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Conserved domains on  [gi|208973246|ref|NP_000311|]
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dihydropteridine reductase isoform 1 [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 ...
 10-232 2.69e-132

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: 372.04  E-value: 2.69e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  10 ARRVLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASIIVKMTDSFTEQADQVTAEVGKLlgEEKVDAILCVAGG 89
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSDSFTEQAKQVVASVARL--SGKVDALICVAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  90 WAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNS 169
Cdd:cd05334   79 WAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 208973246 170 GMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVT 232
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 ...
 10-232 2.69e-132

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: 372.04  E-value: 2.69e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  10 ARRVLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASIIVKMTDSFTEQADQVTAEVGKLlgEEKVDAILCVAGG 89
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSDSFTEQAKQVVASVARL--SGKVDALICVAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  90 WAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNS 169
Cdd:cd05334   79 WAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 208973246 170 GMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVT 232
Cdd:cd05334  159 GLPAGSTANAILPVTLDTPANRKAMPDADFSSWTPLEFIAELILFWASGAARPKSGSLIPVVT 221
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 9-230 4.90e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 66.36  E-value: 4.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   9 EARRVLVYGGRGALGSRCVQAFRARNWWVASVD--------VVENEEASASIIVKMTDSFTEQADQVTAEVGKLLGeeKV 80
Cdd:PRK12828   6 QGKVVAITGGFGGLGRATAAWLAARGARVALIGrgaaplsqTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG--RL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  81 DAILCVAGGWAGGNAKSKSLfKNCDLMWKQSIWTSTISSHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGAVH 158
Cdd:PRK12828  84 DALVNIAGAFVWGTIADGDA-DTWDRMYGVNVKTTLNASKAALPALTAsgGGRIVNIGAGAALKAGPGMGAYAAAKAGVA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 208973246 159 QLCQSLAGKNsgMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQV 230
Cdd:PRK12828 163 RLTEALAAEL--LDRGITVNAVLPSIIDTPPNRADMPDADFSRWVTPEQIAAVIAFLLSDEAQAITGASIPV 232
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
11-204 2.42e-06

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 47.17  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  11 RRVLVYGGRGALGSRCVQAFRARNW--WVASVDVVENEEASASIIVK----------MTDsfTEQADQVTAEVGKLLGee 78
Cdd:COG0300    6 KTVLITGASSGIGRALARALAARGArvVLVARDAERLEALAAELRAAgarvevvaldVTD--PDAVAALAEAVLARFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  79 KVDAILCVAGGWAGGnaksksLFKNCDL-MWKQSIWTSTISSHLATKHL-------KEGGLLTLAGAkAALDGTPGMIGY 150
Cdd:COG0300   82 PIDVLVNNAGVGGGG------PFEELDLeDLRRVFEVNVFGPVRLTRALlplmrarGRGRIVNVSSV-AGLRGLPGMAAY 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 208973246 151 GMAKGAVHQLCQSLAGKNSgmPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTP 204
Cdd:COG0300  155 AASKAALEGFSESLRAELA--PTGVRVTAVCPGPVDTPFTARAGAPAGRPLLSP 206
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 13-192 5.72e-06

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 45.68  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   13 VLVYGGRGALGSRCVQAFRARNWWVASVDVVEN---------EEASASIIVKMTD-SFTEQADQVTAEVGKLLGeeKVDA 82
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEkleavakelGALGGKALFIQGDvTDRAQVKALVEQAVERLG--RLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   83 ILCVAGGWAGGNAKSKSLFKncdlmWKQSI---WTSTIS-SHLATKHLKEG--GLLTLAGAKAALDGTPGMIGYGMAKGA 156
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDED-----WERVIdvnLTGVFNlTRAVLPAMIKGsgGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 208973246  157 VHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRK 192
Cdd:pfam00106 156 VIGFTRSLA--LELAPHGIRVNAVAPGGVDTDMTKE 189
 
Name Accession Description Interval E-value
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
 10-232 2.69e-132

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: 372.04  E-value: 2.69e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  10 ARRVLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASIIVKMTDSFTEQADQVTAEVGKLlgEEKVDAILCVAGG 89
Cdd:cd05334    1 ARVVLVYGGRGALGSAVVQAFKSRGWWVASIDLAENEEADASIIVLDSDSFTEQAKQVVASVARL--SGKVDALICVAGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  90 WAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNS 169
Cdd:cd05334   79 WAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLLSGGLLVLTGAKAALEPTPGMIGYGAAKAAVHQLTQSLAAENS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 208973246 170 GMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQVVT 232
Cdd:cd05334  159 GLPAGSTANAILPVTLDTPANRKAMPDADFSSWTPLEFIAELILFWASGAARPKSGSLIPVVT 221
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 13-230 1.38e-19

