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Conserved domains on  [gi|194382064|dbj|BAG58787|]
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unnamed protein product [Homo sapiens]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
 43-223 1.94e-57

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member cd05327:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 269  Bit Score: 185.51  E-value: 1.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  43 GISSCGR--TREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAHCRGRLDFKRLDRPVVGWRQELRAYADTK 120
Cdd:cd05327   89 GIMAPPRrlTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDFNDLDLENNKEYSPYKAYGQSK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 121 LANVLFARELANQLEATGVTCYAAHPGPVNSELFLRHVP-GWLRPLLRPLAWlvlRAPRGGAQTPLYCALQEGIEPLSGR 199
Cdd:cd05327  169 LANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSfFLLYKLLRPFLK---KSPEQGAQTALYAATSPELEGVSGK 245

                        170       180
                 ....*....|....*....|....
gi 194382064 200 YFANCHVEEVPPAARDDRAAHRLW 223
Cdd:cd05327  246 YFSDCKIKMSSSEALDEELAEKLW 269
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 43-223 1.94e-57

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 185.51  E-value: 1.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  43 GISSCGR--TREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAHCRGRLDFKRLDRPVVGWRQELRAYADTK 120
Cdd:cd05327   89 GIMAPPRrlTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDFNDLDLENNKEYSPYKAYGQSK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 121 LANVLFARELANQLEATGVTCYAAHPGPVNSELFLRHVP-GWLRPLLRPLAWlvlRAPRGGAQTPLYCALQEGIEPLSGR 199
Cdd:cd05327  169 LANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSfFLLYKLLRPFLK---KSPEQGAQTALYAATSPELEGVSGK 245

                        170       180
                 ....*....|....*....|....
gi 194382064 200 YFANCHVEEVPPAARDDRAAHRLW 223
Cdd:cd05327  246 YFSDCKIKMSSSEALDEELAEKLW 269
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 48-231 1.61e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 100.10  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  48 GRTREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAH-CRGRLDFKRLDrpvvgWRQELR---AYADTKLAN 123
Cdd:PRK06197 111 QTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHrIRAAIHFDDLQ-----WERRYNrvaAYGQSKLAN 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 124 VLFARELANQLEATGVTCY--AAHPGPVNSELfLRHVPGWLRPLLRPLAWLVLRAPRGGAQTPLYCALQEGIepLSGRYF 201
Cdd:PRK06197 186 LLFTYELQRRLAAAGATTIavAAHPGVSNTEL-ARNLPRALRPVATVLAPLLAQSPEMGALPTLRAATDPAV--RGGQYY 262

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 194382064 202 ANCHVEEV---------PPAARDDRAAHRLWEASKRLAG 231
Cdd:PRK06197 263 GPDGFGEQrgypkvvasSAQSHDEDLQRRLWAVSEELTG 301
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
49-232 4.09e-10

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 59.62  E-value: 4.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  49 RTREAFNLLLRVNHIGPFLLTHLLLPCLKAC--APSRVVVVASAAHCRGRL----------DFKRLDRPVVGWRQEL--- 113
Cdd:COG5748  103 RSPDGYELSVATNHLGHFLLCNLLLEDLKKSpaSDPRLVILGTVTANPKELggkipipappDLGDLEGFEAGFKAPIsmi 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 114 --------RAYADTKLANVLFARELANQLEA-TGVTCYAAHPGPVNSELFLRHVPGWLRPLlrpLAWLVLRAPRGGAQTP 184
Cdd:COG5748  183 dgkkfkpgKAYKDSKLCNVLTMRELHRRYHEsTGIVFSSLYPGCVADTPLFRNHYPLFQKL---FPLFQKNITGGYVSQE 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194382064 185 LYCAL-----------QEGIEPLSG-RYFANCH--VEEVPPAARDDRAAHRLWEASKRLAGL 232
Cdd:COG5748  260 LAGERvaqvvadpeyaQSGVYWSWGnRQKKGRKsfVQEVSPEASDDDKAKRLWELSAKLVGL 321
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 115-154 2.23e-03

