
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flavin reductase (NADPH) isoform 1 [Mus musculus]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10142826)

atypical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to human biliverdin IX beta reductase (BVR-B, aka flavin reductase) that catalyzes the NADPH-dependent reduction of a variety of flavins, such as riboflavin, FAD or FMN, biliverdins, methemoglobin, and PQQ (pyrroloquinoline quinone); atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
 5-200 9.41e-78

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


:

Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 231.75  E-value: 9.41e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPqPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPT 84
Cdd:cd05244   1 KIAIIGATGRTGSAIVREALARGHEVTALVRDPAKLPAEHE-KLKVVQGDVLDLEDVKEALEGQDAVISALGTRNDLSPT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKV---------PPRLQDVTDDHIRMHKILQESGLKYVAVMPPHIG 155
Cdd:cd05244  80 TLHSEGTRNIVSAMKAAGVKRLIVVGGAGSLDDRPKVtlvldtllfPPALRRVAEDHARMLKVLRESGLDWTAVRPPALF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21450325 156 DQPLTGAYTVT--LDGRGPSRVISKHDLGHFMLRCLTTNEYDGHTTY 200
Cdd:cd05244 160 DGGATGGYYRVelLVDAKGGSRISRADLAIFMLDELETPEHVRKRPT 206
 
Name Accession Description Interval E-value
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
 5-200 9.41e-78

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 231.75  E-value: 9.41e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPqPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPT 84
Cdd:cd05244   1 KIAIIGATGRTGSAIVREALARGHEVTALVRDPAKLPAEHE-KLKVVQGDVLDLEDVKEALEGQDAVISALGTRNDLSPT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKV---------PPRLQDVTDDHIRMHKILQESGLKYVAVMPPHIG 155
Cdd:cd05244  80 TLHSEGTRNIVSAMKAAGVKRLIVVGGAGSLDDRPKVtlvldtllfPPALRRVAEDHARMLKVLRESGLDWTAVRPPALF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21450325 156 DQPLTGAYTVT--LDGRGPSRVISKHDLGHFMLRCLTTNEYDGHTTY 200
Cdd:cd05244 160 DGGATGGYYRVelLVDAKGGSRISRADLAIFMLDELETPEHVRKRPT 206
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
5-198 8.42e-52

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 165.80  E-value: 8.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQpAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDlSPT 84
Cdd:COG2910   1 KIAVIGATGRVGSLIVREALARGHEVTALVRNPEKLPDEHPG-LTVVVGDVLDPAAVAEALAGADAVVSALGAGGG-NPT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEGTRNIVTAMKAHGVDKVVACTSAFLL-------WDPTKVPPRLQDVTDDHIRMHKILQESGLKYVAVMPPHIGDQ 157
Cdd:COG2910  79 TVLSDGARALIDAMKAAGVKRLIVVGGAGSLdvapglgLDTPGFPAALKPAAAAKAAAEELLRASDLDWTIVRPAALTDG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21450325 158 PLTGAYTVTLDG-RGPSRVISKHDLGHFMLRCLTTNEYDGHT 198
Cdd:COG2910 159 ERTGRYRLGGDGlLVDASSISRADVAVALLDELEDPAHIRQR 200
NAD_binding_10 pfam13460
NAD(P)H-binding;
10-191 1.52e-40

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 136.20  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    10 GATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQP-AHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSpttvms 88
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLADLEDHPgVEVVDGDVLDPDDLAEALAGQDAVISALGGGGTDE------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    89 EGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKVPPR-----LQDVTDDHIRMHKILQESGLKYVAVMPPHIGDQPLTGAY 163
Cdd:pfam13460  75 TGAKNIIDAAKAAGVKRFVLVSSLGVGDEVPGPFGPwnkemLGPYLAAKRAAEELLRASGLDYTIVRPGWLTDGPTTGYR 154

                         170       180
                  ....*....|....*....|....*...
gi 21450325   164 TVTLDGRGPSRVISKHDLGHFMLRCLTT 191
Cdd:pfam13460 155 VTGKGEPFKGGSISRADVADVLVALLDD 182
PRK05865 PRK05865
sugar epimerase family protein;
5-149 3.71e-09

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 55.82  E-value: 3.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRdssRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPT 84
Cdd:PRK05865   2 RIAVTGASGVLGRGLTARLLSQGHEVVGIAR---HRPDSWPSSADFIAADIRDATAVESAMTGADVVAHCAWVRGRNDHI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450325   85 TVmsEGTRNIVTAMKAHGVDKVVACTSafllwdPTKVpprlqdvtddhiRMHKILQESGLKYVAV 149
Cdd:PRK05865  79 NI--DGTANVLKAMAETGTGRIVFTSS------GHQP------------RVEQMLADCGLEWVAV 123
 