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: 84.26  E-value: 1.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  13 VLVYGGRGALGSRCVQAFRARNWWVASVD--------VVENEEASASII-VKMTDSFTEQADQVTAEVGKLLGeeKVDAI 83
Cdd:cd05233    1 ALVTGASSGIGRAIARRLAREGAKVVLADrneealaeLAAIEALGGNAVaVQADVSDEEDVEALVEEALEEFG--RLDIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  84 LCVAGGWAGGNAkSKSLFKNCDLMWKQSIWTSTISSHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLC 161
Cdd:cd05233   79 VNNAGIARPGPL-EELTDEDWDRVLDVNLTGVFLLTRAALPHMKKqgGGRIVNISSVAGLRPLPGQAAYAASKAALEGLT 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 208973246 162 QSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPEADFSS---------WTPLEFLVETFHDWITGKNRPSSGSLIQV 230
Cdd:cd05233  158 RSLA--LELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKElaaaiplgrLGTPEEVAEAVVFLASDEASYITGQVIPV 233
PRK12828 PRK12828
short chain dehydrogenase; Provisional
 9-230 4.90e-13

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 66.36  E-value: 4.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   9 EARRVLVYGGRGALGSRCVQAFRARNWWVASVD--------VVENEEASASIIVKMTDSFTEQADQVTAEVGKLLGeeKV 80
Cdd:PRK12828   6 QGKVVAITGGFGGLGRATAAWLAARGARVALIGrgaaplsqTLPGVPADALRIGGIDLVDPQAARRAVDEVNRQFG--RL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  81 DAILCVAGGWAGGNAKSKSLfKNCDLMWKQSIWTSTISSHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAKGAVH 158
Cdd:PRK12828  84 DALVNIAGAFVWGTIADGDA-DTWDRMYGVNVKTTLNASKAALPALTAsgGGRIVNIGAGAALKAGPGMGAYAAAKAGVA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 208973246 159 QLCQSLAGKNsgMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVETFHDWITGKNRPSSGSLIQV 230
Cdd:PRK12828 163 RLTEALAAEL--LDRGITVNAVLPSIIDTPPNRADMPDADFSRWVTPEQIAAVIAFLLSDEAQAITGASIPV 232
PRK06701 PRK06701
short chain dehydrogenase; Provisional
 122-205 5.65e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 49.26  E-value: 5.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246 122 ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGknSGMPPGAAAIAVLPVTLDTPMNRKSMPE---AD 198
Cdd:PRK06701 167 ALPHLKQGSAIINTGSITGYEGNETLIDYSATKGAIHAFTRSLAQ--SLVQKGIRVNAVAPGPIWTPLIPSDFDEekvSQ 244


                 ....*..
gi 208973246 199 FSSWTPL 205
Cdd:PRK06701 245 FGSNTPM 251
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
11-204 2.42e-06

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 47.17  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  11 RRVLVYGGRGALGSRCVQAFRARNW--WVASVDVVENEEASASIIVK----------MTDsfTEQADQVTAEVGKLLGee 78
Cdd:COG0300    6 KTVLITGASSGIGRALARALAARGArvVLVARDAERLEALAAELRAAgarvevvaldVTD--PDAVAALAEAVLARFG-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  79 KVDAILCVAGGWAGGnaksksLFKNCDL-MWKQSIWTSTISSHLATKHL-------KEGGLLTLAGAkAALDGTPGMIGY 150
Cdd:COG0300   82 PIDVLVNNAGVGGGG------PFEELDLeDLRRVFEVNVFGPVRLTRALlplmrarGRGRIVNVSSV-AGLRGLPGMAAY 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 208973246 151 GMAKGAVHQLCQSLAGKNSgmPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTP 204
Cdd:COG0300  155 AASKAALEGFSESLRAELA--PTGVRVTAVCPGPVDTPFTARAGAPAGRPLLSP 206
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 11-199 4.46e-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: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  11 RRVLVYGGRGALGSRCVQAFRARNWWVASVDVVEN--EEASASIIVK----------MTDsfTEQADQVTAEVGKLLGee 78
Cdd:COG1028    7 KVALVTGGSSGIGRAIARALAAEGARVVITDRDAEalEAAAAELRAAggralavaadVTD--EAAVEALVAAAVAAFG-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  79 KVDAILCVAGGWAGGNAKSKSL--FkncDLMWKQSIWTSTISSHLATKHLKE--GGLLTLAGAKAALDGTPGMIGYGMAK 154
Cdd:COG1028   83 RLDILVNNAGITPPGPLEELTEedW---DRVLDVNLKGPFLLTRAALPHMRErgGGRIVNISSIAGLRGSPGQAAYAASK 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 208973246 155 GAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPEADF 199
Cdd:COG1028  160 AAVVGLTRSLA--LELAPRGIRVNAVAPGPIDTPMTRALLGAEEV 202
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 13-192 5.72e-06

