NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1111477935|emb|CVK84676|]
View 

related to aldehyde reductase II [Fusarium proliferatum]

Protein Classification

SDR family oxidoreductase( domain architecture ID 10142552)

extended SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase such as aldehyde reductase that catalyzes the NADPH-dependent reduction of aldehydes such as methylglyoxal, isovaleraldehyde, cinnamic aldehyde, or benzaldehyde; in addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0016491
SCOP:  4000029

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
3-318 1.64e-103

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


:

Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 305.73  E-value: 1.64e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEF-QGLGEEKLDFAIVPDIAAKDAFQGLGAyGLEAAIHV 81
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLKAGYKVRGTVRSLSKSAKLKALLkAAGYNDRLEFVIVDDLTAPNAWDEALK-GVDYVIHV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  82 ASPFHYNITDAKKDLIDPAVLGTTSVLDALHKtCPTVRRVALTSSFAAILDPKLSFTgaKKTYTEADWSPLTIedAYSNP 161
Cdd:cd05227    80 ASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKA-AGSVKRVVLTSSVAAVGDPTAEDP--GKVFTEEDWNDLTI--SKSNG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 162 GLAYATSKALAEKAAWDFMADTKPHFSLTTICPPMVYGPVKYPvkslDSVNTSNQLLADILNGKHkSGLPPTQLPLWIDV 241
Cdd:cd05227   155 LDAYIASKTLAEKAAWEFVKENKPKFELITINPGYVLGPSLLA----DELNSSNELINKLLDGKL-PAIPPNLPFGYVDV 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1111477935 242 RDVALAHVKAVETQEAANKRIFVTAGYYSNQELYRILYENFADLRDRLPEeankgGDPNPALDSFGFDVTRANTILG 318
Cdd:cd05227   230 RDVADAHVRALESPEAAGQRFIVSAGPFSFQEIADLLREEFPQLTAPFPA-----PNPLMLSILVKFDNRKSEELLG 301
 
Name Accession Description Interval E-value
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
3-318 1.64e-103

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 305.73  E-value: 1.64e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEF-QGLGEEKLDFAIVPDIAAKDAFQGLGAyGLEAAIHV 81
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLKAGYKVRGTVRSLSKSAKLKALLkAAGYNDRLEFVIVDDLTAPNAWDEALK-GVDYVIHV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  82 ASPFHYNITDAKKDLIDPAVLGTTSVLDALHKtCPTVRRVALTSSFAAILDPKLSFTgaKKTYTEADWSPLTIedAYSNP 161
Cdd:cd05227    80 ASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKA-AGSVKRVVLTSSVAAVGDPTAEDP--GKVFTEEDWNDLTI--SKSNG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 162 GLAYATSKALAEKAAWDFMADTKPHFSLTTICPPMVYGPVKYPvkslDSVNTSNQLLADILNGKHkSGLPPTQLPLWIDV 241
Cdd:cd05227   155 LDAYIASKTLAEKAAWEFVKENKPKFELITINPGYVLGPSLLA----DELNSSNELINKLLDGKL-PAIPPNLPFGYVDV 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1111477935 242 RDVALAHVKAVETQEAANKRIFVTAGYYSNQELYRILYENFADLRDRLPEeankgGDPNPALDSFGFDVTRANTILG 318
Cdd:cd05227   230 RDVADAHVRALESPEAAGQRFIVSAGPFSFQEIADLLREEFPQLTAPFPA-----PNPLMLSILVKFDNRKSEELLG 301
PLN02662 PLN02662
cinnamyl-alcohol dehydrogenase family protein
4-335 5.00e-54

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178268 [Multi-domain]  Cd Length: 322  Bit Score: 179.91  E-value: 5.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRH--EFQGlGEEKLDFaIVPDIAAKDAFQGLgAYGLEAAIHV 81
Cdd:PLN02662    7 VCVTGASGYIASWLVKLLLQRGYTVKATVRDPNDPKKTEHllALDG-AKERLHL-FKANLLEEGSFDSV-VDGCEGVFHT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  82 ASPFHYNITDAKKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAILdpklsFTGAKKTyteadwsPLTIEDA--YS 159
Cdd:PLN02662   84 ASPFYHDVTDPQAELIDPAVKGTLNVLRSCAKV-PSVKRVVVTSSMAAVA-----YNGKPLT-------PDVVVDEtwFS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 160 NPGLA------YATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGkhKSGLPPT 233
Cdd:PLN02662  151 DPAFCeesklwYVLSKTLAEEAAWKFAKENG--IDMVTINPAMVIGPLLQP-----TLNTSAEAILNLING--AQTFPNA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 234 QLPlWIDVRDVALAHVKAVETQEAANKRIFV-TAGYYSnqELYRILYENFADLrdRLPEeanKGGDPNPALDSFGFDVTR 312
Cdd:PLN02662  222 SYR-WVDVRDVANAHIQAFEIPSASGRYCLVeRVVHYS--EVVKILHELYPTL--QLPE---KCADDKPYVPTYQVSKEK 293
                         330       340
                  ....*....|....*....|...
gi 1111477935 313 ANTiLGIDWIPYENTIIDSVKSL 335
Cdd:PLN02662  294 AKS-LGIEFIPLEVSLKDTVESL 315
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
3-323 2.24e-35

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 130.10  E-value: 2.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHefqglgEEKLDFAIVpDIAAKDAFQGLgAYGLEAAIHVA 82
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAA------LPGVEFVRG-DLRDPEALAAA-LAGVDAVVHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 SPFHYNITDAkKDLIDPAVLGTTSVLDALHKTCptVRRVALTSSFAAILDPKLSFTgakktyteadwspltiEDAYSNPG 162
Cdd:COG0451    73 APAGVGEEDP-DETLEVNVEGTLNLLEAARAAG--VKRFVYASSSSVYGDGEGPID----------------EDTPLRPV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 163 LAYATSKALAEKAAWDFMAdtKPHFSLTTICPPMVYGPVKYPVksldsvntSNQLLADILNGK----HKSGLPPTQlplW 238
Cdd:COG0451   134 SPYGASKLAAELLARAYAR--RYGLPVTILRPGNVYGPGDRGV--------LPRLIRRALAGEpvpvFGDGDQRRD---F 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 239 IDVRDVALAHVKAVETQEAANKRIFVTAG-YYSNQELYRILyENFADLRDRLPEEANKGGdpnpaLDSFGFDVTRANTIL 317
Cdd:COG0451   201 IHVDDVARAIVLALEAPAAPGGVYNVGGGePVTLRELAEAI-AEALGRPPEIVYPARPGD-----VRPRRADNSKARREL 274

                  ....*.
gi 1111477935 318 GidWIP 323
Cdd:COG0451   275 G--WRP 278
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
4-262 2.17e-14

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 71.56  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRseqkaQSIRHEFQGLGEEKLDFAIVPDIAAKDAFqgLGAYGLEAAIHVAS 83
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDR-----LTSASNTARLADLRFVEGDLTDRDALEKL--LADVRPDAVIHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  84 PFHY--NITDAkKDLIDPAVLGTTSVLDALHKTcpTVRRVALTSSfAAILDPKLSFTGAKKTyteadwspLTIEDAYSNP 161
Cdd:pfam01370  74 VGGVgaSIEDP-EDFIEANVLGTLNLLEAARKA--GVKRFLFASS-SEVYGDGAEIPQEETT--------LTGPLAPNSP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 162 glaYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPvkypvksLDSVNTSNQLLADILNgKHKSGLPP------TQL 235
Cdd:pfam01370 142 ---YAAAKLAGEWLVLAYAAAYG--LRAVILRLFNVYGP-------GDNEGFVSRVIPALIR-RILEGKPIllwgdgTQR 208
                         250       260
                  ....*....|....*....|....*..
gi 1111477935 236 PLWIDVRDVALAHVKAVETQEAANKRI 262
Cdd:pfam01370 209 RDFLYVDDVARAILLALEHGAVKGEIY 235
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
4-151 1.35e-06

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 49.18  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAqsirhefqglgeeKLDFAIVPDIAAKDAFQGLGayGLEAAIHVA- 82
Cdd:TIGR01777   1 ILITGGTGFIGRALTQRLTKRGHEVTILTRSPPPG-------------ANTKWEGYKPWAGEDADSLE--GADAVINLAg 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 -SPFHYNITDAKKDLIDPAVLGTTSVLDALHKTCPTVRRVALTSSFAAILDPKLSftgakKTYTEADWSP 151
Cdd:TIGR01777  66 ePIADKRWTEERKQEIRDSRIDTTRLLVEAIAAAEQKPKVFISASAVGYYGPSED-----REYTEEDSPA 130
 
Name Accession Description Interval E-value
AR_SDR_e cd05227
aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the ...
3-318 1.64e-103

aldehyde reductase, extended (e) SDRs; This subgroup contains aldehyde reductase of the extended SDR-type and related proteins. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187538 [Multi-domain]  Cd Length: 301  Bit Score: 305.73  E-value: 1.64e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEF-QGLGEEKLDFAIVPDIAAKDAFQGLGAyGLEAAIHV 81
Cdd:cd05227     1 LVLVTGATGFIASHIVEQLLKAGYKVRGTVRSLSKSAKLKALLkAAGYNDRLEFVIVDDLTAPNAWDEALK-GVDYVIHV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  82 ASPFHYNITDAKKDLIDPAVLGTTSVLDALHKtCPTVRRVALTSSFAAILDPKLSFTgaKKTYTEADWSPLTIedAYSNP 161
Cdd:cd05227    80 ASPFPFTGPDAEDDVIDPAVEGTLNVLEAAKA-AGSVKRVVLTSSVAAVGDPTAEDP--GKVFTEEDWNDLTI--SKSNG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 162 GLAYATSKALAEKAAWDFMADTKPHFSLTTICPPMVYGPVKYPvkslDSVNTSNQLLADILNGKHkSGLPPTQLPLWIDV 241
Cdd:cd05227   155 LDAYIASKTLAEKAAWEFVKENKPKFELITINPGYVLGPSLLA----DELNSSNELINKLLDGKL-PAIPPNLPFGYVDV 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1111477935 242 RDVALAHVKAVETQEAANKRIFVTAGYYSNQELYRILYENFADLRDRLPEeankgGDPNPALDSFGFDVTRANTILG 318
Cdd:cd05227   230 RDVADAHVRALESPEAAGQRFIVSAGPFSFQEIADLLREEFPQLTAPFPA-----PNPLMLSILVKFDNRKSEELLG 301
PLN02662 PLN02662
cinnamyl-alcohol dehydrogenase family protein
4-335 5.00e-54