Name Accession Description Interval E-value
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
 5-200 9.41e-78

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 231.75  E-value: 9.41e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPqPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPT 84
Cdd:cd05244   1 KIAIIGATGRTGSAIVREALARGHEVTALVRDPAKLPAEHE-KLKVVQGDVLDLEDVKEALEGQDAVISALGTRNDLSPT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKV---------PPRLQDVTDDHIRMHKILQESGLKYVAVMPPHIG 155
Cdd:cd05244  80 TLHSEGTRNIVSAMKAAGVKRLIVVGGAGSLDDRPKVtlvldtllfPPALRRVAEDHARMLKVLRESGLDWTAVRPPALF 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21450325 156 DQPLTGAYTVT--LDGRGPSRVISKHDLGHFMLRCLTTNEYDGHTTY 200
Cdd:cd05244 160 DGGATGGYYRVelLVDAKGGSRISRADLAIFMLDELETPEHVRKRPT 206
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
5-198 8.42e-52

Putative NADH-flavin reductase [General function prediction only];


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 165.80  E-value: 8.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQpAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDlSPT 84
Cdd:COG2910   1 KIAVIGATGRVGSLIVREALARGHEVTALVRNPEKLPDEHPG-LTVVVGDVLDPAAVAEALAGADAVVSALGAGGG-NPT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEGTRNIVTAMKAHGVDKVVACTSAFLL-------WDPTKVPPRLQDVTDDHIRMHKILQESGLKYVAVMPPHIGDQ 157
Cdd:COG2910  79 TVLSDGARALIDAMKAAGVKRLIVVGGAGSLdvapglgLDTPGFPAALKPAAAAKAAAEELLRASDLDWTIVRPAALTDG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21450325 158 PLTGAYTVTLDG-RGPSRVISKHDLGHFMLRCLTTNEYDGHT 198
Cdd:COG2910 159 ERTGRYRLGGDGlLVDASSISRADVAVALLDELEDPAHIRQR 200
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
 6-201 3.30e-47

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. 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.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 152.94  E-value: 3.30e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   6 IAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDL-SPT 84
Cdd:cd05226   1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRLSKEDQEPVAVVEGDLRDLDSLSDAVQGVDVVIHLAGAPRDTrDFC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEGTRNIVTAMKAHGVDKVVACTSAFLLWD--PTKVPPRLQDVTDDHIRMHKILQESGLKYVAVMPPHIGDqpltga 162
Cdd:cd05226  81 EVDVEGTRNVLEAAKEAGVKHFIFISSLGAYGDlhEETEPSPSSPYLAVKAKTEAVLREASLPYTIVRPGVIYG------ 154

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21450325 163 ytvtldgrgpsrviskhDLGHFMLRCLTTNEYDGHTTYP 201
Cdd:cd05226 155 -----------------DLARAIANAVVTPGKKNETFNA 176
NAD_binding_10 pfam13460
NAD(P)H-binding;
10-191 1.52e-40

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 136.20  E-value: 1.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    10 GATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQP-AHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSpttvms 88
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLADLEDHPgVEVVDGDVLDPDDLAEALAGQDAVISALGGGGTDE------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    89 EGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKVPPR-----LQDVTDDHIRMHKILQESGLKYVAVMPPHIGDQPLTGAY 163
Cdd:pfam13460  75 TGAKNIIDAAKAAGVKRFVLVSSLGVGDEVPGPFGPwnkemLGPYLAAKRAAEELLRASGLDYTIVRPGWLTDGPTTGYR 154

                         170       180
                  ....*....|....*....|....*...
gi 21450325   164 TVTLDGRGPSRVISKHDLGHFMLRCLTT 191
Cdd:pfam13460 155 VTGKGEPFKGGSISRADVADVLVALLDD 182
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
 5-198 1.56e-27

Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General function prediction only];


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 103.39  E-value: 1.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPt 84
Cdd:COG0702   1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAGVEVVQGDLDDPESLAAALAGVDAVFLLVPSGPGGDF- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEGTRNIVTAMKAHGVDKVVaCTSAFLLWDPTKVPPrlqdvTDDHIRMHKILQESGLKYVAVMP-------PHIGDQ 157
Cdd:COG0702  80 AVDVEGARNLADAAKAAGVKRIV-YLSALGADRDSPSPY-----LRAKAAVEEALRASGLPYTILRPgwfmgnlLGFFER 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 21450325 158 PLTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTNEYDGHT 198
Cdd:COG0702 154 LRERGVLPLPAGDGRVQPIAVRDVAEAAAAALTDPGHAGRT 194
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
 5-193 1.71e-23