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 45.68  E-value: 5.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   13 VLVYGGRGALGSRCVQAFRARNWWVASVDVVEN---------EEASASIIVKMTD-SFTEQADQVTAEVGKLLGeeKVDA 82
Cdd:pfam00106   3 ALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEkleavakelGALGGKALFIQGDvTDRAQVKALVEQAVERLG--RLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   83 ILCVAGGWAGGNAKSKSLFKncdlmWKQSI---WTSTIS-SHLATKHLKEG--GLLTLAGAKAALDGTPGMIGYGMAKGA 156
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDED-----WERVIdvnLTGVFNlTRAVLPAMIKGsgGRIVNISSVAGLVPYPGGSAYSASKAA 155

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 208973246  157 VHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRK 192
Cdd:pfam00106 156 VIGFTRSLA--LELAPHGIRVNAVAPGGVDTDMTKE 189
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
 13-198 2.24e-05

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 44.38  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  13 VLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASIIVKMTDSFTEQADQVTAEVGKLLGE-EKVDAILCVAGGWA 91
Cdd:cd05331    1 VIVTGAAQGIGRAVARHLLQAGATVIALDLPFVLLLEYGDPLRLTPLDVADAAAVREVCSRLLAEhGPIDALVNCAGVLR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  92 GGNAKSKSlfkncDLMWkQSIWTSTISSHLAT-----KHLKE--GGLLTLAGAKAAldGTP--GMIGYGMAKGAVHQLCQ 162
Cdd:cd05331   81 PGATDPLS-----TEDW-EQTFAVNVTGVFNLlqavaPHMKDrrTGAIVTVASNAA--HVPriSMAAYGASKAALASLSK 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 208973246 163 SLAGKNSgmPPGAAAIAVLPVTLDTPMNRKSMPEAD 198
Cdd:cd05331  153 CLGLELA--PYGVRCNVVSPGSTDTAMQRTLWHDED 186
PRK12827 PRK12827
short chain dehydrogenase; Provisional
 10-210 2.74e-05

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 43.94  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  10 ARRVLVYGGRGALGSRCVQAFRARNWWVASVDV------VENEEASASIIVKMTDSFTEQAD----QVTAEVGKLLGEE- 78
Cdd:PRK12827   6 SRRVLITGGSGGLGRAIAVRLAADGADVIVLDIhpmrgrAEADAVAAGIEAAGGKALGLAFDvrdfAATRAALDAGVEEf 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  79 -KVDAILCVAGGWAGGNAKSKSLfKNCDLMWKQSIWTSTISSHLATKHL---KEGGLLTLAGAKAALDGTPGMIGYGMAK 154
Cdd:PRK12827  86 gRLDILVNNAGIATDAAFAELSI-EEWDDVIDVNLDGFFNVTQAALPPMiraRRGGRIVNIASVAGVRGNRGQVNYAASK 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 208973246 155 GAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPEADFSSWTPLEFLVE 210
Cdd:PRK12827 165 AGLIGLTKTLA--NELAPRGITVNAVAPGAINTPMADNAAPTEHLLNPVPVQRLGE 218
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
 26-165 1.12e-04

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: 42.03  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   26 CVQAFRARNWWVASVDVVENEEASASIIVKMTD--------SFTEQADQVTAEVGKLLGeeKVDAILCVAGgWAGgnaKS 97
Cdd:pfam13561  12 IARALAEEGAEVVLTDLNEALAKRVEELAEELGaavlpcdvTDEEQVEALVAAAVEKFG--RLDILVNNAG-FAP---KL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 208973246   98 KSLFKNCDL-MWKQSIWTSTISSHLATKH----LKEGG-LLTLAGAkAALDGTPGMIGYGMAKGAVHQLCQSLA 165
Cdd:pfam13561  86 KGPFLDTSReDFDRALDVNLYSLFLLAKAalplMKEGGsIVNLSSI-GAERVVPNYNAYGAAKAALEALTRYLA 158
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
 13-189 3.41e-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: 40.26  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  13 VLVYGGRGALGSRCVQAFRARnwwvaSVDVVENEEASASIIVKMTDsfTEQADQVTAEVGKllgeekVDAILCVAGGwag 92
Cdd:cd11731    1 IIVIGATGTIGLAVAQLLSAH-----GHEVITAGRSSGDYQVDITD--EASIKALFEKVGH------FDAIVSTAGD--- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  93 gnAKSKSLFkncdlMWKQSIWTSTISSHL---------ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQS 163
Cdd:cd11731   65 --AEFAPLA-----ELTDADFQRGLNSKLlgqinlvrhGLPYLNDGGSITLTSGILAQRPIPGGAAAATVNGALEGFVRA 137

