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Conserved domains on  [gi|807066350|ref|NP_001293069|]
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dihydropteridine reductase isoform 2 [Homo sapiens]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10143191)

classical SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase similar to dihydropteridine reductase that converts dihydrobiopterin into tetrahydrobiopterin, a cofactor necessary in catecholamine synthesis; classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 10-201 4.03e-109

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


:

Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 311.95  E-value: 4.03e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  10 ARRVLVYGGRGALGSRCVQAFRARNW-------------------------------VTAEVGKLlgEEKVDAILCVAGG 58
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWwvasidlaeneeadasiivldsdsfteqakqVVASVARL--SGKVDALICVAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  59 WAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNS 138
Cdd:cd05334   79 WAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807066350 139 GMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVT 201
Cdd:cd05334  159 GLPAGSTANAILPVTLDTPANRKAMPDADFSSWTPLEFIAELILFWASGAARPKSGSLIPVVT 221
 
Name Accession Description Interval E-value
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 10-201 4.03e-109

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 311.95  E-value: 4.03e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  10 ARRVLVYGGRGALGSRCVQAFRARNW-------------------------------VTAEVGKLlgEEKVDAILCVAGG 58
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWwvasidlaeneeadasiivldsdsfteqakqVVASVARL--SGKVDALICVAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  59 WAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNS 138
Cdd:cd05334   79 WAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807066350 139 GMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVT 201
Cdd:cd05334  159 GLPAGSTANAILPVTLDTPANRKAMPDADFSSWTPLEFIAELILFWASGAARPKSGSLIPVVT 221
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 48-199 3.68e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 63.28  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  48 KVDAILCVAGGWAGGNAKSKSLfKNCDLMWKQSIWTSTISSHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGA 125
Cdd:PRK12828  82 RLDALVNIAGAFVWGTIADGDA-DTWDRMYGVNVKTTLNASKAALPALTAsgGGRIVNIGAGAALKAGPGMGAYAAAKAG 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807066350 126 VHQLCQSLAGKNsgMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQV 199
Cdd:PRK12828 161 VARLTEALAAEL--LDRGITVNAVLPSIIDTPPNRADMPDADFSRWVTPEQIAAVIAFLLSDEAQAITGASIPV 232
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 88-168 3.66e-06

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: 46.32  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  88 SHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPE 165
Cdd:COG1028  122 TRAALPHMRErgGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLA--LELAPRGIRVNAVAPGPIDTPMTRALLGA 199


                 ...
gi 807066350 166 ADF 168
Cdd:COG1028  200 EEV 202
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 36-134 3.66e-03

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 37.41  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350   36 VTAEVGKLLGeeKVDAILCVAGgWAGgnaKSKSLFKNCDL-MWKQSIWTSTISSHLATKH----LKEGG-LLTLAGAkAA 109
Cdd:pfam13561  61 LVAAAVEKFG--RLDILVNNAG-FAP---KLKGPFLDTSReDFDRALDVNLYSLFLLAKAalplMKEGGsIVNLSSI-GA 133

                          90       100
                  ....*....|....*....|....*
gi 807066350  110 LDGTPGMIGYGMAKGAVHQLCQSLA 134
Cdd:pfam13561 134 ERVVPNYNAYGAAKAALEALTRYLA 158
 
Name Accession Description Interval E-value
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 10-201 4.03e-109

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 311.95  E-value: 4.03e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  10 ARRVLVYGGRGALGSRCVQAFRARNW-------------------------------VTAEVGKLlgEEKVDAILCVAGG 58
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWwvasidlaeneeadasiivldsdsfteqakqVVASVARL--SGKVDALICVAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  59 WAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNS 138
Cdd:cd05334   79 WAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807066350 139 GMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVT 201
Cdd:cd05334  159 GLPAGSTANAILPVTLDTPANRKAMPDADFSSWTPLEFIAELILFWASGAARPKSGSLIPVVT 221
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 36-199 2.10e-13

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 66.54  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  36 VTAEVGKLLGEE-KVDAILCVAGGWAGGNAkSKSLFKNCDLMWKQSIWTSTISSHLATKHLKE--GGLLTLAGAKAALDG 112
Cdd:cd05233   61 VEALVEEALEEFgRLDILVNNAGIARPGPL-EELTDEDWDRVLDVNLTGVFLLTRAALPHMKKqgGGRIVNISSVAGLRP 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350 113 TPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPEADFSS---------WTPLEFLVETFHD 183
Cdd:cd05233  140 LPGQAAYAASKAALEGLTRSLA--LELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKElaaaiplgrLGTPEEVAEAVVF 217

                        170
                 ....*....|....*.
gi 807066350 184 WITGKNRPSSGSLIQV 199
Cdd:cd05233  218 LASDEASYITGQVIPV 233
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 48-199 3.68e-12