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178268 [Multi-domain]  Cd Length: 322  Bit Score: 179.91  E-value: 5.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRH--EFQGlGEEKLDFaIVPDIAAKDAFQGLgAYGLEAAIHV 81
Cdd:PLN02662    7 VCVTGASGYIASWLVKLLLQRGYTVKATVRDPNDPKKTEHllALDG-AKERLHL-FKANLLEEGSFDSV-VDGCEGVFHT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  82 ASPFHYNITDAKKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAILdpklsFTGAKKTyteadwsPLTIEDA--YS 159
Cdd:PLN02662   84 ASPFYHDVTDPQAELIDPAVKGTLNVLRSCAKV-PSVKRVVVTSSMAAVA-----YNGKPLT-------PDVVVDEtwFS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 160 NPGLA------YATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGkhKSGLPPT 233
Cdd:PLN02662  151 DPAFCeesklwYVLSKTLAEEAAWKFAKENG--IDMVTINPAMVIGPLLQP-----TLNTSAEAILNLING--AQTFPNA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 234 QLPlWIDVRDVALAHVKAVETQEAANKRIFV-TAGYYSnqELYRILYENFADLrdRLPEeanKGGDPNPALDSFGFDVTR 312
Cdd:PLN02662  222 SYR-WVDVRDVANAHIQAFEIPSASGRYCLVeRVVHYS--EVVKILHELYPTL--QLPE---KCADDKPYVPTYQVSKEK 293
                         330       340
                  ....*....|....*....|...
gi 1111477935 313 ANTiLGIDWIPYENTIIDSVKSL 335
Cdd:PLN02662  294 AKS-LGIEFIPLEVSLKDTVESL 315
FR_SDR_e cd08958
flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended ...
4-291 1.12e-51

flavonoid reductase (FR), extended (e) SDRs; This subgroup contains FRs of the extended SDR-type and related proteins. These FRs act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites; they have the characteristic active site triad of the SDRs (though not the upstream active site Asn) and a NADP-binding motif that is very similar to the typical extended SDR motif. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187661 [Multi-domain]  Cd Length: 293  Bit Score: 172.76  E-value: 1.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVR---SEQKAQSIRhEFQGLgEEKLDFaivpdiaakdaFQG-LGAYG-LEAA 78
Cdd:cd08958     1 VCVTGASGFIGSWLVKRLLQRGYTVRATVRdpgDEKKVAHLL-ELEGA-KERLKL-----------FKAdLLDYGsFDAA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  79 I-------HVASPFHYNITDAKKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAI-LDPKLsftGAKKTYTEADWS 150
Cdd:cd08958    68 IdgcdgvfHVASPVDFDSEDPEEEMIEPAVKGTLNVLEACAKA-KSVKRVVFTSSVAAVvWNPNR---GEGKVVDESCWS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 151 PLtieDAYSNPGLAYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGKhKSGL 230
Cdd:cd08958   144 DL---DFCKKTKLWYALSKTLAEKAAWEFAEENG--LDLVTVNPSLVVGPFLQP-----SLNSSSQLILSLLKGN-AEMY 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111477935 231 PPTQLPlWIDVRDVALAHVKAVETqEAANKRIFVTAGYYSNQELyrilyenFADLRDRLPE 291
Cdd:cd08958   213 QNGSLA-LVHVDDVADAHILLYEK-PSASGRYICSSHVVTRPEL-------AALLAKKYPQ 264
AR_like_SDR_e cd05193
aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This ...
4-309 1.38e-37

aldehyde reductase, flavonoid reductase, and related proteins, extended (e) SDRs; This subgroup contains aldehyde reductase and flavonoid reductase of the extended SDR-type and related proteins. Proteins in this subgroup have a complete SDR-type active site tetrad and a close match to the canonical extended SDR NADP-binding motif. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187536 [Multi-domain]  Cd Length: 295  Bit Score: 136.21  E-value: 1.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQgLGEEKLDFAI-VPDIAAKDAFQGLGAyGLEAAIHVA 82
Cdd:cd05193     1 VLVTGASGFVASHVVEQLLERGYKVRATVRDPSKVKKVNHLLD-LDAKPGRLELaVADLTDEQSFDEVIK-GCAGVFHVA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 SPFHYNITDAkKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAILDPKLSFTGAkkTYTEADWSPLTIEDAYSNPG 162
Cdd:cd05193    79 TPVSFSSKDP-NEVIKPAIGGTLNALKAAAAA-KSVKRFVLTSSAGSVLIPKPNVEGI--VLDEKSWNLEEFDSDPKKSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 163 LAYATSKALAEKAAWDFmADtKPHFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGK--HKSGLPPTQLPLWID 240
Cdd:cd05193   155 WVYAASKTLAEKAAWKF-AD-ENNIDLITVIPTLTIGTIFDS-----ETPSSSGWAMSLITGNegVSPALALIPPGYYVH 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1111477935 241 VRDVALAHVKAVEtQEAANKRIFVTAGYYSNQELyrilyenFADLRDRLPEEANKGGDPNPALDSFGFD 309
Cdd:cd05193   228 VVDICLAHIGCLE-LPIARGRYICTAGNFDWNTL-------LKTLRKKYPSYTFPTDFPDQGQDLSKFS 288
PLN02986 PLN02986
cinnamyl-alcohol dehydrogenase family protein
4-335 1.12e-35

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178567 [Multi-domain]  Cd Length: 322  Bit Score: 131.68  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEKLDFAIVPDIAAKDAFQGlGAYGLEAAIHVAS 83
Cdd:PLN02986    8 VCVTGASGYIASWIVKLLLLRGYTVKATVRDLTDRKKTEHLLALDGAKERLKLFKADLLEESSFEQ-AIEGCDAVFHTAS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  84 PFHYNITDAKKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAILdpklsftgAKKTYTEAdwSPLTIEDAYSNPGL 163
Cdd:PLN02986   87 PVFFTVKDPQTELIDPALKGTINVLNTCKET-PSVKRVILTSSTAAVL--------FRQPPIEA--NDVVDETFFSDPSL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 164 A------YATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGKHksgLPPTQLPL 237
Cdd:PLN02986  156 CretknwYPLSKILAENAAWEFAKDNG--IDMVVLNPGFICGPLLQP-----TLNFSVELIVDFINGKN---LFNNRFYR 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 238 WIDVRDVALAHVKAVETqEAANKRIFVTAGYYSNQELYRILYENFADLrdrLPEEANKGGDPNPALDSFGFDVTRAntiL 317
Cdd:PLN02986  226 FVDVRDVALAHIKALET-PSANGRYIIDGPIMSVNDIIDILRELFPDL---CIADTNEESEMNEMICKVCVEKVKN---L 298
                         330
                  ....*....|....*...
gi 1111477935 318 GIDWIPYENTIIDSVKSL 335
Cdd:PLN02986  299 GVEFTPMKSSLRDTILSL 316
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
3-323 2.24e-35

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 130.10  E-value: 2.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHefqglgEEKLDFAIVpDIAAKDAFQGLgAYGLEAAIHVA 82
Cdd:COG0451     1 RILVTGGAGFIGSHLARRLLARGHEVVGLDRSPPGAANLAA------LPGVEFVRG-DLRDPEALAAA-LAGVDAVVHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 SPFHYNITDAkKDLIDPAVLGTTSVLDALHKTCptVRRVALTSSFAAILDPKLSFTgakktyteadwspltiEDAYSNPG 162
Cdd:COG0451    73 APAGVGEEDP-DETLEVNVEGTLNLLEAARAAG--VKRFVYASSSSVYGDGEGPID----------------EDTPLRPV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 163 LAYATSKALAEKAAWDFMAdtKPHFSLTTICPPMVYGPVKYPVksldsvntSNQLLADILNGK----HKSGLPPTQlplW 238
Cdd:COG0451   134 SPYGASKLAAELLARAYAR--RYGLPVTILRPGNVYGPGDRGV--------LPRLIRRALAGEpvpvFGDGDQRRD---F 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 239 IDVRDVALAHVKAVETQEAANKRIFVTAG-YYSNQELYRILyENFADLRDRLPEEANKGGdpnpaLDSFGFDVTRANTIL 317
Cdd:COG0451   201 IHVDDVARAIVLALEAPAAPGGVYNVGGGePVTLRELAEAI-AEALGRPPEIVYPARPGD-----VRPRRADNSKARREL 274

                  ....*.
gi 1111477935 318 GidWIP 323
Cdd:COG0451   275 G--WRP 278
PLN00198 PLN00198
anthocyanidin reductase; Provisional
3-282 2.42e-32

anthocyanidin reductase; Provisional


Pssm-ID: 215100 [Multi-domain]  Cd Length: 338  Bit Score: 123.07  E-value: 2.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRH--EFQGLGEEKLDFAivpDIAAKDAFQGLGAyGLEAAIH 80
Cdd:PLN00198   11 TACVIGGTGFLASLLIKLLLQKGYAVNTTVRDPENQKKIAHlrALQELGDLKIFGA---DLTDEESFEAPIA-GCDLVFH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  81 VASPFHYNITDAKKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAILDPKLSFTGAkkTYTEADWSPLTIEDAYSN 160
Cdd:PLN00198   87 VATPVNFASEDPENDMIKPAIQGVHNVLKACAKA-KSVKRVILTSSAAAVSINKLSGTGL--VMNEKNWTDVEFLTSEKP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 161 PGLAYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGP--VKYPVKSLD---SVNTSNQLLADILNGKHK-SGLPPtq 234
Cdd:PLN00198  164 PTWGYPASKTLAEKAAWKFAEENN--IDLITVIPTLMAGPslTSDIPSSLSlamSLITGNEFLINGLKGMQMlSGSIS-- 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1111477935 235 lplWIDVRDVALAHVKAVEtQEAANKRIFVTAGYYSNQELYRILYENF 282
Cdd:PLN00198  240 ---ITHVEDVCRAHIFLAE-KESASGRYICCAANTSVPELAKFLIKRY 283
PLN02989 PLN02989
cinnamyl-alcohol dehydrogenase family protein
4-335 2.20e-31