                        170       180
                 ....*....|....*....|....*.
gi 208973246 164 LAGKnsgMPPGAAAIAVLPVTLDTPM 189
Cdd:cd11731  138 AAIE---LPRGIRINAVSPGVVEESL 160
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
11-205 3.59e-04

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 40.53  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  11 RRVLVYGGRGALGSRCVQAFRAR--NWWVASVDVVENEEASASI----------IVKMTDSftEQADQVTAEVGKLLGEe 78
Cdd:PRK05653   6 KTALVTGASRGIGRAIALRLAADgaKVVIYDSNEEAAEALAAELraaggearvlVFDVSDE--AAVRALIEAAVEAFGA- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  79 kVDAILCVAGGwaggnakskslfkNCD-LMWKQSI--WTSTIS---------SHLATKHLKE--GGLLTLAGAKAALDGT 144
Cdd:PRK05653  83 -LDILVNNAGI-------------TRDaLLPRMSEedWDRVIDvnltgtfnvVRAALPPMIKarYGRIVNISSVSGVTGN 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246 145 PGMIGYGMAKGAVHQLCQSLA----GKNsgmppgaaaI---AVLPVTLDTPMNRKS--MPEADFSSWTPL 205
Cdd:PRK05653 149 PGQTNYSAAKAGVIGFTKALAlelaSRG---------ItvnAVAPGFIDTDMTEGLpeEVKAEILKEIPL 209
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
 13-189 5.75e-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: 39.81  E-value: 5.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  13 VLVYGGRGALGSRCVQAFRARNW--WVASVD--VVENEEASASIIVKMTDSFTEQADQVTAEvgkllGEEKVDAILcvag 88
Cdd:cd11730    1 ALILGATGGIGRALARALAGRGWrlLLSGRDagALAGLAAEVGALARPADVAAELEVWALAQ-----ELGPLDLLV---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  89 gWAGGNAKSKSLFKNCDLMWKQSIWTSTISSHLATKH----LKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSL 164
Cdd:cd11730   72 -YAAGAILGKPLARTKPAAWRRILDANLTGAALVLKHalalLAAGARLVFLGAYPELVMLPGLSAYAAAKAALEAYVEVA 150

                        170       180
                 ....*....|....*....|....*
gi 208973246 165 AGKNSgmppGAAAIAVLPVTLDTPM 189
Cdd:cd11730  151 RKEVR----GLRLTLVRPPAVDTGL 171
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
 13-165 1.34e-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: 38.90  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  13 VLVYGGRGALGSRCVQAFRARNWWVA----------SVDVVENEEASASIIVKMTDSFTEqaDQVTAEVGKLLGE-EKVD 81
Cdd:cd05373    2 AAVVGAGDGLGAAIARRFAAEGFSVAlaarreakleALLVDIIRDAGGSAKAVPTDARDE--DEVIALFDLIEEEiGPLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  82 AILCVAGG--WAGGNAKSKSLFKNCdlmWKQSIWTSTISSHLATKHL--KEGGLLTLAGAKAALDGTPGMIGYGMAKGAV 157
Cdd:cd05373   80 VLVYNAGAnvWFPILETTPRVFEKV---WEMAAFGGFLAAREAAKRMlaRGRGTIIFTGATASLRGRAGFAAFAGAKFAL 156


                 ....*...
gi 208973246 158 HQLCQSLA 165
Cdd:cd05373  157 RALAQSMA 164
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 122-228 1.47e-03

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: 38.80  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246 122 ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPEAD--- 198
Cdd:cd05362  123 AAKRLRDGGRIINISSSLTAAYTPNYGAYAGSKAAVEAFTRVLA--KELGGRGITVNAVAPGPVDTDMFYAGKTEEAveg 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 208973246 199 FSSWTPLE-------------FLVETFHDWITGKNRPSSGSLI 228
Cdd:cd05362  201 YAKMSPLGrlgepediapvvaFLASPDGRWVNGQVIRANGGYV 243
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
 108-198 2.72e-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: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246 108 WKQSIWTSTISSHLATKHL------KEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNsgmppGAAAI--- 178
Cdd:cd08944  102 WDQTMAINLRGTFLCCRHAaprmiaRGGGSIVNLSSIAGQSGDPGYGAYGASKAAIRNLTRTLAAEL-----RHAGIrcn 176