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 38.36  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 194382064  115 AYADTKLANVLFARELANQLEATGVTCYAAHPGPVNSELF 154
Cdd:pfam00106 148 AYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
 
Name Accession Description Interval E-value
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
 43-223 1.94e-57

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 185.51  E-value: 1.94e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  43 GISSCGR--TREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAHCRGRLDFKRLDRPVVGWRQELRAYADTK 120
Cdd:cd05327   89 GIMAPPRrlTKDGFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDFNDLDLENNKEYSPYKAYGQSK 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 121 LANVLFARELANQLEATGVTCYAAHPGPVNSELFLRHVP-GWLRPLLRPLAWlvlRAPRGGAQTPLYCALQEGIEPLSGR 199
Cdd:cd05327  169 LANILFTRELARRLEGTGVTVNALHPGVVRTELLRRNGSfFLLYKLLRPFLK---KSPEQGAQTALYAATSPELEGVSGK 245

                        170       180
                 ....*....|....*....|....
gi 194382064 200 YFANCHVEEVPPAARDDRAAHRLW 223
Cdd:cd05327  246 YFSDCKIKMSSSEALDEELAEKLW 269
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
 43-226 3.08e-53

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 174.96  E-value: 3.08e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  43 GISSCGR--TREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAHCRGRLDFKRLDrpvvgWRQ---ELRAYA 117
Cdd:cd09807   89 GVMRCPYskTEDGFEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINFDDLN-----SEKsynTGFAYC 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 118 DTKLANVLFARELANQLEATGVTCYAAHPGPVNSELFlRHV---PGWLRPLLRPLAWLVLRAPRGGAQTPLYCALQEGIE 194
Cdd:cd09807  164 QSKLANVLFTRELARRLQGTGVTVNALHPGVVRTELG-RHTgihHLFLSTLLNPLFWPFVKTPREGAQTSIYLALAEELE 242

                        170       180       190
                 ....*....|....*....|....*....|..
gi 194382064 195 PLSGRYFANCHVEEVPPAARDDRAAHRLWEAS 226
Cdd:cd09807  243 GVSGKYFSDCKLKEPAPEAMDEETARRLWEIS 274
human_WWOX_like_SDR_c-like cd09809
human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like ...
 49-229 1.70e-26

human WWOX (WW domain-containing oxidoreductase)-like, classical (c)-like SDRs; Classical-like SDR domain of human WWOX and related proteins. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. 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: 187669 [Multi-domain]  Cd Length: 284  Bit Score: 105.37  E-value: 1.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  49 RTREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAH-------CRGRLDFKRLDRPVVGWRQELrAYADTKL 121
Cdd:cd09809   97 LTEDGLETTFQVNHLGHFYLVQLLEDVLRRSAPARVIVVSSESHrftdlpdSCGNLDFSLLSPPKKKYWSML-AYNRAKL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 122 ANVLFARELANQLEATGVTCYAAHPGP-VNSELflrHVPGWLRPLLRPLAWLVLRAPRGGAQTPLYCALQEGIEPLSGRY 200
Cdd:cd09809  176 CNILFSNELHRRLSPRGITSNSLHPGNmMYSSI---HRNWWVYTLLFTLARPFTKSMQQGAATTVYCATAPELEGLGGMY 252

                        170       180
                 ....*....|....*....|....*....
gi 194382064 201 FANCHVEEVPPAARDDRAAHRLWEASKRL 229
Cdd:cd09809  253 FNNCFRCLPSPEAQSEATAQQLWELSERL 281
PRK06197 PRK06197
short chain dehydrogenase; Provisional
 48-231 1.61e-24

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 100.10  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  48 GRTREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAH-CRGRLDFKRLDrpvvgWRQELR---AYADTKLAN 123
Cdd:PRK06197 111 QTTADGFELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHrIRAAIHFDDLQ-----WERRYNrvaAYGQSKLAN 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 124 VLFARELANQLEATGVTCY--AAHPGPVNSELfLRHVPGWLRPLLRPLAWLVLRAPRGGAQTPLYCALQEGIepLSGRYF 201
Cdd:PRK06197 186 LLFTYELQRRLAAAGATTIavAAHPGVSNTEL-ARNLPRALRPVATVLAPLLAQSPEMGALPTLRAATDPAV--RGGQYY 262