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 92.68  E-value: 1.71e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGN--DLS 82
Cdd:cd05243   1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAAGAEVVVGDLTDAESLAAALEGIDAVISAAGSGGkgGPR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  83 PTTVMSEGTRNIVTAMKAHGVDKVV----ACTSAFLLWDPTKVP-PRLQDVTDDHirmhkiLQESGLKYVAVMPPHIGDQ 157
Cdd:cd05243  81 TEAVDYDGNINLIDAAKKAGVKRFVlvssIGADKPSHPLEALGPyLDAKRKAEDY------LRASGLDYTIVRPGGLTDD 154

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21450325 158 P-LTGAYTVTLDGRGPSRVISKHDLGHFMLRCLTTNE 193
Cdd:cd05243 155 PaGTGRVVLGGDGTRLDGPISRADVAEVLAEALDTPA 191
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
5-112 1.10e-15

Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 73.47  E-value: 1.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPS-EGPQPAHVVVGDVRQAADVDKTVAGQEAVIVL---LGTGND 80
Cdd:COG0451   1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANlAALPGVEFVRGDLRDPEALAAALAGVDAVVHLaapAGVGEE 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21450325  81 lSPTTVMS---EGTRNIVTAMKAHGVDKVVACTSA 112
Cdd:COG0451  81 -DPDETLEvnvEGTLNLLEAARAAGVKRFVYASSS 114
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
 6-151 3.15e-12

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 63.83  E-value: 3.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   6 IAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAviVLLGTGNDLSPtt 85
Cdd:cd05269   1 ILVTGATGKLGTAVVELLLAKVASVVALVRNPEKAKAFAADGVEVRQGDYDDPETLERAFEGVDR--LLLISPSDLED-- 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450325  86 vMSEGTRNIVTAMKAHGVDKVVAcTSAFLLWDPTKVPprlqdVTDDHIRMHKILQESGLKYVAVMP 151
Cdd:cd05269  77 -RIQQHKNFIDAAKQAGVKHIVY-LSASGADEDSPFL-----LARDHGATEKYLEASGIPYTILRP 135
SDR_a6 cd05267
atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only ...
 4-152 3.59e-12

atypical (a) SDRs, subgroup 6; These atypical SDR family members of unknown function have only a partial match to a prototypical glycine-rich NAD(P)-binding motif consensus, GXXG, which conserves part of the motif of extended SDR. Furthermore, they lack the characteristic active site residues of the SDRs. This subgroup is related to phenylcoumaran benzylic ether reductase, an NADPH-dependent aromatic alcohol reductase. One member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187577 [Multi-domain]  Cd Length: 203  Bit Score: 62.76  E-value: 3.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   4 KKIAIFGATGRTG--LTTLAQAvQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGtGNDL 81
Cdd:cd05267   1 KKVLILGANGEIAreATTMLLE-NSNVELTLFLRNAHRLLHLKSARVTVVEGDALNSDDLKAAMRGQDVVYANLG-GTDL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  82 spttvmSEGTRNIVTAMKAHGVDKVVACTSA---------FLLWDP----TKVPPrlqdvtddHIRMHKILQESGLKYVA 148
Cdd:cd05267  79 ------DQQAENVVQAMKAVGVKRLIWTTSLgiydevpgkFGEWNKefigNYLAP--------YRKSAAVIENSDLDYTL 144


                ....
gi 21450325 149 VMPP 152
Cdd:cd05267 145 LRPA 148
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
 10-113 1.09e-11

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 62.69  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  10 GATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSP------ 83
Cdd:cd05228   5 GATGFLGSNLVRALLAQGYRVRALVRSGSDAVLLDGLPVEVVEGDLTDAASLAAAMKGCDRVFHLAAFTSLWAKdrkely 84

                        90       100       110
                ....*....|....*....|....*....|.
gi 21450325  84 -TTVmsEGTRNIVTAMKAHGVDKVVAcTSAF 113
Cdd:cd05228  85 rTNV--EGTRNVLDAALEAGVRRVVH-TSSI 112
NmrA_TMR_like_1_SDR_a cd05231
NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, ...
 6-200 2.49e-11