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 63.28  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  48 KVDAILCVAGGWAGGNAKSKSLfKNCDLMWKQSIWTSTISSHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGA 125
Cdd:PRK12828  82 RLDALVNIAGAFVWGTIADGDA-DTWDRMYGVNVKTTLNASKAALPALTAsgGGRIVNIGAGAALKAGPGMGAYAAAKAG 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807066350 126 VHQLCQSLAGKNsgMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQV 199
Cdd:PRK12828 161 VARLTEALAAEL--LDRGITVNAVLPSIIDTPPNRADMPDADFSRWVTPEQIAAVIAFLLSDEAQAITGASIPV 232
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 91-174 3.81e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 49.26  E-value: 3.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  91 ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGknSGMPPGAAAIAVLPVTLDTPMNRKSMPE---AD 167
Cdd:PRK06701 167 ALPHLKQGSAIINTGSITGYEGNETLIDYSATKGAIHAFTRSLAQ--SLVQKGIRVNAVAPGPIWTPLIPSDFDEekvSQ 244


                 ....*..
gi 807066350 168 FSSWTPL 174
Cdd:PRK06701 245 FGSNTPM 251
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 88-168 3.66e-06

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: 46.32  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  88 SHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPE 165
Cdd:COG1028  122 TRAALPHMRErgGGRIVNISSIAGLRGSPGQAAYAASKAAVVGLTRSLA--LELAPRGIRVNAVAPGPIDTPMTRALLGA 199


                 ...
gi 807066350 166 ADF 168
Cdd:COG1028  200 EEV 202
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
88-173 5.38e-05

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 42.93  E-value: 5.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  88 SHLATKHLKE---GGLLTLAGAkAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSgmPPGAAAIAVLPVTLDTPMNRKSMP 164
Cdd:COG0300  121 TRALLPLMRArgrGRIVNVSSV-AGLRGLPGMAAYAASKAALEGFSESLRAELA--PTGVRVTAVCPGPVDTPFTARAGA 197


                 ....*....
gi 807066350 165 EADFSSWTP 173
Cdd:COG0300  198 PAGRPLLSP 206
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 13-158 2.80e-04

Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a classical SDR which binds NADP. Members of this subgroup contain the YXXXK active site characteristic of SDRs. Also, an upstream Asn residue of the canonical catalytic tetrad is partially conserved in this subgroup of proteins of undetermined function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 40.58  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  13 VLVYGGRGALGSRCVQAFRARNW--------------VTAEVGKLL------GEEKVDAILCVAGG-----WAGGNAKSK 67
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWrlllsgrdagalagLAAEVGALArpadvaAELEVWALAQELGPldllvYAAGAILGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  68 SLFKNCDLMWKQSIWTSTISSHLATKH----LKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSgmppG 143
Cdd:cd11730   81 PLARTKPAAWRRILDANLTGAALVLKHalalLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVARKEVR----G 156

                        170
                 ....*....|....*
gi 807066350 144 AAAIAVLPVTLDTPM 158
Cdd:cd11730  157 LRLTLVRPPAVDTGL 171
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 13-158 4.95e-04

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 39.49  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  13 VLVYGGRGALGSRCVQAFRARNWVTAEVGKLLGE------------------EKVDAILCVAGGwaggnAKSKSLFkncd 74
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAHGHEVITAGRSSGDyqvditdeasikalfekvGHFDAIVSTAGD-----AEFAPLA---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  75 lMWKQSIWTSTISSHL---------ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKnsgMPPGAA 145
Cdd:cd11731   72 -ELTDADFQRGLNSKLlgqinlvrhGLPYLNDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRAAAIE---LPRGIR 147

                        170
                 ....*....|...
gi 807066350 146 AIAVLPVTLDTPM 158
Cdd:cd11731  148 INAVSPGVVEESL 160
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
82-174 7.22e-04

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 39.37  E-value: 7.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  82 WTSTIS---------SHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLA----GKNsgmppgaaa 146
Cdd:PRK05653 106 WDRVIDvnltgtfnvVRAALPPMIKarYGRIVNISSVSGVTGNPGQTNYSAAKAGVIGFTKALAlelaSRG--------- 176

                         90       100       110
                 ....*....|....*....|....*....|...
gi 807066350 147 I---AVLPVTLDTPMNRKS--MPEADFSSWTPL 174
Cdd:PRK05653 177 ItvnAVAPGFIDTDMTEGLpeEVKAEILKEIPL 209
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 91-197 8.81e-04

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 39.18  E-value: 8.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  91 ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPEAD--- 167
Cdd:cd05362  123 AAKRLRDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLA--KELGGRGITVNAVAPGPVDTDMFYAGKTEEAveg 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 807066350 168 FSSWTPLE-------------FLVETFHDWITGKNRPSSGSLI 197
Cdd:cd05362  201 YAKMSPLGrlgepediapvvaFLASPDGRWVNGQVIRANGGYV 243
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 77-167 1.69e-03