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 194382064 202 ANCHVEEV---------PPAARDDRAAHRLWEASKRLAG 231
Cdd:PRK06197 263 GPDGFGEQrgypkvvasSAQSHDEDLQRRLWAVSEELTG 301
PRK06196 PRK06196
oxidoreductase; Provisional
 43-234 2.28e-18

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 83.58  E-value: 2.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  43 GISSCGRTR--EAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAHCRG--RLDFKRLDRPVVGWrqelRAYAD 118
Cdd:PRK06196 108 GVMACPETRvgDGWEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRSpiRWDDPHFTRGYDKW----LAYGQ 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 119 TKLANVLFARELANQLEATGVTCYAAHPGPVNSELfLRHVP-------GWLRPLLRPLAwLVLRAPRGGAQTPLYCALQE 191
Cdd:PRK06196 184 SKTANALFAVHLDKLGKDQGVRAFSVHPGGILTPL-QRHLPreeqvalGWVDEHGNPID-PGFKTPAQGAATQVWAATSP 261

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194382064 192 GIEPLSGRYFANCHVEE----------VPPAARDDRAAHRLWEASKRLAGLGP 234
Cdd:PRK06196 262 QLAGMGGLYCEDCDIAEptpkdapwsgVRPHAIDPEAAARLWALSAALTGVDA 314
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
 49-232 9.53e-15

light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical SDR-like subgroup containing LPOR and related proteins. Protochlorophyllide (Pchlide) reductases act in chlorophyll biosynthesis. There are distinct enzymes that catalyze Pchlide reduction in light or dark conditions. Light-dependent reduction is via an NADP-dependent SDR, LPOR. Proteins in this subfamily share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. 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: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 72.94  E-value: 9.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  49 RTREAFNLLLRVNHIGPFLLTHLLLP--CLKACAPSRVVVVASAAHCRGRL------------------DFKRLDRPVVG 108
Cdd:cd09810   99 FTADGFELTVGVNHLGHFLLTNLLLEdlQRSENASPRIVIVGSITHNPNTLagnvppratlgdleglagGLKGFNSMIDG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 109 WRQE-LRAYADTKLANVLFARELANQL-EATGVTCYAAHPGPVNSELFLRHVPgwlrPLLRPLAWLVLRAPRGGAQTPLY 186
Cdd:cd09810  179 GEFEgAKAYKDSKVCNMLTTYELHRRLhEETGITFNSLYPGCIAETGLFREHY----PLFRTLFPPFQKYITKGYVSEEE 254

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194382064 187 ---CALQEGIEP---LSGRYFAN-----CHVEEVPPAARDDRAAHRLWEASKRLAGL 232
Cdd:cd09810  255 ageRLAAVIADPslgVSGVYWSWgkasgSFENQSSQESSDDEKARKLWEISEKLVGL 311
PRK05854 PRK05854
SDR family oxidoreductase;
50-231 1.80e-10

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 60.46  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  50 TREAFNLLLRVNHIGPFLLTHLLLPCLKAcAPSRVVVVASAAHCRGRLDFKRLDrpvvgWRQ---ELRAYADTKLANVLF 126
Cdd:PRK05854 112 TADGFELQFGTNHLGHFALTAHLLPLLRA-GRARVTSQSSIAARRGAINWDDLN-----WERsyaGMRAYSQSKIAVGLF 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 127 ARELANQLEAT--GVTCYAAHPGPVNSELFL------RHVPGWLRPLLRPL-AWLVLRAPRGGAQTP-LYCALQEGIEPl 196
Cdd:PRK05854 186 ALELDRRSRAAgwGITSNLAHPGVAPTNLLAarpevgRDKDTLMVRLIRSLsARGFLVGTVESAILPaLYAATSPDAEG- 264

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 194382064 197 sGRYFANC---HV------EEVPPAARDDRAAHRLWEASKRLAG 231
Cdd:PRK05854 265 -GAFYGPRgpgELgggpveQALYPPLRRNAEAARLWEVSEQLTG 307
LPOR COG5748
Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];
49-232 4.09e-10