NmrA (a transcriptional regulator) and triphenylmethane reductase (TMR) like proteins, subgroup 1, atypical (a) SDRs; Atypical SDRs related to NMRa, TMR, and HSCARG (an NADPH sensor). This subgroup resembles the SDRs and has a partially conserved characteristic [ST]GXXGXXG NAD-binding motif, but lacks the conserved active site residues. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187542 [Multi-domain]  Cd Length: 259  Bit Score: 61.19  E-value: 2.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   6 IAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVL--LGTGNDLSP 83
Cdd:cd05231   1 ILVTGATGRIGSKVATTLLEAGRPVRALVRSDERAAALAARGAEVVVGDLDDPAVLAAALAGVDAVFFLapPAPTADARP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  84 TTVmsEGTRNIVTAMKAHGVDKVVACTSafllwdptkVPPRLQDVTdDHIRMHKILQE----SGLKYVAVMPPHIGDQPL 159
Cdd:cd05231  81 GYV--QAAEAFASALREAGVKRVVNLSS---------VGADPESPS-GLIRGHWLMEQvlnwAGLPVVHLRPAWFMENLL 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 21450325 160 TGAYTVTLDGR------GPSRV--ISKHDLGHFMLRCLTTNEYDGHTTY 200
Cdd:cd05231 149 SQAPSIRKAGVlalpfpGDGRLppIATDDIARVAAKLLLDPEWHGHRVY 197
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
 6-154 6.32e-10

NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 56.92  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325     6 IAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQ--EAVIVLLGTGND--- 80
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFVEGDLTDRDALEKLLADVrpDAVIHLAAVGGVgas 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    81 -LSPTTVMS---EGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKVPPRLQDVTDD----------HIRMHKILQ----ES 142
Cdd:pfam01370  81 iEDPEDFIEanvLGTLNLLEAARKAGVKRFLFASSSEVYGDGAEIPQEETTLTGPlapnspyaaaKLAGEWLVLayaaAY 160

                         170
                  ....*....|..
gi 21450325   143 GLKYVAVMPPHI 154
Cdd:pfam01370 161 GLRAVILRLFNV 172
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
 5-149 8.86e-10

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 56.93  E-value: 8.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTL-AQAVQAGYEVTVLVRDSSRLPSE-GPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGndls 82
Cdd:cd05259   1 KIAIAGATGTLGGPIVsALLASPGFTVTVLTRPSSTSSNEfQPSGVKVVPVDYASHESLVAALKGVDAVISALGGA---- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21450325  83 pttvMSEGTRNIVTAMKAHGVDKvvactsaFLLW----DPTKVPPR-LQDVTDDHIRMHKILQES--GLKYVAV 149
Cdd:cd05259  77 ----AIGDQLKLIDAAIAAGVKR-------FIPSefgvDYDRIGALpLLDLFDEKRDVRRYLRAKnaGLPWTYV 139
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
 4-107 3.13e-09

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 55.33  E-value: 3.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   4 KKIAIFGATGRTGLTTLAQAVQAGYEVTVLVRD---SSRLPSEGPQPAHVVV-GDVRQAADVDKTVAGQEAVIVLLG--- 76
Cdd:cd05271   1 MVVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCeayARRLLVMGDLGQVLFVeFDLRDDESIRKALEGSDVVINLVGrly 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 21450325  77 -TGNDlSPTTVMSEGTRNIVTAMKAHGVDKVV 107
Cdd:cd05271  81 eTKNF-SFEDVHVEGPERLAKAAKEAGVERLI 111
PRK05865 PRK05865
sugar epimerase family protein;
5-149 3.71e-09

sugar epimerase family protein;


Pssm-ID: 235630 [Multi-domain]  Cd Length: 854  Bit Score: 55.82  E-value: 3.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRdssRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPT 84
Cdd:PRK05865   2 RIAVTGASGVLGRGLTARLLSQGHEVVGIAR---HRPDSWPSSADFIAADIRDATAVESAMTGADVVAHCAWVRGRNDHI 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450325   85 TVmsEGTRNIVTAMKAHGVDKVVACTSafllwdPTKVpprlqdvtddhiRMHKILQESGLKYVAV 149
Cdd:PRK05865  79 NI--DGTANVLKAMAETGTGRIVFTSS------GHQP------------RVEQMLADCGLEWVAV 123
PLN00141 PLN00141
Tic62-NAD(P)-related group II protein; Provisional
 2-161 1.54e-08