cinnamyl-alcohol dehydrogenase family protein


Pssm-ID: 178569 [Multi-domain]  Cd Length: 325  Bit Score: 120.13  E-value: 2.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEKLDFAIVPDIAAKDAFQgLGAYGLEAAIHVAS 83
Cdd:PLN02989    8 VCVTGASGYIASWIVKLLLFRGYTINATVRDPKDRKKTDHLLALDGAKERLKLFKADLLDEGSFE-LAIDGCETVFHTAS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  84 PFHYNI-TDAKKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAILDPKlsftgakktyTEADWSPLTIEDAYSNPG 162
Cdd:PLN02989   87 PVAITVkTDPQVELINPAVNGTINVLRTCTKV-SSVKRVILTSSMAAVLAPE----------TKLGPNDVVDETFFTNPS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 163 LA------YATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGKHKSGlppTQLP 236
Cdd:PLN02989  156 FAeerkqwYVLSKTLAEDAAWRFAKDNE--IDLIVLNPGLVTGPILQP-----TLNFSVAVIVELMKGKNPFN---TTHH 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 237 LWIDVRDVALAHVKAVETqEAANKRIFVTAGYYSNQELYRILYENFADL--RDRlpeeankgGDPNPALDSFGFDVT--R 312
Cdd:PLN02989  226 RFVDVRDVALAHVKALET-PSANGRYIIDGPVVTIKDIENVLREFFPDLciADR--------NEDITELNSVTFNVCldK 296
                         330       340
                  ....*....|....*....|...
gi 1111477935 313 ANTILGIDWIPYENTIIDSVKSL 335
Cdd:PLN02989  297 VKSLGIIEFTPTETSLRDTVLSL 319
AR_FR_like_1_SDR_e cd05228
uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, ...
4-253 5.91e-27

uncharacterized subgroup of aldehyde reductase and flavonoid reductase related proteins, extended (e) SDRs; This subgroup contains proteins of unknown function related to aldehyde reductase and flavonoid reductase of the extended SDR-type. Aldehyde reductase I (aka carbonyl reductase) is an NADP-binding SDR; it has an NADP-binding motif consensus that is slightly different from the canonical SDR form and lacks the Asn of the extended SDR active site tetrad. Aldehyde reductase I catalyzes the NADP-dependent reduction of ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. The related flavonoid reductases act in the NADP-dependent reduction of flavonoids, ketone-containing plant secondary metabolites. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187539 [Multi-domain]  Cd Length: 318  Bit Score: 108.14  E-value: 5.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAqsirhefQGLGEEKLDFAI--VPDIAA-KDAFQglgayGLEAAIH 80
Cdd:cd05228     1 ILVTGATGFLGSNLVRALLAQGYRVRALVRSGSDA-------VLLDGLPVEVVEgdLTDAASlAAAMK-----GCDRVFH 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  81 VASPFHYNITDAKKdLIDPAVLGTTSVLDALHKTcpTVRRVALTSSFAAILDPklsftgakkTYTEADwspltiEDAYSN 160
Cdd:cd05228    69 LAAFTSLWAKDRKE-LYRTNVEGTRNVLDAALEA--GVRRVVHTSSIAALGGP---------PDGRID------ETTPWN 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 161 P---GLAYATSKALAEKAAWDFMAdtkPHFSLTTICPPMVYGPvkypvksLDSVNTS-NQLLADILNGKHKsGLPPTQLP 236
Cdd:cd05228   131 ErpfPNDYYRSKLLAELEVLEAAA---EGLDVVIVNPSAVFGP-------GDEGPTStGLDVLDYLNGKLP-AYPPGGTS 199
                         250
                  ....*....|....*..
gi 1111477935 237 LwIDVRDVALAHVKAVE 253
Cdd:cd05228   200 F-VDVRDVAEGHIAAME 215
PLN02214 PLN02214
cinnamoyl-CoA reductase
4-335 5.46e-22

cinnamoyl-CoA reductase


Pssm-ID: 177862 [Multi-domain]  Cd Length: 342  Bit Score: 94.82  E-value: 5.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIR-HEFQGlGEEKLdFAIVPDIAAKDAFQGlGAYGLEAAIHVA 82
Cdd:PLN02214   13 VCVTGAGGYIASWIVKILLERGYTVKGTVRNPDDPKNTHlRELEG-GKERL-ILCKADLQDYEALKA-AIDGCDGVFHTA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 SPfhynITDAKKDLIDPAVLGTTSVLDALHKTcpTVRRVALTSSFAAI-LDPKlsfTGAKKTYTEADWSPLtieDAYSNP 161
Cdd:PLN02214   90 SP----VTDDPEQMVEPAVNGAKFVINAAAEA--KVKRVVITSSIGAVyMDPN---RDPEAVVDESCWSDL---DFCKNT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 162 GLAYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGKHKSGLPPTQlpLWIDV 241
Cdd:PLN02214  158 KNWYCYGKMVAEQAAWETAKEKG--VDLVVLNPVLVLGPPLQP-----TINASLYHVLKYLTGSAKTYANLTQ--AYVDV 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 242 RDVALAHVKAVETQEAANKRIFVTAGYYSNQelyriLYENFADLRDRLPEEANKGGDPNPALDSFGFDVTRANTiLGIDW 321
Cdd:PLN02214  229 RDVALAHVLVYEAPSASGRYLLAESARHRGE-----VVEILAKLFPEYPLPTKCKDEKNPRAKPYKFTNQKIKD-LGLEF 302
                         330
                  ....*....|....
gi 1111477935 322 IPYENTIIDSVKSL 335
Cdd:PLN02214  303 TSTKQSLYDTVKSL 316
PLN02650 PLN02650
dihydroflavonol-4-reductase
4-200 4.10e-21

dihydroflavonol-4-reductase


Pssm-ID: 178256 [Multi-domain]  Cd Length: 351  Bit Score: 92.58  E-value: 4.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEKLDFAIVPDIAAKDAFQGlGAYGLEAAIHVAS 83
Cdd:PLN02650    8 VCVTGASGFIGSWLVMRLLERGYTVRATVRDPANVKKVKHLLDLPGATTRLTLWKADLAVEGSFDD-AIRGCTGVFHVAT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  84 PFHYNITDAKKDLIDPAVLGTTSVLDALHKTcPTVRRVALTSSfAAILDPKlsfTGAKKTYTEADWSPLTIEDAYSNPGL 163
Cdd:PLN02650   87 PMDFESKDPENEVIKPTVNGMLSIMKACAKA-KTVRRIVFTSS-AGTVNVE---EHQKPVYDEDCWSDLDFCRRKKMTGW 161
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1111477935 164 AYATSKALAEKAAWDFMADTkpHFSLTTICPPMVYGP 200
Cdd:PLN02650  162 MYFVSKTLAEKAAWKYAAEN--GLDFISIIPTLVVGP 196
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
3-282 2.04e-17

UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of bacterial proteins, and includes the Staphylococcus aureus capsular polysaccharide Cap5N, which may have a role in the synthesis of UDP-N-acetyl-d-fucosamine. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187543 [Multi-domain]  Cd Length: 303  Bit Score: 81.24  E-value: 2.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAqsirhefqglgEEKLDFAIVPDIAAKDAFQGlgayGLEAAIHVA 82
Cdd:cd05232     1 KVLVTGANGFIGRALVDKLLSRGEEVRIAVRNAENA-----------EPSVVLAELPDIDSFTDLFL----GVDAVVHLA 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 SPFHYN---ITDAKKDLIDPAVLGTTSVLDALHKTcpTVRRVALTSSFAAILDPKLSftgakKTYTEaDWSPltiedays 159
Cdd:cd05232    66 ARVHVMndqGADPLSDYRKVNTELTRRLARAAARQ--GVKRFVFLSSVKVNGEGTVG-----APFDE-TDPP-------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 160 NPGLAYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGP-VKYPVKSLdsvntsNQLLadilngkhKSGLPptqLPLW 238
Cdd:cd05232   130 APQDAYGRSKLEAERALLELGASDG--MEVVILRPPMVYGPgVRGNFARL------MRLI--------DRGLP---LPPG 190
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1111477935 239 ID--------VRDVALAHVKAVETQEAANKRIFVTAG-YYSNQELYRILYENF 282
Cdd:cd05232   191 AVknrrslvsLDNLVDAIYLCISLPKAANGTFLVSDGpPVSTAELVDEIRRAL 243
PLN02896 PLN02896
cinnamyl-alcohol dehydrogenase
2-282 5.70e-16

cinnamyl-alcohol dehydrogenase


Pssm-ID: 178484 [Multi-domain]  Cd Length: 353  Bit Score: 77.55  E-value: 5.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   2 TRVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEKLDFAivpDIAAKDAFQGlGAYGLEAAIHV 81
Cdd:PLN02896   11 GTYCVTGATGYIGSWLVKLLLQRGYTVHATLRDPAKSLHLLSKWKEGDRLRLFRA---DLQEEGSFDE-AVKGCDGVFHV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  82 ASPFHYNITDAKKDL--------IDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAiLDPKLSFTGAKKTYTEADWSPlt 153
Cdd:PLN02896   87 AASMEFDVSSDHNNIeeyvqskvIDPAIKGTLNVLKSCLKS-KTVKRVVFTSSIST-LTAKDSNGRWRAVVDETCQTP-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 154 IEDAYSN--PGLAYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPVKYPvksldSVNTSNQLLADILNGKHK--SG 229
Cdd:PLN02896  163 IDHVWNTkaSGWVYVLSKLLTEEAAFKYAKENG--IDLVSVITTTVAGPFLTP-----SVPSSIQVLLSPITGDSKlfSI 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1111477935 230 LPPTQ-----LPLwIDVRDVALAHVKAVEtQEAANKRIFVTAGYYSNQELYRILYENF 282
Cdd:PLN02896  236 LSAVNsrmgsIAL-VHIEDICDAHIFLME-QTKAEGRYICCVDSYDMSELINHLSKEY 291
SDR_e cd08946
extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann ...
4-254 4.61e-15

extended (e) SDRs; Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 212494 [Multi-domain]  Cd Length: 200  Bit Score: 72.72  E-value: 4.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEqkaqsirhefqglgeekldfAIVPdiaakdafqglgaygLEAAIHVAS 83
Cdd:cd08946     1 ILVTGGAGFIGSHLVRRLLERGHEVVVIDRLD--------------------VVVH---------------LAALVGVPA 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  84 PFhynitDAKKDLIDPAVLGTTSVLDALHKTcpTVRRVALTSSFAAildpklsfTGAKKTYTEADWSPLtiedaysNPGL 163
Cdd:cd08946    46 SW-----DNPDEDFETNVVGTLNLLEAARKA--GVKRFVYASSASV--------YGSPEGLPEEEETPP-------RPLS 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 164 AYATSKALAEKAAWDFMADTkpHFSLTTICPPMVYGPvkYPVKSLDSVntSNQLLADILNGKH-KSGLPPTQLPLWIDVR 242
Cdd:cd08946   104 PYGVSKLAAEHLLRSYGESY--GLPVVILRLANVYGP--GQRPRLDGV--VNDFIRRALEGKPlTVFGGGNQTRDFIHVD 177
                         250
                  ....*....|..
gi 1111477935 243 DVALAHVKAVET 254
Cdd:cd08946   178 DVVRAILHALEN 189
PLN02686 PLN02686
cinnamoyl-CoA reductase
4-253 5.51e-15