                         90       100
                 ....*....|....*....|
gi 208973246 179 AVLPVTLDTPMNRKSMPEAD 198
Cdd:cd08944  177 ALAPGLIDTPLLLAKLAGFE 196
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
 13-189 3.90e-03

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 37.67  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  13 VLVYGGRGALGSRCVQAFRARNWWVASVDVVENEEASASI--IVKMTDSFTEQAD-----QVTAEVGKLLGEEK-VDAIL 84
Cdd:cd05323    3 AIITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAELqaINPKVKATFVQCDvtsweQLAAAFKKAIEKFGrVDILI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  85 CVAGGwaggnAKSKSLFKNCDLM--WKQSI---WTSTI-SSHLATKHLK-----EGGLLTLAGAKAALDGTPGMIGYGMA 153
Cdd:cd05323   83 NNAGI-----LDEKSYLFAGKLPppWEKTIdvnLTGVInTTYLALHYMDknkggKGGVIVNIGSVAGLYPAPQFPVYSAS 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 208973246 154 KGAVHQLCQSLAGKnSGMPPGAAAIAVLPVTLDTPM 189
Cdd:cd05323  158 KHGVVGFTRSLADL-LEYKTGVRVNAICPGFTNTPL 192
PRK07478 PRK07478
short chain dehydrogenase; Provisional
 108-202 4.07e-03

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 37.60  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246 108 WKQSIWTSTISSHLATKH-----LKEGG-----LLTLAGAKAALdgtPGMIGYGMAKGAVHQLCQSLAGKNSgmPPGAAA 177
Cdd:PRK07478 108 WRETLATNLTSAFLGAKHqipamLARGGgslifTSTFVGHTAGF---PGMAAYAASKAGLIGLTQVLAAEYG--AQGIRV 182

                         90       100
                 ....*....|....*....|....*
gi 208973246 178 IAVLPVTLDTPMNRKSMPEADFSSW 202
Cdd:PRK07478 183 NALLPGGTDTPMGRAMGDTPEALAF 207
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
 9-191 4.62e-03

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 37.56  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246   9 EARRVLVYG-GRGaLGSRCVQAFRARNWWVASVDVVENEEAS---ASIIVKMTDsfteqADQVTAEVGKLLGE-EKVDAI 83
Cdd:PRK08220   7 SGKTVWVTGaAQG-IGYAVALAFVEAGAKVIGFDQAFLTQEDypfATFVLDVSD-----AAAVAQVCQRLLAEtGPLDVL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246  84 LCVAGGWAGGNAKSKSlfkncDLMWKQSIWTST-----ISSHLAtKHLKE--GGLLTLAGAKAAldGTP--GMIGYGMAK 154
Cdd:PRK08220  81 VNAAGILRMGATDSLS-----DEDWQQTFAVNAggafnLFRAVM-PQFRRqrSGAIVTVGSNAA--HVPriGMAAYGASK 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 208973246 155 GAVHQLCQSLagknsGM---PPGAAAIAVLPVTLDTPMNR 191
Cdd:PRK08220 153 AALTSLAKCV-----GLelaPYGVRCNVVSPGSTDTDMQR 187
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
 105-213 6.39e-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: 36.99  E-value: 6.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246 105 DLMWKQSIWTSTISSHLATKHLK--EGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAGKNSGMppGAAAIAVLP 182
Cdd:cd05338  117 DLMQRVNLRGTYLLSQAALPHMVkaGQGHILNISPPLSLRPARGDVAYAAGKAGMSRLTLGLAAELRRH--GIAVNSLWP 194

                         90       100       110
                 ....*....|....*....|....*....|..
gi 208973246 183 VTL-DTPMNRKSMPEADFSSWTPLEFLVETFH 213
Cdd:cd05338  195 STAiETPAATELSGGSDPARARSPEILSDAVL 226
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
 122-206 9.15e-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: 9.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 208973246 122 ATKHLKEGGLLTLAGAKAALDGTPGMIGYGMAKGAVHQLCQSLAgkNSGMPPGAAAIAVLPVTLDTPMNRKSMPE---AD 198
Cdd:cd05355  148 ALPHLKKGSSIINTTSVTAYKGSPHLLDYAATKGAIVAFTRGLS--LQLAEKGIRVNAVAPGPIWTPLIPSSFPEekvSE 225


                 ....*...
gi 208973246 199 FSSWTPLE 206
Cdd:cd05355  226 FGSQVPMG 233
 
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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