Tic62-NAD(P)-related group II protein; Provisional


Pssm-ID: 215072 [Multi-domain]  Cd Length: 251  Bit Score: 52.94  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    2 TVKKIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQ-PA-HVVVGDVRQAADVDKTVAGQEAVIVLLGTG- 78
Cdd:PLN00141  16 KTKTVFVAGATGRTGKRIVEQLLAKGFAVKAGVRDVDKAKTSLPQdPSlQIVRADVTEGSDKLVEAIGDDSDAVICATGf 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   79 ----NDLSPTTVMSEGTRNIVTAMKAHGVDKVVACTSAFL-------LWDPTKVPPRLQDVT-DDHIRMHKILQESGLKY 146
Cdd:PLN00141  96 rrsfDPFAPWKVDNFGTVNLVEACRKAGVTRFILVSSILVngaamgqILNPAYIFLNLFGLTlVAKLQAEKYIRKSGINY 175

                        170
                 ....*....|....*
gi 21450325  147 VAVMPPHIGDQPLTG 161
Cdd:PLN00141 176 TIVRPGGLTNDPPTG 190
NmrA_TMR_like_SDR_a cd08947
NmrA (a transcriptional regulator), HSCARG (an NADPH sensor), and triphenylmethane reductase ...
 6-198 3.04e-08

NmrA (a transcriptional regulator), HSCARG (an NADPH sensor), and triphenylmethane reductase (TMR) like proteins, atypical (a) SDRs; Atypical SDRs belonging to this subgroup include NmrA, HSCARG, and TMR, these proteins bind NAD(P) but they lack the usual catalytic residues of the SDRs. Atypical SDRs are distinct from classical SDRs. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. TMR, an NADP-binding protein, lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187651 [Multi-domain]  Cd Length: 224  Bit Score: 51.78  E-value: 3.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   6 IAIFGATGRTGLTTLAQAVQAG-YEVTVLVRDSSRLPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDLSPT 84
Cdd:cd08947   1 IAVTGATGQQGGSVIRHLLAKGaSQVRAVVRNVEKAATLADQGVEVRQGDYNQPELLQKAFAGASKLFIITGPHYDNTLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  85 TVMSEgtrNIVTAMKAHGVDKVVACTSAFLLWDptkVPPRLqdvtDDHIRMHKILQESGLKYVAVMPP--------HIGD 156
Cdd:cd08947  81 IKQGK---NVADAARRAGVKHIYSTGYAFAEES---AIPLA----HVKLAVEYAIRTTGIPYTFLRNGlytenfvsEGLP 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21450325 157 QPLTGAYTVTLD-GRGPSRVISKHDLGHFMLRCLTTNEYDGHT 198
Cdd:cd08947 151 AADTGSGAIVLPaGDGPVPSVTRNDLGPAAAQLLKEEGHEGKT 193
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
 6-130 1.95e-06

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 46.98  E-value: 1.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   6 IAIFGATGRTGlTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVR--QAADVdKTVAGQEAVIVLlgtGNDLSP 83
Cdd:cd05240   1 ILVTGAAGGLG-RLLARRLAASPRVIGVDGLDRRRPPGSPPKVEYVRLDIRdpAAADV-FREREADAVVHL---AFILDP 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450325  84 TTVMSE-------GTRNIVTAMKAHGVDKVVACTSA------------FLLWDPTKVPPRLQDVTD 130
Cdd:cd05240  76 PRDGAErhrinvdGTQNVLDACAAAGVPRVVVTSSVavygahpdnpapLTEDAPLRGSPEFAYSRD 141
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 4-108 3.48e-06

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 46.21  E-value: 3.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   4 KKIAIFGAtGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVR-----QAADVDKTvagqEAVIVLlgTG 78
Cdd:COG0569  96 MHVIIIGA-GRVGRSLARELEEEGHDVVVIDKDPERVERLAEEDVLVIVGDATdeevlEEAGIEDA----DAVIAA--TG 168

                        90       100       110
                ....*....|....*....|....*....|..
gi 21450325  79 NDlspttvmsegTRNIVTAM--KAHGVDKVVA 108
Cdd:COG0569 169 DD----------EANILACLlaKELGVPRIIA 190
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
 6-107 5.73e-06

NmrA-like family; NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 45.41  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325     6 IAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLPSEGPQ--PAHVVVGDVRQAADVDKTVAGQEAVIVLlgTGNDLSp 83
Cdd:pfam05368   1 ILVFGATGQQGGSVVRASLKAGHKVRALVRDPKSELAKSLKeaGVELVKGDLDDKESLVEALKGVDVVFSV--TGFWAG- 77