Light-dependent NADPH-protochlorophyllide oxidoreductase [Coenzyme transport and metabolism];


Pssm-ID: 444458 [Multi-domain]  Cd Length: 324  Bit Score: 59.62  E-value: 4.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  49 RTREAFNLLLRVNHIGPFLLTHLLLPCLKAC--APSRVVVVASAAHCRGRL----------DFKRLDRPVVGWRQEL--- 113
Cdd:COG5748  103 RSPDGYELSVATNHLGHFLLCNLLLEDLKKSpaSDPRLVILGTVTANPKELggkipipappDLGDLEGFEAGFKAPIsmi 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 114 --------RAYADTKLANVLFARELANQLEA-TGVTCYAAHPGPVNSELFLRHVPGWLRPLlrpLAWLVLRAPRGGAQTP 184
Cdd:COG5748  183 dgkkfkpgKAYKDSKLCNVLTMRELHRRYHEsTGIVFSSLYPGCVADTPLFRNHYPLFQKL---FPLFQKNITGGYVSQE 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194382064 185 LYCAL-----------QEGIEPLSG-RYFANCH--VEEVPPAARDDRAAHRLWEASKRLAGL 232
Cdd:COG5748  260 LAGERvaqvvadpeyaQSGVYWSWGnRQKKGRKsfVQEVSPEASDDDKAKRLWELSAKLVGL 321
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 50-154 5.64e-08

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: 52.48  E-value: 5.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  50 TREAFNLLLRVNHIGPFllthlllPCLKACAP-------SRVVVVASAAHCRGRLDfkrldrpvvgwrqeLRAYADTKLA 122
Cdd:COG1028  103 TEEDWDRVLDVNLKGPF-------LLTRAALPhmrerggGRIVNISSIAGLRGSPG--------------QAAYAASKAA 161

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194382064 123 NVLFARELANQLEATGVTCYAAHPGPVNSELF 154
Cdd:COG1028  162 VVGLTRSLALELAPRGIRVNAVAPGPIDTPMT 193
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
43-168 4.78e-06

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 46.79  E-value: 4.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  43 GISSCGR----TREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAHCRGRldfkrldrPVVGwrqelrAYAD 118
Cdd:COG0300   91 GVGGGGPfeelDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGL--------PGMA------AYAA 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 194382064 119 TKLANVLFARELANQLEATGVTCYAAHPGPVNSELFLRHVPGWLRPLLRP 168
Cdd:COG0300  157 SKAALEGFSESLRAELAPTGVRVTAVCPGPVDTPFTARAGAPAGRPLLSP 206
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
 50-184 6.33e-06

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: 46.51  E-value: 6.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  50 TREAFNLLLRVNHIGPFLLThlllpclKACAP-------SRVVVVASAAhcrGRldfkrldRPVVGWRqelrAYADTKLA 122
Cdd:cd05233   94 TDEDWDRVLDVNLTGVFLLT-------RAALPhmkkqggGRIVNISSVA---GL-------RPLPGQA----AYAASKAA 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194382064 123 NVLFARELANQLEATGVTCYAAHPGPVNSElFLRHVPGWlrpllRPLAWLVLRAPRGGAQTP 184
Cdd:cd05233  153 LEGLTRSLALELAPYGIRVNAVAPGLVDTP-MLAKLGPE-----EAEKELAAAIPLGRLGTP 208
PLN00015 PLN00015
protochlorophyllide reductase
 114-231 1.10e-05

protochlorophyllide reductase


Pssm-ID: 177654  Cd Length: 308  Bit Score: 46.24  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 114 RAYADTKLANVLFARELANQL-EATGVTCYAAHPGPV-NSELFLRHVPgWLRPLLRPLAWLVlraprggaqTPLYCALQE 191
Cdd:PLN00015 183 KAYKDSKVCNMLTMQEFHRRYhEETGITFASLYPGCIaTTGLFREHIP-LFRLLFPPFQKYI---------TKGYVSEEE 252