cinnamoyl-CoA reductase


Pssm-ID: 215370  Cd Length: 367  Bit Score: 74.82  E-value: 5.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRhEFQGLGEEKLDFAIVPDIAAK--------DAFQGlgaygl 75
Cdd:PLN02686   56 VCVTGGVSFLGLAIVDRLLRHGYSVRIAVDTQEDKEKLR-EMEMFGEMGRSNDGIWTVMANltepeslhEAFDG------ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  76 eaaihVASPFHyniTDAkkdLIDPAVL-GTT------------SVLDALHKTcPTVRRVALTSSFAAILdpklsftgAKK 142
Cdd:PLN02686  129 -----CAGVFH---TSA---FVDPAGLsGYTksmaeleakaseNVIEACVRT-ESVRKCVFTSSLLACV--------WRQ 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 143 TYTeADWSPLTIEDAYSNPGLA------YATSKALAEKAAWDfMADTKpHFSLTTICPPMVYGPVKY---PVKSLDSVNT 213
Cdd:PLN02686  189 NYP-HDLPPVIDEESWSDESFCrdnklwYALGKLKAEKAAWR-AARGK-GLKLATICPALVTGPGFFrrnSTATIAYLKG 265
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1111477935 214 SNQLLADilngkhksGLPPTqlplwIDVRDVALAHVKAVE 253
Cdd:PLN02686  266 AQEMLAD--------GLLAT-----ADVERLAEAHVCVYE 292
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
4-262 2.17e-14

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


Pssm-ID: 396097 [Multi-domain]  Cd Length: 238  Bit Score: 71.56  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRseqkaQSIRHEFQGLGEEKLDFAIVPDIAAKDAFqgLGAYGLEAAIHVAS 83
Cdd:pfam01370   1 ILVTGATGFIGSHLVRRLLEKGYEVIGLDR-----LTSASNTARLADLRFVEGDLTDRDALEKL--LADVRPDAVIHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  84 PFHY--NITDAkKDLIDPAVLGTTSVLDALHKTcpTVRRVALTSSfAAILDPKLSFTGAKKTyteadwspLTIEDAYSNP 161
Cdd:pfam01370  74 VGGVgaSIEDP-EDFIEANVLGTLNLLEAARKA--GVKRFLFASS-SEVYGDGAEIPQEETT--------LTGPLAPNSP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 162 glaYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGPvkypvksLDSVNTSNQLLADILNgKHKSGLPP------TQL 235
Cdd:pfam01370 142 ---YAAAKLAGEWLVLAYAAAYG--LRAVILRLFNVYGP-------GDNEGFVSRVIPALIR-RILEGKPIllwgdgTQR 208
                         250       260
                  ....*....|....*....|....*..
gi 1111477935 236 PLWIDVRDVALAHVKAVETQEAANKRI 262
Cdd:pfam01370 209 RDFLYVDDVARAILLALEHGAVKGEIY 235
MupV_like_SDR_e cd05263
Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family ...
4-306 6.34e-12

Pseudomonas fluorescens MupV-like, extended (e) SDRs; This subgroup of extended SDR family domains have the characteristic active site tetrad and a well-conserved NAD(P)-binding motif. This subgroup is not well characterized, its members are annotated as having a variety of putative functions. One characterized member is Pseudomonas fluorescens MupV a protein involved in the biosynthesis of Mupirocin, a polyketide-derived antibiotic. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187573 [Multi-domain]  Cd Length: 293  Bit Score: 65.08  E-value: 6.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEKLDFAIVPDIAAKDAfqGLGA-YGLEAAIHVA 82
Cdd:cd05263     1 VFVTGGTGFLGRHLVKRLLENGFKVLVLVRSESLGEAHERIEEAGLEADRVRVLEGDLTQPNL--GLSAaASRELAGKVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 SPFH----YNITDAKKDLIDPAVLGTTSVLDALHkTCPTVRRVALTSSFAAILdpklsFTGakkTYTEADWSPLTiedAY 158
Cdd:cd05263    79 HVIHcaasYDFQAPNEDAWRTNIDGTEHVLELAA-RLDIQRFHYVSTAYVAGN-----REG---NIRETELNPGQ---NF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 159 SNPglaYATSKALAEKAAWDFMADtkphFSLTTICPPMVYGPVKY-PVKSLDSVNTSNQLLADILNGKHKSGLPPTQLPL 237
Cdd:cd05263   147 KNP---YEQSKAEAEQLVRAAATQ----IPLTVYRPSIVVGDSKTgRIEKIDGLYELLNLLAKLGRWLPMPGNKGARLNL 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111477935 238 wIDVRDVALAHVKAVETQEAANKRIFVTAGyysnqelYRILYENFADL---------RDRLPEEANKGGDPNPALDSF 306
Cdd:cd05263   220 -VPVDYVADAIVYLSKKPEANGQIFHLTDP-------TPQTLREIADLfksaflspgLLVLLMNEPNASLPNALRRSL 289
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
3-262 6.70e-12

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


Pssm-ID: 440466 [Multi-domain]  Cd Length: 215  Bit Score: 64.10  E-value: 6.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHE----FQGlgeeklDFAIVPDIAAkdAFQglgayGLEAA 78
Cdd:COG0702     1 KILVTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAAAgvevVQG------DLDDPESLAA--ALA-----GVDAV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  79 IHVASPFHYNITDAkkdlidpAVLGTTSVLDALHKTcpTVRRVALTSSFAaildpklsftgakktyteadwspltiedAY 158
Cdd:COG0702    68 FLLVPSGPGGDFAV-------DVEGARNLADAAKAA--GVKRIVYLSALG----------------------------AD 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 159 SNPGLAYATSKALAEKAawdfMADTKPHFslTTICPPMVYGpvkypvksldsvNTSNQLLADILNGKHKSGLPPTQLPlW 238
Cdd:COG0702   111 RDSPSPYLRAKAAVEEA----LRASGLPY--TILRPGWFMG------------NLLGFFERLRERGVLPLPAGDGRVQ-P 171
                         250       260
                  ....*....|....*....|....
gi 1111477935 239 IDVRDVALAHVKAVETQEAANKRI 262
Cdd:COG0702   172 IAVRDVAEAAAAALTDPGHAGRTY 195
SDR_a1 cd05265
atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been ...
3-278 3.16e-11

atypical (a) SDRs, subgroup 1; Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187575 [Multi-domain]  Cd Length: 250  Bit Score: 62.69  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKA---QSIRHefqglgeekldfaIVPDIAAKDAfqglgaygLEAAI 79
Cdd:cd05265     2 KILIIGGTRFIGKALVEELLAAGHDVTVFNRGRTKPdlpEGVEH-------------IVGDRNDRDA--------LEELL 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  80 HvASPFHYnitdakkdLIDpaVLGTT--SVLDALHKTCPTVRRVALTSSFAAILDPKLSFTgakktyteaDWSPLTIEDA 157
Cdd:cd05265    61 G-GEDFDV--------VVD--TIAYTprQVERALDAFKGRVKQYIFISSASVYLKPGRVIT---------ESTPLREPDA 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 158 YSNPGLA-YATSKALAEKaawdfMADTKPHFSLTTICPPMVYGPVKYPVKsldsvntSNQLLADILNGK----HKSGLPP 232
Cdd:cd05265   121 VGLSDPWdYGRGKRAAED-----VLIEAAAFPYTIVRPPYIYGPGDYTGR-------LAYFFDRLARGRpilvPGDGHSL 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1111477935 233 TQLplwIDVRDVALAHVKAVETQEAANKrIF--VTAGYYSNQELYRIL 278
Cdd:cd05265   189 VQF---IHVKDLARALLGAAGNPKAIGG-IFniTGDEAVTWDELLEAC 232
UDP_G4E_2_SDR_e cd05234
UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
3-173 2.30e-10

UDP-glucose 4 epimerase, subgroup 2, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup is comprised of archaeal and bacterial proteins, and has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187545 [Multi-domain]  Cd Length: 305  Bit Score: 60.78  E-value: 2.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVV------TTVRSEQKAQSIRHEFQGLGEEKLDFaivPDIAAKDafqglgayGLE 76
Cdd:cd05234     1 RILVTGGAGFIGSHLVDRLLEEGNEVVvvdnlsSGRRENIEPEFENKAFRFVKRDLLDT---ADKVAKK--------DGD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  77 AAIHVASPfhyniTDAKKDLIDPA------VLGTTSVLDALHKTcpTVRRVALTSSfAAIldpklsftgakktYTEADWS 150
Cdd:cd05234    70 TVFHLAAN-----PDVRLGATDPDidleenVLATYNVLEAMRAN--GVKRIVFASS-STV-------------YGEAKVI 128
                         170       180
                  ....*....|....*....|...
gi 1111477935 151 PlTIEDAYSNPGLAYATSKALAE 173
Cdd:cd05234   129 P-TPEDYPPLPISVYGASKLAAE 150
Lys2b COG3320
Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary ...
3-185 1.60e-09

Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs [Secondary metabolites biosynthesis, transport and catabolism]; Thioester reductase domain of alpha aminoadipate reductase Lys2 and NRPSs is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 442549 [Multi-domain]  Cd Length: 265  Bit Score: 57.91  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTT-VRSEQKAQSIRH-----EFQGLGEEKLDFAIVP---DIAAKD------AF 67
Cdd:COG3320     2 TVLLTGATGFLGAHLLRELLRRTDARVYClVRASDEAAARERleallERYGLWLELDASRVVVvagDLTQPRlglseaEF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  68 QGLGAyGLEAAIHVASpfHYNITDAKKDLIDPAVLGTTSVLD-ALHKtcpTVRRVALTSSFAAIldpklSFTGAKKTYTE 146
Cdd:COG3320    82 QELAE-EVDAIVHLAA--LVNLVAPYSELRAVNVLGTREVLRlAATG---RLKPFHYVSTIAVA-----GPADRSGVFEE 150
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1111477935 147 ADwspLTIEDAYSNPglaYATSKALAEKAAWDFMADTKP 185
Cdd:COG3320   151 DD---LDEGQGFANG---YEQSKWVAEKLVREARERGLP 183
UDP_AE_SDR_e cd05256
UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains ...
3-173 5.09e-09