                          90       100
                  ....*....|....*....|....
gi 21450325    84 ttVMSEGTRNIVTAMKAHGVDKVV 107
Cdd:pfam05368  78 --KEIEDGKKLADAAKEAGVKHFI 99
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
5-112 1.53e-05

NAD dependent epimerase/dehydratase family enzyme [General function prediction only];


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 44.29  E-value: 1.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGlTTLAQA-VQAGYEVTVLVRDssrlPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTG-NDLS 82
Cdd:COG1090   1 KILITGGTGFIG-SALVAAlLARGHEVVVLTRR----PPKAPDEVTYVAWDPETGGIDAAALEGADAVINLAGASiADKR 75

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 21450325  83 PT-----TVMS---EGTRNIVTAMKAHGVD-KVVACTSA 112
Cdd:COG1090  76 WTearkqEILDsrvDSTRLLVEAIAAAANPpKVLISASA 114
PLN00016 PLN00016
RNA-binding protein; Provisional
 4-154 5.58e-05

RNA-binding protein; Provisional


Pssm-ID: 215029 [Multi-domain]  Cd Length: 378  Bit Score: 43.15  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325    4 KKIAI----FGATGRTGLTTLAQAVQAGYEVTVLVR---DSSRLPSEGPQ--------PAHVVVGDvrqAADVDKTVAGQ 68
Cdd:PLN00016  53 KKVLIvntnSGGHAFIGFYLAKELVKAGHEVTLFTRgkePSQKMKKEPFSrfselssaGVKTVWGD---PADVKSKVAGA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   69 EAVIVLLGTGNDLSPTtvmsegtRNIVTAMKAHGVDKVVACTSAFlLWDPTKVPPRLQ----DVTDDHIRMHKILQESGL 144
Cdd:PLN00016 130 GFDVVYDNNGKDLDEV-------EPVADWAKSPGLKQFLFCSSAG-VYKKSDEPPHVEgdavKPKAGHLEVEAYLQKLGV 201

                        170
                 ....*....|
gi 21450325  145 KYVAVMPPHI 154
Cdd:PLN00016 202 NWTSFRPQYI 211
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 5-122 8.31e-05

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 42.52  E-value: 8.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLvrD----SSR--LPSEGPQPAHVVVGDVRQAADVDKTVAGQ--EAVI---V 73
Cdd:cd05247   1 KVLVTGGAGYIGSHTVVELLEAGYDVVVL--DnlsnGHReaLPRIEKIRIEFYEGDIRDRAALDKVFAEHkiDAVIhfaA 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325  74 LLGTG-----------NDLSpttvmseGTRNIVTAMKAHGVDKVVACTSAFLLWDPTKVP 122
Cdd:cd05247  79 LKAVGesvqkplkyydNNVV-------GTLNLLEAMRAHGVKNFVFSSSAAVYGEPETVP 131
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
 7-112 1.10e-04

3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid dehydrogenase/5-ene-4-ene isomerase (3 beta-HSD) catalyzes the oxidation and isomerization of 5-ene-3 beta-hydroxypregnene and 5-ene-hydroxyandrostene steroid precursors into the corresponding 4-ene-ketosteroids necessary for the formation of all classes of steroid hormones.


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 41.97  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325     7 AIFGATGRTGLTTLAQAVQAG--YEVTVL-VRDSSRLPSE--GPQPAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGNDL 81
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGelKEVRVFdLRESPELLEDfsKSNVIKYIQGDVTDKDDLDNALEGVDVVIHTASAVDVF 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21450325    82 SPTT------VMSEGTRNIVTAMKAHGVDKVVACTSA 112
Cdd:pfam01073  81 GKYTfdeimkVNVKGTQNVLEACVKAGVRVLVYTSSA 117
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
 4-69 1.39e-04

classical (c) SDR, subgroup 4; 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: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 41.34  E-value: 1.39e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21450325   4 KKIAIFGATGRTGLTTlAQAV-QAGYEVTVLVRDSSRL----PSEGPQpAHVVVGDVRQAADVDKTVAGQE 69
Cdd:cd08929   1 KAALVTGASRGIGEAT-ARLLhAEGYRVGICARDEARLaaaaAQELEG-VLGLAGDVRDEADVRRAVDAME 69
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 4-63 2.92e-04

daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically important therapeutic compound used in some cancer treatments. Daunorubicin C-13 ketoreductase is member of the classical SDR family with a canonical glycine-rich NAD(P)-binding motif, but lacking a complete match to the active site tetrad characteristic of this group. The critical Tyr, plus the Lys and upstream Asn are present, but the catalytic Ser is replaced, generally by Gln. 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: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 40.55  E-value: 2.92e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450325   4 KKIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLP---SEGPQPAHVVVGDVRQAADVDK 63
Cdd:cd08951   8 KRIFITGSSDGLGLAAARTLLHQGHEVVLHARSQKRAAdakAACPGAAGVLIGDLSSLAETRK 70
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 6-108 3.56e-04