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 38.24  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  77 WKQSIWTSTISSHLATKHL------KEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNsgmppGAAAI--- 147
Cdd:cd08944  102 WDQTMAINLRGTFLCCRHAaprmiaRGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAEL-----RHAGIrcn 176

                         90       100
                 ....*....|....*....|
gi 807066350 148 AVLPVTLDTPMNRKSMPEAD 167
Cdd:cd08944  177 ALAPGLIDTPLLLAKLAGFE 196
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 77-134 2.21e-03

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). 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: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 37.75  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  77 WKQSIWTSTISSHLATKHL--KEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLA 134
Cdd:cd05373  105 WEMAAFGGFLAAREAAKRMlaRGRGTIIFTGATASLRGRAGFAAFAGAKFALRALAQSMA 164
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 36-134 3.66e-03

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 37.41  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350   36 VTAEVGKLLGeeKVDAILCVAGgWAGgnaKSKSLFKNCDL-MWKQSIWTSTISSHLATKH----LKEGG-LLTLAGAkAA 109
Cdd:pfam13561  61 LVAAAVEKFG--RLDILVNNAG-FAP---KLKGPFLDTSReDFDRALDVNLYSLFLLAKAalplMKEGGsIVNLSSI-GA 133

                          90       100
                  ....*....|....*....|....*
gi 807066350  110 LDGTPGMIGYGMAKGAVHQLCQSLA 134
Cdd:pfam13561 134 ERVVPNYNAYGAAKAALEALTRYLA 158
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 77-171 3.82e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 37.22  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  77 WKQSIWTSTISSHLATKH-----LKEGG-----LLTLAGAKAALdgtPGMIGYGMAKGAVHQLCQSLAGKNSgmPPGAAA 146
Cdd:PRK07478 108 WRETLATNLTSAFLGAKHqipamLARGGgslifTSTFVGHTAGF---PGMAAYAASKAGLIGLTQVLAAEYG--AQGIRV 182

                         90       100
                 ....*....|....*....|....*
gi 807066350 147 IAVLPVTLDTPMNRKSMPEADFSSW 171
Cdd:PRK07478 183 NALLPGGTDTPMGRAMGDTPEALAF 207
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 74-182 3.99e-03

human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup includes human DHRS1 and human HSDL2 and related proteins. These are members of the classical SDR family, with a canonical Gly-rich NAD-binding motif and the typical YXXXK active site motif. However, the rest of the catalytic tetrad is not strongly conserved. DHRS1 mRNA has been detected in many tissues, liver, heart, skeletal muscle, kidney and pancreas; a longer transcript is predominantly expressed in the liver , a shorter one in the heart. HSDL2 may play a part in fatty acid metabolism, as it is found in peroxisomes. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 37.37  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  74 DLMWKQSIWTSTISSHLATKHLK--EGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMppGAAAIAVLP 151
Cdd:cd05338  117 DLMQRVNLRGTYLLSQAALPHMVkaGQGHILNISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRH--GIAVNSLWP 194

                         90       100       110
                 ....*....|....*....|....*....|..
gi 807066350 152 VTL-DTPMNRKSMPEADFSSWTPLEFLVETFH 182
Cdd:cd05338  195 STAiETPAATELSGGSDPARARSPEILSDAVL 226
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 91-175 6.24e-03

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 36.50  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350  91 ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPE---AD 167
Cdd:cd05355  148 ALPHLKKGSSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLS--LQLAEKGIRVNAVAPGPIWTPLIPSSFPEekvSE 225


                 ....*...
gi 807066350 168 FSSWTPLE 175
Cdd:cd05355  226 FGSQVPMG 233
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 77-161 7.53e-03

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 36.05  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807066350   77 WKQSI---WTSTIS-SHLATKHLKEG--GLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVL 150
Cdd:pfam00106 101 WERVIdvnLTGVFNlTRAVLPAMIKGsgGRIVNISSVAGLVPYPGGSAYSASKAAVIGFTRSLA--LELAPHGIRVNAVA 178

                          90
                  ....*....|.
gi 807066350  151 PVTLDTPMNRK 161
Cdd:pfam00106 179 PGGVDTDMTKE 189
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 68-134 7.71e-03

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 36.24  E-value: 7.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807066350  68 SLFKNCD--LMWKQsIWTSTIS----SHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLA 134
Cdd:PRK06077  98 SPFLNVDdkLIDKH-ISTDFKSviycSQELAKEMREGGAIVNIASVAGIRPAYGLSIYGAMKAAVINLTKYLA 169
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
 108-163 9.24e-03

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 36.19  E-value: 9.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 807066350 108 AALDGT---PGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSM 163
Cdd:cd08932  131 NSLSGKrvlAGNAGYSASKFALRALAHALR--QEGWDHGVRVSAVCPGFVDTPMAQGLT 187
 
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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