UDP-N-acetylglucosamine 4-epimerase, extended (e) SDRs; This subgroup contains UDP-N-acetylglucosamine 4-epimerase of Pseudomonas aeruginosa, WbpP, an extended SDR, that catalyzes the NAD+ dependent conversion of UDP-GlcNAc and UDPGalNA to UDP-Glc and UDP-Gal. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187566 [Multi-domain]  Cd Length: 304  Bit Score: 56.46  E-value: 5.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVV-----TTVRSEQKAQsirhefqglGEEKLDFaIVPDIAAKDAFQGLGAyGLEA 77
Cdd:cd05256     1 RVLVTGGAGFIGSHLVERLLERGHEVIvldnlSTGKKENLPE---------VKPNVKF-IEGDIRDDELVEFAFE-GVDY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  78 AIHVASpfhynITDAKKDLIDPA------VLGTTSVLDALHKTcpTVRRVALTSSFAAILDPKLsftgakktyteadwSP 151
Cdd:cd05256    70 VFHQAA-----QASVPRSIEDPIkdhevnVLGTLNLLEAARKA--GVKRFVYASSSSVYGDPPY--------------LP 128
                         170       180
                  ....*....|....*....|..
gi 1111477935 152 lTIEDAYSNPGLAYATSKALAE 173
Cdd:cd05256   129 -KDEDHPPNPLSPYAVSKYAGE 149
YfcH COG1090
NAD dependent epimerase/dehydratase family enzyme [General function prediction only];
3-50 3.67e-08

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


Pssm-ID: 440707 [Multi-domain]  Cd Length: 298  Bit Score: 53.92  E-value: 3.67e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGE 50
Cdd:COG1090     1 KILITGGTGFIGSALVAALLARGHEVVVLTRRPPKAPDEVTYVAWDPE 48
3Beta_HSD pfam01073
3-beta hydroxysteroid dehydrogenase/isomerase family; The enzyme 3 beta-hydroxysteroid ...
5-252 4.00e-08

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


Pssm-ID: 366449 [Multi-domain]  Cd Length: 279  Bit Score: 53.52  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   5 LVTGGTGFVAGHVIDALLQRGHsvVTTVRSEQKA--QSIRHEFQGLGEEKLdfaIVPDIAAKD----AFQglgayGLEAA 78
Cdd:pfam01073   1 VVTGGGGFLGRHIIKLLVREGE--LKEVRVFDLResPELLEDFSKSNVIKY---IQGDVTDKDdldnALE-----GVDVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  79 IHVASpfhynITDAKK----DLIDPA-VLGTTSVLDALhkTCPTVRRVALTSSFAAILDPKLS---FTGAKKTYTEadws 150
Cdd:pfam01073  71 IHTAS-----AVDVFGkytfDEIMKVnVKGTQNVLEAC--VKAGVRVLVYTSSAEVVGPNSYGqpiLNGDEETPYE---- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 151 pltiedaySNPGLAYATSKALAEKA-----AWDFMADTKphfsLTTIC--PPMVYGPvkypvksldsvnTSNQLLADILN 223
Cdd:pfam01073 140 --------STHQDAYPRSKAIAEKLvlkanGRPLKNGGR----LYTCAlrPAGIYGE------------GDRLLVPFIVN 195
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1111477935 224 -GKHKSGLP----PTQLPLWIDVRDVALAHVKAV 252
Cdd:pfam01073 196 lAKLGLAKFktgdDNNLSDRVYVGNVAWAHILAA 229
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
3-44 6.49e-08

atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187554 [Multi-domain]  Cd Length: 203  Bit Score: 52.24  E-value: 6.49e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHE 44
Cdd:cd05243     1 KVLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQAEKLEAA 42
SDR_a7 cd05262
atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. ...
3-39 9.90e-08

atypical (a) SDRs, subgroup 7; This subgroup contains atypical SDRs of unknown function. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187572 [Multi-domain]  Cd Length: 291  Bit Score: 52.74  E-value: 9.90e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQ 39
Cdd:cd05262     2 KVFVTGATGFIGSAVVRELVAAGHEVVGLARSDAGAA 38
3b-HSD-like_SDR_e cd05241
3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family ...
3-280 1.70e-07

3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs; Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187552 [Multi-domain]  Cd Length: 331  Bit Score: 52.05  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQR-GHSVVT--TVRSEQKAQSIRHEfqGLGEEKLDFAIVPDIAAKDAfqglgayGLEAAI 79
Cdd:cd05241     1 SVLVTGGSGFFGERLVKQLLERgGTYVRSfdIAPPGEALSAWQHP--NIEFLKGDITDRNDVEQALS-------GADCVF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  80 HVASPFHyniTDAKKDLIDPA-VLGTTSVLDALHKTcpTVRRVALTSSFAAILDPKLSFTGAKKTyteadwsPLTIEDAY 158
Cdd:cd05241    72 HTAAIVP---LAGPRDLYWEVnVGGTQNVLDACQRC--GVQKFVYTSSSSVIFGGQNIHNGDETL-------PYPPLDSD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 159 snpglAYATSKALAEKAAwdfMADTKPHFSLTTICPPM-VYGP-VKYPVKSLDSVntsnqlladILNGKHKSGL-PPTQL 235
Cdd:cd05241   140 -----MYAETKAIAEIIV---LEANGRDDLLTCALRPAgIFGPgDQGLVPILFEW---------AEKGLVKFVFgRGNNL 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1111477935 236 PLWIDVRDVALAHVKA----VETQEAANKRIFVTAGYYSNQ-ELYRILYE 280
Cdd:cd05241   203 VDFTYVHNLAHAHILAaaalVKGKTISGQTYFITDAEPHNMfELLRPVWK 252
GalE COG1087
UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];
3-174 2.24e-07

UDP-glucose 4-epimerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440704 [Multi-domain]  Cd Length: 328  Bit Score: 51.56  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTT---VRSEQKAQSIRHEFqglgeEKLDFAivpDIAA-KDAFQglgAYGLEAA 78
Cdd:COG1087     2 KILVTGGAGYIGSHTVVALLEAGHEVVVLdnlSNGHREAVPKGVPF-----VEGDLR---DRAAlDRVFA---EHDIDAV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  79 IH----------VASPFHY---NITdakkdlidpavlGTTSVLDALHKTCptVRRVALTSSfAAildpklsftgakkTYT 145
Cdd:COG1087    71 IHfaalkavgesVEKPLKYyrnNVV------------GTLNLLEAMREAG--VKRFVFSSS-AA-------------VYG 122
                         170       180
                  ....*....|....*....|....*....
gi 1111477935 146 EADWSPLTiEDAYSNPGLAYATSKALAEK 174
Cdd:COG1087   123 EPESVPIT-EDAPTNPTNPYGRSKLMVEQ 150
NAD_binding_4 pfam07993
Male sterility protein; This family represents the C-terminal region of the male sterility ...
6-199 5.70e-07

Male sterility protein; This family represents the C-terminal region of the male sterility protein in a number of arabidopsis and drosophila. A sequence-related jojoba acyl CoA reductase is also included.


Pssm-ID: 462334 [Multi-domain]  Cd Length: 257  Bit Score: 49.92  E-value: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   6 VTGGTGFVAGHVIDALLqRGHSVVTTV------RSEQKAQS-IRHEFQ--GLGEEKLDFA---IVP---DIA------AK 64
Cdd:pfam07993   1 LTGATGFLGKVLLEKLL-RSTPDVKKIyllvraKDGESALErLRQELEkyPLFDALLKEAlerIVPvagDLSepnlglSE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  65 DAFQGLGAyGLEAAIHVASPfhYNITDAKKDLIDPAVLGTTSVLDaLHKTCPTVRRVALTSSfaAILDPKLSFTGAKKTY 144
Cdd:pfam07993  80 EDFQELAE-EVDVIIHSAAT--VNFVEPYDDARAVNVLGTREVLR-LAKQGKQLKPFHHVST--AYVNGERGGLVEEKPY 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111477935 145 TEADWSPLTIEDA------YSNPglaYATSKALAEKAAWDFMADTKPhfsLTTICPPMVYG 199
Cdd:pfam07993 154 PEGEDDMLLDEDEpallggLPNG---YTQTKWLAEQLVREAARRGLP---VVIYRPSIITG 208
NDUFA9_like_SDR_a cd05271
NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, ...
3-279 6.55e-07

NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, subunit 9, 39 kDa, (NDUFA9) -like, atypical (a) SDRs; This subgroup of extended SDR-like proteins are atypical SDRs. They have a glycine-rich NAD(P)-binding motif similar to the typical SDRs, GXXGXXG, and have the YXXXK active site motif (though not the other residues of the SDR tetrad). Members identified include NDUFA9 (mitochondrial) and putative nucleoside-diphosphate-sugar epimerase. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187579 [Multi-domain]  Cd Length: 273  Bit Score: 49.94  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQkaQSIRHEFQGLgeekldfaivpdiaakdafqgLGAYgleaaihva 82
Cdd:cd05271     2 VVTVFGATGFIGRYVVNRLAKRGSQVIVPYRCEA--YARRLLVMGD---------------------LGQV--------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 SPFHYNITDakKDLIDPAVLGTTSVLDALHKTCPTVRRvaltsSFAAIldpklSFTGAKKTyteADW------------S 150
Cdd:cd05271    50 LFVEFDLRD--DESIRKALEGSDVVINLVGRLYETKNF-----SFEDV-----HVEGPERL---AKAakeagverlihiS 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 151 PLtieDAYSNPGLAYATSKALAEKAawdfmadTKPHFSLTTIC-PPMVYGPVKYPVKSLDSVNTSNQLLADILNGKHKSg 229
Cdd:cd05271   115 AL---GADANSPSKYLRSKAEGEEA-------VREAFPEATIVrPSVVFGREDRFLNRFAKLLAFLPFPPLIGGGQTKF- 183
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1111477935 230 lpptQlPLWIDvrDVALAHVKAVETQEAANKRI-FVTAGYYSNQELYRILY 279
Cdd:cd05271   184 ----Q-PVYVG--DVAEAIARALKDPETEGKTYeLVGPKVYTLAELVELLR 227
3b-HSD-NSDHL-like_SDR_e cd09813
human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This ...
3-264 6.83e-07