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 38.66  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325     6 IAIFGAtGRTGlTTLAQAVQAGYEVTVLVRDSSRLPSEGPQPAHVVVGDVR-----QAADVDktvagqEAVIVLLGTGND 80
Cdd:pfam02254   1 IIIIGY-GRVG-RSLAEELSEGGDVVVIDKDEERVEELREEGVPVVVGDATdeevlEEAGIE------EADAVIAATGDD 72

                          90       100       110
                  ....*....|....*....|....*....|.
gi 21450325    81 lspttvmsegTRNIVTAMKA---HGVDKVVA 108
Cdd:pfam02254  73 ----------EANILIVLLArelNPDKKIIA 93
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
 5-131 5.15e-04

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 40.02  E-value: 5.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVR--DSSRLPSEgpQPAHVVVGDVRQAADVDKTVAGQEAVIvLLGTGNDLS 82
Cdd:cd05262   2 KVFVTGATGFIGSAVVRELVAAGHEVVGLARsdAGAAKLEA--AGAQVHRGDLEDLDILRKAAAEADAVI-HLAFTHDFD 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21450325  83 PTTVMSEGTRNIVTAMK--AHGVDKVVACTSAFLLWDPTKVPPRLQDVTDD 131
Cdd:cd05262  79 NFAQACEVDRRAIEALGeaLRGTGKPLIYTSGIWLLGPTGGQEEDEEAPDD 129
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
 5-74 5.57e-04

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 39.98  E-value: 5.57e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450325   5 KIAIFGATGRTGlTTLAQA-VQAGYEVTVLVRDSSR-----LPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIVL 74
Cdd:cd05257   1 NVLVTGADGFIG-SHLTERlLREGHEVRALDIYNSFnswglLDNAVHDRFHFISGDVRDASEVEYLVKKCDVVFHL 75
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
 6-107 1.10e-03

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 38.87  E-value: 1.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   6 IAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRLpSEGPQPAHV--VVGDVRQAADVDKTVAGQEAVIVL---LGTGND 80
Cdd:cd05245   1 VLVTGATGYVGGRLVPRLLQEGHQVRALVRSPEKL-ADRPWSERVtvVRGDLEDPESLRAALEGIDTAYYLvhsMGSGGD 79

                        90       100
                ....*....|....*....|....*..
gi 21450325  81 LSPTTVMSegTRNIVTAMKAHGVDKVV 107
Cdd:cd05245  80 FEEADRRA--ARNFARAARAAGVKRII 104
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
 5-76 1.38e-03

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 38.75  E-value: 1.38e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450325   5 KIAIFGATGRTGlTTLAQAVQA-GYEVTVLVRDssrlPSEGPQPAHVVVGDVRQAAdvDKTVAGQEAVIVLLG 76
Cdd:cd05242   1 KIVITGGTGFIG-RALTRRLTAaGHEVVVLSRR----PGKAEGLAEVITWDGLSLG--PWELPGADAVINLAG 66
NmrA_like_SDR_a cd05251
NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) ...
 6-107 2.75e-03

NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs; NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.


Pssm-ID: 187561 [Multi-domain]  Cd Length: 242  Bit Score: 37.64  E-value: 2.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   6 IAIFGATGRTGLTTLAQAVQ-AGYEVTVLVRDSSR-----LPSEGpqpAHVVVGDVRQAADVDKTVAGQEAVIVLLGTGN 79
Cdd:cd05251   1 ILVFGATGKQGGSVVRALLKdPGFKVRALTRDPSSpaakaLAAPG---VEVVQGDLDDPESLEAALKGVYGVFLVTDFWE 77

                        90       100
                ....*....|....*....|....*...
gi 21450325  80 DLSPTTVmsEGTRNIVTAMKAHGVDKVV 107
Cdd:cd05251  78 AGGEDEI--AQGKNVVDAAKRAGVQHFV 103
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-66 2.87e-03