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 192 GIEPL-----------SGRY---------FANchveEVPPAARDDRAAHRLWEASKRLAG 231
Cdd:PLN00015 253 AGKRLaqvvsdpsltkSGVYwswnggsasFEN----QLSQEASDAEKAKKVWEISEKLVG 308
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
 115-155 1.78e-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: 42.26  E-value: 1.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 194382064 115 AYADTKLANVLFARELANQLEATGVTCYAAHPGPVNSELFL 155
Cdd:cd05362  150 AYAGSKAAVEAFTRVLAKELGGRGITVNAVAPGPVDTDMFY 190
DR_C-13_KR_SDR_c_like cd08951
daunorubicin C-13 ketoreductase (KR), classical (c)-like SDRs; Daunorubicin is a clinically ...
 81-232 2.97e-04

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


Pssm-ID: 187654 [Multi-domain]  Cd Length: 260  Bit Score: 41.71  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  81 PSRVVVVASAAHCRGRLDFKRLDRPVVGWrQELRAYADTKLANVLFARELANQLEATGVTcyAAHPGPVNSELFLRHVPG 160
Cdd:cd08951  124 PKRLIYLSSGMHRGGNASLDDIDWFNRGE-NDSPAYSDSKLHVLTLAAAVARRWKDVSSN--AVHPGWVPTKMGGAGAPD 200

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194382064 161 WLRPLLRPLAWLVlraprggaqtplycalqEGIEP---LSGRYFANCHVEEVPPAARDDRAAHRLWEASKRLAGL 232
Cdd:cd08951  201 DLEQGHLTQVWLA-----------------ESDDPqalTSGGYFYHRRLQEPHPASEDSRLQEKLVQALEEVTGV 258
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
 50-153 1.32e-03

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 39.20  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064  50 TREAFNLLLRVNHIGPFLLTHLLLPCLKACAPSRVVVVASAAhcrGRLDfkrlDRPVVGWrqelRAYADTKLANVLFARE 129
Cdd:cd05325   96 DSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRV---GSIG----DNTSGGW----YSYRASKAALNMLTKS 164

                         90       100
                 ....*....|....*....|....
gi 194382064 130 LANQLEATGVTCYAAHPGPVNSEL 153
Cdd:cd05325  165 LAVELKRDGITVVSLHPGWVRTDM 188
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
 115-154 2.23e-03

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 38.36  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 194382064  115 AYADTKLANVLFARELANQLEATGVTCYAAHPGPVNSELF 154
Cdd:pfam00106 148 AYSASKAAVIGFTRSLALELAPHGIRVNAVAPGGVDTDMT 187
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 108-184 3.79e-03

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 38.13  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 108 GWRQ-----ELrAYADTKLANVLFARELANQLEATGVTCYAAHPGPVNSelflrhvpGWLRPLLRplAWLVLRAPRGGAQ 182
Cdd:PRK12748 155 GQSLgpmpdEL-AYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDT--------GWITEELK--HHLVPKFPQGRVG 223


                 ..
gi 194382064 183 TP 184
Cdd:PRK12748 224 EP 225
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
 115-201 8.58e-03

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 36.83  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194382064 115 AYADTKLANVLFARELANQLEATGVTCYAAHPGPVNSELflrhvpgwlrplLRPLAWlvlRAPRGGAQTPLYCALQEGIE 194
Cdd:cd05324  146 AYGVSKAALNALTRILAKELKETGIKVNACCPGWVKTDM------------GGGKAP---KTPEEGAETPVYLALLPPDG 210


                 ....*..
gi 194382064 195 PLSGRYF 201
Cdd:cd05324  211 EPTGKFF 217
PRK12939 PRK12939
short chain dehydrogenase; Provisional
 106-155 8.69e-03

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 36.87  E-value: 8.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 194382064 106 VVGWRQE-LRAYADTKLANVLFARELANQLEATGVTCYAAHPGPVNSELFL 155
Cdd:PRK12939 145 TALWGAPkLGAYVASKGAVIGMTRSLARELGGRGITVNAIAPGLTATEATA 195
 
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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