human NSDHL (NAD(P)H steroid dehydrogenase-like protein)-like, extended (e) SDRs; This subgroup includes human NSDHL and related proteins. These proteins have the characteristic active site tetrad of extended SDRs, and also have a close match to their NAD(P)-binding motif. Human NSDHL is a 3beta-hydroxysteroid dehydrogenase (3 beta-HSD) which functions in the cholesterol biosynthetic pathway. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. Mutations in the gene encoding NSDHL cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. This subgroup also includes an unusual bifunctional [3beta-hydroxysteroid dehydrogenase (3b-HSD)/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187673 [Multi-domain]  Cd Length: 335  Bit Score: 50.43  E-value: 6.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHsvvTTVRseqkAQSIRHEFQGLGEEKLDFA-IVPDIAAK-DAFQGLGAYGLEAAIH 80
Cdd:cd09813     1 SCLVVGGSGFLGRHLVEQLLRRGN---PTVH----VFDIRPTFELDPSSSGRVQfHTGDLTDPqDLEKAFNEKGPNVVFH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  81 VASPFHyNITDAKKDLIDpaVLGTTSVLDALHKtcPTVRRVALTSSFAAILDpklsftgaKKTYTEADWSPLTIEDAYSn 160
Cdd:cd09813    74 TASPDH-GSNDDLYYKVN--VQGTRNVIEACRK--CGVKKLVYTSSASVVFN--------GQDIINGDESLPYPDKHQD- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 161 pglAYATSKALAEKAAwdfMADTKPHFSLTTIC--PPMVYGPvkypvkslDSVNTSNQLLADILNGKHKSGL-PPTQLPL 237
Cdd:cd09813   140 ---AYNETKALAEKLV---LKANDPESGLLTCAlrPAGIFGP--------GDRQLVPGLLKAAKNGKTKFQIgDGNNLFD 205
                         250       260
                  ....*....|....*....|....*..
gi 1111477935 238 WIDVRDVALAHVKAVETQEAANKRIFV 264
Cdd:cd09813   206 FTYVENVAHAHILAADALLSSSHAETV 232
SDR_e_a cd05226
Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases ...
4-126 7.47e-07

Extended (e) and atypical (a) SDRs; Extended or atypical short-chain dehydrogenases/reductases (SDRs, aka tyrosine-dependent oxidoreductases) are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187537 [Multi-domain]  Cd Length: 176  Bit Score: 48.55  E-value: 7.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAqsIRHEFQGLGEEKLDFAivPDIAAKDAFQglgayGLEAAIHVAS 83
Cdd:cd05226     1 ILILGATGFIGRALARELLEQGHEVTLLVRNTKRL--SKEDQEPVAVVEGDLR--DLDSLSDAVQ-----GVDVVIHLAG 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1111477935  84 PFHYnitdaKKDLIDPAVLGTTSVLDALHKTCptVRRVALTSS 126
Cdd:cd05226    72 APRD-----TRDFCEVDVEGTRNVLEAAKEAG--VKHFIFISS 107
SDR_a8 cd05242
atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. ...
3-150 1.05e-06

atypical (a) SDRs, subgroup 8; This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187553 [Multi-domain]  Cd Length: 296  Bit Score: 49.53  E-value: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEKLDFAIVpdiaakdafqglgayGLEAAIHVA 82
Cdd:cd05242     1 KIVITGGTGFIGRALTRRLTAAGHEVVVLSRRPGKAEGLAEVITWDGLSLGPWELP---------------GADAVINLA 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1111477935  83 SpfhYNI-----TDAKKDLIDPAVLGTTSVLDALHKTCPTVRRVALTSSFAAILDPKLSftgakKTYTEADWS 150
Cdd:cd05242    66 G---EPIacrrwTEANKKEILSSRIESTRVLVEAIANAPAPPKVLISASAVGYYGHSGD-----EVLTENSPS 130
yfcH TIGR01777
TIGR01777 family protein; This model represents a clade of proteins of unknown function ...
4-151 1.35e-06

TIGR01777 family protein; This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved]


Pssm-ID: 273800 [Multi-domain]  Cd Length: 291  Bit Score: 49.18  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAqsirhefqglgeeKLDFAIVPDIAAKDAFQGLGayGLEAAIHVA- 82
Cdd:TIGR01777   1 ILITGGTGFIGRALTQRLTKRGHEVTILTRSPPPG-------------ANTKWEGYKPWAGEDADSLE--GADAVINLAg 65
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  83 -SPFHYNITDAKKDLIDPAVLGTTSVLDALHKTCPTVRRVALTSSFAAILDPKLSftgakKTYTEADWSP 151
Cdd:TIGR01777  66 ePIADKRWTEERKQEIRDSRIDTTRLLVEAIAAAEQKPKVFISASAVGYYGPSED-----REYTEEDSPA 130
UDP_G4E_3_SDR_e cd05240
UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial ...
4-253 1.66e-06

UDP-glucose 4 epimerase (G4E), subgroup 3, extended (e) SDRs; Members of this bacterial subgroup are identified as possible sugar epimerases, such as UDP-glucose 4 epimerase. However, while the NAD(P)-binding motif is fairly well conserved, not all members retain the canonical active site tetrad of the extended SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187551 [Multi-domain]  Cd Length: 306  Bit Score: 48.90  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQ--RGHSVVTTVRSEQKAQSIRHEFQGLgeekldfaivpDIAAKDAFQGLGAYGLEAAIHV 81
Cdd:cd05240     1 ILVTGAAGGLGRLLARRLAAspRVIGVDGLDRRRPPGSPPKVEYVRL-----------DIRDPAAADVFREREADAVVHL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  82 ASPFHYNITDAKKDLIDpaVLGTTSVLDALHKTcpTVRRVALTSSFAAildpklsftgakktYTEADWSPLTI-EDA--Y 158
Cdd:cd05240    70 AFILDPPRDGAERHRIN--VDGTQNVLDACAAA--GVPRVVVTSSVAV--------------YGAHPDNPAPLtEDAplR 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 159 SNPGLAYATSKALAEKAAWDFMADtKPHFSLTTICPPMVYGPvkypvksldsvNTSNQlLADILNGKHKSGL----PPTQ 234
Cdd:cd05240   132 GSPEFAYSRDKAEVEQLLAEFRRR-HPELNVTVLRPATILGP-----------GTRNT-TRDFLSPRRLPVPggfdPPFQ 198
                         250
                  ....*....|....*....
gi 1111477935 235 LpLWIDvrDVALAHVKAVE 253
Cdd:cd05240   199 F-LHED--DVARALVLAVR 214
3b-HSD_HSDB1_like_SDR_e cd09811
human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, ...
5-175 3.68e-06

human 3beta-HSD (hydroxysteroid dehydrogenase) and HSD3B1(delta 5-delta 4-isomerase)-like, extended (e) SDRs; This extended-SDR subgroup includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7], and related proteins. These proteins have the characteristic active site tetrad and NAD(P)-binding motif of extended SDRs. 3 beta-HSD catalyzes the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration; this activity is essential for the biosynthesis of all classes of hormonal steroids. C(27) 3beta-HSD is a membrane-bound enzyme of the endoplasmic reticulum, it catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187671 [Multi-domain]  Cd Length: 354  Bit Score: 48.27  E-value: 3.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   5 LVTGGTGFVAGHVIDALLQRGHSvVTTVRSEQKA---QSIRHEFQGLGEEKL-----DFAIVPDIAAKDAfqglgayGLE 76
Cdd:cd09811     3 LVTGGGGFLGQHIIRLLLERKEE-LKEIRVLDKAfgpELIEHFEKSQGKTYVtdiegDIKDLSFLFRACQ-------GVS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  77 AAIHVASPFHYNITDAKKDLIDPAVLGTTSVLDALHKTcpTVRRVALTSSFAAILDP---KLSFTGAKKTYTEADWSPlt 153
Cdd:cd09811    75 VVIHTAAIVDVFGPPNYEELEEVNVNGTQAVLEACVQN--NVKRLVYTSSIEVAGPNfkgRPIFNGVEDTPYEDTSTP-- 150
                         170       180
                  ....*....|....*....|..
gi 1111477935 154 iedaysnpglAYATSKALAEKA 175
Cdd:cd09811   151 ----------PYASSKLLAENI 162
Arna_like_SDR_e cd05257
Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme ...
3-200 4.77e-06

Arna decarboxylase_like, extended (e) SDRs; Decarboxylase domain of ArnA. ArnA, is an enzyme involved in the modification of outer membrane protein lipid A of gram-negative bacteria. It is a bifunctional enzyme that catalyzes the NAD-dependent decarboxylation of UDP-glucuronic acid and N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-l-arabinose; its NAD-dependent decaboxylating activity is in the C-terminal 360 residues. This subgroup belongs to the extended SDR family, however the NAD binding motif is not a perfect match and the upstream Asn of the canonical active site tetrad is not conserved. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187567 [Multi-domain]  Cd Length: 316  Bit Score: 47.68  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSvvttVRSEQKAQSIRHEFQGLGEEKLDFAIVP-DIaaKDAFQGLGAY-GLEAAIH 80
Cdd:cd05257     1 NVLVTGADGFIGSHLTERLLREGHE----VRALDIYNSFNSWGLLDNAVHDRFHFISgDV--RDASEVEYLVkKCDVVFH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  81 VAS----PFHYNitdAKKDLIDPAVLGTTSVLDALHKTcpTVRRVALTSSfaaildpklsftgaKKTYTEADWSPLTIED 156
Cdd:cd05257    75 LAAliaiPYSYT---APLSYVETNVFGTLNVLEAACVL--YRKRVVHTST--------------SEVYGTAQDVPIDEDH 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1111477935 157 ---AYSNPGLAYATSKALAEKAAWDFMAdtkpHFSL--TTICPPMVYGP 200
Cdd:cd05257   136 pllYINKPRSPYSASKQGADRLAYSYGR----SFGLpvTIIRPFNTYGP 180
UDP_G4E_1_SDR_e cd05247
UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
3-335 7.28e-06

UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs; UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187558 [Multi-domain]  Cd Length: 323  Bit Score: 47.14  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVV-------TTVRSEQKAQSIRHEF-QG--LGEEKLDfaivpdiaakDAFQglgA 72
Cdd:cd05247     1 KVLVTGGAGYIGSHTVVELLEAGYDVVvldnlsnGHREALPRIEKIRIEFyEGdiRDRAALD----------KVFA---E 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  73 YGLEAAIHVAspfhynitdAKKDL----IDPA------VLGTTSVLDALHKTcpTVRRVALTSSfAAildpklsftgakk 142
Cdd:cd05247    68 HKIDAVIHFA---------ALKAVgesvQKPLkyydnnVVGTLNLLEAMRAH--GVKNFVFSSS-AA------------- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 143 TYTEADWSPLTiEDAYSNPGLAYATSKALAEKAAWDFmaDTKPHFSLTTicppmvygpVKY--PVksldsvntsnqllad 220
Cdd:cd05247   123 VYGEPETVPIT-EEAPLNPTNPYGRTKLMVEQILRDL--AKAPGLNYVI---------LRYfnPA--------------- 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 221 ilnGKHKSGL------PPTQL-PL-----------------------------WIDVRDVALAHVKAVETQEAANKRIFV 264
Cdd:cd05247   176 ---GAHPSGLigedpqIPNNLiPYvlqvalgrreklaifgddyptpdgtcvrdYIHVVDLADAHVLALEKLENGGGSEIY 252
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 265 TAGY---YSNQELYR---------ILYEnFADLRdrlpeeankGGDPnPALDSfgfDVTRANTILGidWIPyENTIIDSV 332
Cdd:cd05247   253 NLGTgrgYSVLEVVEafekvsgkpIPYE-IAPRR---------AGDP-ASLVA---DPSKAREELG--WKP-KRDLEDMC 315

                  ...
gi 1111477935 333 KSL 335
Cdd:cd05247   316 EDA 318
PLN02206 PLN02206
UDP-glucuronate decarboxylase
3-133 1.13e-05

UDP-glucuronate decarboxylase


Pssm-ID: 177856 [Multi-domain]  Cd Length: 442  Bit Score: 46.90  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVT-----TVRSEqkaqSIRHEFQGLGEEKLDFAIV-PDIAAKDAFQGLGAygle 76
Cdd:PLN02206  121 RVVVTGGAGFVGSHLVDRLMARGDSVIVvdnffTGRKE----NVMHHFSNPNFELIRHDVVePILLEVDQIYHLAC---- 192
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1111477935  77 aaihVASPFHYNITDAKKdlIDPAVLGTTSVLdALHKTCPTvrRVALTSSFAAILDP 133
Cdd:PLN02206  193 ----PASPVHYKFNPVKT--IKTNVVGTLNML-GLAKRVGA--RFLLTSTSEVYGDP 240
PLN02583 PLN02583
cinnamoyl-CoA reductase
4-200 1.47e-05

cinnamoyl-CoA reductase


Pssm-ID: 178195 [Multi-domain]  Cd Length: 297  Bit Score: 45.86  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQsIRHEFQGLG--EEKL--------DF-AIVpdiaakDAFQGLGA 72
Cdd:PLN02583    9 VCVMDASGYVGFWLVKRLLSRGYTVHAAVQKNGETE-IEKEIRGLSceEERLkvfdvdplDYhSIL------DALKGCSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  73 --YGLEaaihvaSPFHYNITDAKkdLIDPAVLGTTSVLDALHKTcPTVRRVALTSSFAAIL---DPKlsftGAKKTYTEA 147
Cdd:PLN02583   82 lfCCFD------PPSDYPSYDEK--MVDVEVRAAHNVLEACAQT-DTIEKVVFTSSLTAVIwrdDNI----STQKDVDER 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1111477935 148 DWSPLTIEDAYSnpgLAYATSKALAEKAAWDFMADTKphFSLTTICPPMVYGP 200
Cdd:PLN02583  149 SWSDQNFCRKFK---LWHALAKTLSEKTAWALAMDRG--VNMVSINAGLLMGP 196
UGD_SDR_e cd05230
UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the ...
3-109 2.04e-05

UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs; UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187541 [Multi-domain]  Cd Length: 305  Bit Score: 45.71  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVV-------------TTVRSEQKAQSIRHEFQGLGEEKLDFAIvpDIAAKdafqg 69
Cdd:cd05230     2 RILITGGAGFLGSHLCDRLLEDGHEVIcvdnfftgrkrniEHLIGHPNFEFIRHDVTEPLYLEVDQIY--HLACP----- 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1111477935  70 lgaygleaaihvASPFHYnitdaKKD---LIDPAVLGTTSVLD 109
Cdd:cd05230    75 ------------ASPVHY-----QYNpikTLKTNVLGTLNMLG 100
SDR_a2 cd05245
atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified ...
4-37 3.61e-05

atypical (a) SDRs, subgroup 2; This subgroup contains atypical SDRs, one member is identified as Escherichia coli protein ybjT, function unknown. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif consensus that generally matches the extended SDRs, TGXXGXXG, but lacks the characteristic active site residues of the SDRs. This subgroup has basic residues (HXXXR) in place of the active site motif YXXXK, these may have a catalytic role. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187556 [Multi-domain]  Cd Length: 293  Bit Score: 44.64  E-value: 3.61e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQK 37
Cdd:cd05245     1 VLVTGATGYVGGRLVPRLLQEGHQVRALVRSPEK 34
GDP_MD_SDR_e cd05260
GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, ...
3-119 3.97e-05

GDP-mannose 4,6 dehydratase, extended (e) SDRs; GDP-mannose 4,6 dehydratase, a homodimeric SDR, catalyzes the NADP(H)-dependent conversion of GDP-(D)-mannose to GDP-4-keto, 6-deoxy-(D)-mannose in the fucose biosynthesis pathway. These proteins have the canonical active site triad and NAD-binding pattern, however the active site Asn is often missing and may be substituted with Asp. A Glu residue has been identified as an important active site base. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187570 [Multi-domain]  Cd Length: 316  Bit Score: 44.90  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQgLGEEKLDFAIVPDIAakDAFQGLGA---------Y 73
Cdd:cd05260     1 RALITGITGQDGSYLAEFLLEKGYEVHGIVRRSSSFNTDRIDHL-YINKDRITLHYGDLT--DSSSLRRAiekvrpdeiY 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1111477935  74 GLEAAIHVASPFhynitDAKKDLIDPAVLGTTSVLDALHKTCPTVR 119
Cdd:cd05260    78 HLAAQSHVKVSF-----DDPEYTAEVNAVGTLNLLEAIRILGLDAR 118
YwnB COG2910
Putative NADH-flavin reductase [General function prediction only];
3-133 6.35e-05

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


Pssm-ID: 442154 [Multi-domain]  Cd Length: 205  Bit Score: 43.31  E-value: 6.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAqSIRHEfqGLGeekldfAIVPDIAAKDAFQGLgAYGLEAAIHVA 82
Cdd:COG2910     1 KIAVIGATGRVGSLIVREALARGHEVTALVRNPEKL-PDEHP--GLT------VVVGDVLDPAAVAEA-LAGADAVVSAL 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1111477935  83 SPFHYNITDakkDLIDpavlGTTSVLDALHKTCptVRRVALTSSfAAILDP 133
Cdd:COG2910    71 GAGGGNPTT---VLSD----GARALIDAMKAAG--VKRLIVVGG-AGSLDV 111
GDP_Man_Dehyd pfam16363
GDP-mannose 4,6 dehydratase;
5-127 6.88e-05

GDP-mannose 4,6 dehydratase;


Pssm-ID: 465104 [Multi-domain]  Cd Length: 327  Bit Score: 44.08  E-value: 6.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   5 LVTGGTGFVAGHVIDALLQRGHSVVTTVR--SEQKAQSIRHEFQGLGEEKLDFAIVpDIAAKDAFQGLGA-------YGL 75
Cdd:pfam16363   1 LITGITGQDGSYLAELLLEKGYEVHGIVRrsSSFNTGRLEHLYDDHLNGNLVLHYG-DLTDSSNLVRLLAevqpdeiYNL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1111477935  76 EAAIHVA----SPFHYNITDakkdlidpaVLGTTSVLDAlhktcptVRRVALTSSF 127
Cdd:pfam16363  80 AAQSHVDvsfeQPEYTADTN---------VLGTLRLLEA-------IRSLGLEKKV 119
PLN02166 PLN02166
dTDP-glucose 4,6-dehydratase
3-133 1.09e-04

dTDP-glucose 4,6-dehydratase


Pssm-ID: 165812 [Multi-domain]  Cd Length: 436  Bit Score: 43.85  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVT-----TVRSEqkaqSIRHEFQGLGEEKLDFAIV-PDIAAKDAFQGLGAygle 76
Cdd:PLN02166  122 RIVVTGGAGFVGSHLVDKLIGRGDEVIVidnffTGRKE----NLVHLFGNPRFELIRHDVVePILLEVDQIYHLAC---- 193
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1111477935  77 aaihVASPFHYNITDAKKdlIDPAVLGTTSVLdALHKTCPTvrRVALTSSFAAILDP 133
Cdd:PLN02166  194 ----PASPVHYKYNPVKT--IKTNVMGTLNML-GLAKRVGA--RFLLTSTSEVYGDP 241
TMR_SDR_a cd05269
triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an ...
5-129 2.09e-04

triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs; TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187578 [Multi-domain]  Cd Length: 272  Bit Score: 42.26  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   5 LVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQsirhEFQGLGEE--KLDFAIVPDIAAkdAFQglgayGLEAAIHVA 82
Cdd:cd05269     2 LVTGATGKLGTAVVELLLAKVASVVALVRNPEKAK----AFAADGVEvrQGDYDDPETLER--AFE-----GVDRLLLIS 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1111477935  83 SPFHYNITDAKKDLIDPAV-LGttsvldalhktcptVRRVALTSSFAA 129
Cdd:cd05269    71 PSDLEDRIQQHKNFIDAAKqAG--------------VKHIVYLSASGA 104
Polysacc_synt_2 pfam02719
Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide ...
4-110 2.15e-04

Polysaccharide biosynthesis protein; This is a family of diverse bacterial polysaccharide biosynthesis proteins including the CapD protein, WalL protein mannosyl-transferase and several putative epimerases (e.g. WbiI).