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 37.54  E-value: 2.87e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450325   1 MTVKKIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSRL-------PSEGPQpAHVVVGDVRQAADVDKTVA 66
Cdd:COG0300   3 LTGKTVLITGASSGIGRALARALAARGARVVLVARDAERLealaaelRAAGAR-VEVVALDVTDPDAVAALAE 74
PRK06180 PRK06180
short chain dehydrogenase; Provisional
 15-70 3.56e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 37.20  E-value: 3.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21450325   15 TGLTT-----LAQAV-QAGYEVTVLVRDSSR---LPSEGPQPAHVVVGDVRQAADVDKTVAGQEA 70
Cdd:PRK06180  10 TGVSSgfgraLAQAAlAAGHRVVGTVRSEAAradFEALHPDRALARLLDVTDFDAIDAVVADAEA 74
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
 4-66 5.37e-03

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 36.86  E-value: 5.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21450325    4 KKIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDS---SRLPSEGPQPAHVVVGDVRQAADVDKTVA 66
Cdd:PRK06200   7 QVALITGGGSGIGRALVERFLAEGARVAVLERSAeklASLRQRFGDHVLVVEGDVTSYADNQRAVD 72
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
 8-112 5.44e-03

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase 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.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 37.03  E-value: 5.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   8 IFGATGRTGLTTLAQAV-QAGYEVTVLVRDSSRLP--SEGPQPAHVVVGDVRQAADVDKTVAGQEAV-----IVLLGTGN 79
Cdd:cd05241   4 VTGGSGFFGERLVKQLLeRGGTYVRSFDIAPPGEAlsAWQHPNIEFLKGDITDRNDVEQALSGADCVfhtaaIVPLAGPR 83

                        90       100       110
                ....*....|....*....|....*....|...
gi 21450325  80 DLSpTTVMSEGTRNIVTAMKAHGVDKVVACTSA 112
Cdd:cd05241  84 DLY-WEVNVGGTQNVLDACQRCGVQKFVYTSSS 115
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
 5-103 5.57e-03

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they 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 numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, 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. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. 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.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 36.94  E-value: 5.57e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGLTTLAQAVQAGYEVTVLVRdssRLPSEGPQPAHVVVGDVRQAADVdktVAGQEAVIVLLGTGNDLSPT 84
Cdd:cd05232   1 KVLVTGANGFIGRALVDKLLSRGEEVRIAVR---NAENAEPSVVLAELPDIDSFTDL---FLGVDAVVHLAARVHVMNDQ 74

                        90       100
                ....*....|....*....|....*...
gi 21450325  85 T---------VMSEGTRNIVTAMKAHGV 103
Cdd:cd05232  75 GadplsdyrkVNTELTRRLARAAARQGV 102
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 5-73 6.74e-03

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 36.75  E-value: 6.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21450325    5 KIAIFGAtGRTGLTTLAQAVQAGYEVTVLVRDSSR---LPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVIV 73
Cdd:PRK06522   2 KIAILGA-GAIGGLFGAALAQAGHDVTLVARRGAHldaLNENGLRLEDGEITVPVLAADDPAELGPQDLVIL 72
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 5-114 7.02e-03

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 36.25  E-value: 7.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21450325   5 KIAIFGATGRTGlTTLAQAVQA--GYEVT-VLVRDSSRlpsegPQPAHVVVGDVRQAADVDKTVAGQEAVIvllgtgnDL 81
Cdd:COG0289   2 KIAVAGASGRMG-RELIRAVLEapDLELVaAIDRPGSP-----GQDAGELALGVPVTDDLEEALAKADVVI-------DF 68

                        90       100       110
                ....*....|....*....|....*....|....
gi 21450325  82 S-PTTVMSegtrNIVTAMKaHGVdKVVACTSAFL 114
Cdd:COG0289  69 ThPEATLE----NLEAALE-AGV-PVVIGTTGFS 96
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 1-66 7.68e-03

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: 36.30  E-value: 7.68e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21450325   1 MTVKKIAIFGATGRTGLTTLAQAVQAGYEVTVLVRDSSR-------LPSEGPQpAHVVVGDVRQAADVDKTVA 66
Cdd:COG1028   4 LKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEAleaaaaeLRAAGGR-ALAVAADVTDEAAVEALVA 75
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 5-72 8.00e-03

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 34.90  E-value: 8.00e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21450325     5 KIAIFGATGRTGlTTLAQAVQA--GYEVT-VLVRDSSrlPSEGPQPAHVVVGDVRQAADVDKTVAGQEAVI 72
Cdd:pfam01113   2 KIAVAGASGRMG-RELIKAVLEapDLELVaAVDRPGS--SLLGSDAGELAPLGVPVTDDLEEVLADADVLI 69
 
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.
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