Pssm-ID: 426938 [Multi-domain]  Cd Length: 284  Bit Score: 42.50  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRG-HSVVTTVRSEQKAQSIRHEF-QGLGEEKLDFAIVPDIA-AKDA---FQGLGAYGLEA 77
Cdd:pfam02719   1 VLVTGGGGSIGSELCRQILKFNpKKIILFSRDELKLYEIRQELrEKFNDPKLRFFIVPVIGdVRDRerlERAMEQYGVDV 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1111477935  78 AIHVASPFH-----YNITDAkkdlIDPAVLGTTSVLDA 110
Cdd:pfam02719  81 VFHAAAYKHvplveYNPMEA----IKTNVLGTENVADA 114
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
3-36 2.32e-04

dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; dTDP-6-deoxy-L-lyxo-4-hexulose reductase, an extended SDR, synthesizes dTDP-L-rhamnose from alpha-D-glucose-1-phosphate, providing the precursor of L-rhamnose, an essential cell wall component of many pathogenic bacteria. This subgroup has the characteristic active site tetrad and NADP-binding motif. This subgroup also contains human MAT2B, the regulatory subunit of methionine adenosyltransferase (MAT); MAT catalyzes S-adenosylmethionine synthesis. The human gene encoding MAT2B encodes two major splicing variants which are induced in human cell liver cancer and regulate HuR, an mRNA-binding protein which stabilizes the mRNA of several cyclins, to affect cell proliferation. Both MAT2B variants include this extended SDR domain. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187564 [Multi-domain]  Cd Length: 280  Bit Score: 42.23  E-value: 2.32e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQ 36
Cdd:cd05254     1 KILITGATGMLGRALVRLLKERGYEVIGTGRSRA 34
UDP_invert_4-6DH_SDR_e cd05237
UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; ...
3-126 2.40e-04

UDP-Glcnac (UDP-linked N-acetylglucosamine) inverting 4,6-dehydratase, extended (e) SDRs; UDP-Glcnac inverting 4,6-dehydratase was identified in Helicobacter pylori as the hexameric flaA1 gene product (FlaA1). FlaA1 is hexameric, possesses UDP-GlcNAc-inverting 4,6-dehydratase activity, and catalyzes the first step in the creation of a pseudaminic acid derivative in protein glycosylation. Although this subgroup has the NADP-binding motif characteristic of extended SDRs, its members tend to have a Met substituted for the active site Tyr found in most SDR families. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187548 [Multi-domain]  Cd Length: 287  Bit Score: 42.22  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTV-RSEQKAQSIRHEFQGLG-EEKLDFAIVpDIAAKDAFQGLGA-YGLEAAI 79
Cdd:cd05237     4 TILVTGGAGSIGSELVRQILKFGPKKLIVFdRDENKLHELVRELRSRFpHDKLRFIIG-DVRDKERLRRAFKeRGPDIVF 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1111477935  80 HVASPFH-----YNITDAkkdlIDPAVLGTTSVLDALHKtCPtVRRVALTSS 126
Cdd:cd05237    83 HAAALKHvpsmeDNPEEA----IKTNVLGTKNVIDAAIE-NG-VEKFVCIST 128
Thioester-redct TIGR01746
thioester reductase domain; This model includes the terminal domain from the fungal alpha ...
4-174 2.40e-04

thioester reductase domain; This model includes the terminal domain from the fungal alpha aminoadipate reductase enzyme (also known as aminoadipate semialdehyde dehydrogenase) which is involved in the biosynthesis of lysine, as well as the reductase-containing component of the myxochelin biosynthetic gene cluster, MxcG. The mechanism of reduction involves activation of the substrate by adenylation and transfer to a covalently-linked pantetheine cofactor as a thioester. This thioester is then reduced to give an aldehyde (thus releasing the product) and a regenerated pantetheine thiol. (In myxochelin biosynthesis this aldehyde is further reduced to an alcohol or converted to an amine by an aminotransferase.) This is a fundamentally different reaction than beta-ketoreductase domains of polyketide synthases which act at a carbonyl two carbons removed from the thioester and forms an alcohol as a product. This domain is invariably found at the C-terminus of the proteins which contain it (presumably because it results in the release of the product). The majority of hits to this model are non-ribosomal peptide synthetases in which this domain is similarly located proximal to a thiolation domain (pfam00550). In some cases this domain is found at the end of a polyketide synthetase enzyme, but is unlike ketoreductase domains which are found before the thiolase domains. Exceptions to this observed relationship with the thiolase domain include three proteins which consist of stand-alone reductase domains (GP|466833 from M. leprae, GP|435954 from Anabaena and OMNI|NTL02SC1199 from Strep. coelicolor) and one protein (OMNI|NTL01NS2636 from Nostoc) which contains N-terminal homology with a small group of hypothetical proteins but no evidence of a thiolation domain next to the putative reductase domain. Below the noise cutoff to this model are proteins containing more distantly related ketoreductase and dehydratase/epimerase domains. It has been suggested that a NADP-binding motif can be found in the N-terminal portion of this domain that may form a Rossman-type fold.


Pssm-ID: 273787 [Multi-domain]  Cd Length: 367  Bit Score: 42.40  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGH--SVVTTVR--SEQKAQS-IRHEF--QGLGEEKLDFAIVPDIAAKDAFQGLgayGLE 76
Cdd:TIGR01746   2 VLLTGATGFLGAYLLEELLRRSTraKVICLVRadSEEHAMErLREALrsYRLWHENLAMERIEVVAGDLSKPRL---GLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  77 AA------------IHVASPFHYNITDAKkdLIDPAVLGTTSVLD--ALHKTCPtvrrvaltssfaaildpkLSF--TGA 140
Cdd:TIGR01746  79 DAewerlaenvdtiVHNGALVNHVYPYSE--LRGANVLGTVEVLRlaASGRAKP------------------LHYvsTIS 138
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1111477935 141 KKTYTEADWSPLTIEDAYSNPGL---AYATSKALAEK 174
Cdd:TIGR01746 139 VGAAIDLSTGVTEDDATVTPYPGlagGYTQSKWVAEL 175
RfbD COG1091
dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];
3-35 3.55e-04

dTDP-4-dehydrorhamnose reductase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440708 [Multi-domain]  Cd Length: 279  Bit Score: 41.66  E-value: 3.55e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSE 35
Cdd:COG1091     1 RILVTGANGQLGRALVRLLAERGYEVVALDRSE 33
WbmH_like_SDR_e cd08957
Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella ...
3-29 5.47e-04

Bordetella bronchiseptica enzymes WbmH and WbmG-like, extended (e) SDRs; Bordetella bronchiseptica enzymes WbmH and WbmG, and related proteins. This subgroup exhibits the active site tetrad and NAD-binding motif of the extended SDR family. It has been proposed that the active site in Bordetella WbmG and WbmH cannot function as an epimerase, and that it plays a role in O-antigen synthesis pathway from UDP-2,3-diacetamido-2,3-dideoxy-l-galacturonic acid. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187660 [Multi-domain]  Cd Length: 307  Bit Score: 41.33  E-value: 5.47e-04
                          10        20
                  ....*....|....*....|....*..
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVV 29
Cdd:cd08957     2 KVLITGGAGQIGSHLIEHLLERGHQVV 28
UDP_G4E_5_SDR_e cd05264
UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially ...
3-29 5.83e-04

UDP-glucose 4-epimerase (G4E), subgroup 5, extended (e) SDRs; This subgroup partially conserves the characteristic active site tetrad and NAD-binding motif of the extended SDRs, and has been identified as possible UDP-glucose 4-epimerase (aka UDP-galactose 4-epimerase), a homodimeric member of the extended SDR family. UDP-glucose 4-epimerase catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187574 [Multi-domain]  Cd Length: 300  Bit Score: 41.15  E-value: 5.83e-04
                          10        20
                  ....*....|....*....|....*..
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVV 29
Cdd:cd05264     1 RVLIVGGNGFIGSHLVDALLEEGPQVR 27
NAD_binding_10 pfam13460
NAD(P)H-binding;
8-69 6.08e-04

NAD(P)H-binding;


Pssm-ID: 463885 [Multi-domain]  Cd Length: 183  Bit Score: 40.28  E-value: 6.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1111477935   8 GGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRhefQGLGEE--KLDFAIVPDIAAkdAFQG 69
Cdd:pfam13460   1 GATGKIGRLLVKQLLARGHEVTALVRNPEKLADLE---DHPGVEvvDGDVLDPDDLAE--ALAG 59
NmrA pfam05368
NmrA-like family; NmrA is a negative transcriptional regulator involved in the ...
4-51 6.98e-04

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


Pssm-ID: 398829 [Multi-domain]  Cd Length: 236  Bit Score: 40.40  E-value: 6.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1111477935   4 VLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSirHEFQGLGEE 51
Cdd:pfam05368   1 ILVFGATGQQGGSVVRASLKAGHKVRALVRDPKSELA--KSLKEAGVE 46
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-77 7.50e-04

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 40.62  E-value: 7.50e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1111477935   1 MTRVLVTGGTGFVAGHVIDALLQRGHSVVTTVRS-EQKAQSIRHEFQGLGEEKLdfAIVPDIAAKDAFQGLGAYGLEA 77
Cdd:PRK12825    6 GRVALVTGAARGLGRAIALRLARAGADVVVHYRSdEEAAEELVEAVEALGRRAQ--AVQADVTDKAALEAAVAAAVER 81
GME-like_SDR_e cd05273
Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup ...
3-29 1.16e-03

Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME)-like, extended (e) SDRs; This subgroup of NDP-sugar epimerase/dehydratases are extended SDRs; they have the characteristic active site tetrad, and an NAD-binding motif: TGXXGXX[AG], which is a close match to the canonical NAD-binding motif. Members include Arabidopsis thaliana GDP-mannose-3',5'-epimerase (GME) which catalyzes the epimerization of two positions of GDP-alpha-D-mannose to form GDP-beta-L-galactose. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187581 [Multi-domain]  Cd Length: 328  Bit Score: 40.16  E-value: 1.16e-03
                          10        20
                  ....*....|....*....|....*..
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVV 29
Cdd:cd05273     2 RALVTGAGGFIGSHLAERLKAEGHYVR 28
FAR-N_SDR_e cd05236
fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding ...
3-213 1.28e-03

fatty acyl CoA reductases (FARs), extended (e) SDRs; SDRs are Rossmann-fold NAD(P)H-binding proteins, many of which may function as fatty acyl CoA reductases (FAR), acting on medium and long chain fatty acids, and have been reported to be involved in diverse processes such as biosynthesis of insect pheromones, plant cuticular wax production, and mammalian wax biosynthesis. In Arabidopsis thaliana, proteins with this particular architecture have also been identified as the MALE STERILITY 2 (MS2) gene product, which is implicated in male gametogenesis. Mutations in MS2 inhibit the synthesis of exine (sporopollenin), rendering plants unable to reduce pollen wall fatty acids to corresponding alcohols. This N-terminal domain shares the catalytic triad (but not the upstream Asn) and characteristic NADP-binding motif of the extended SDR family. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187547 [Multi-domain]  Cd Length: 320  Bit Score: 39.97  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALL---------------QRGHSVVTTVRSEQKAQSIRH--EFQGLGEEKLdFAIVPDIAAKD 65
Cdd:cd05236     2 SVLITGATGFLGKVLLEKLLrscpdigkiyllirgKSGQSAEERLRELLKDKLFDRgrNLNPLFESKI-VPIEGDLSEPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935  66 afqglgaYGLEAA------------IHVASpfhyNIT-DAK-KDLIDPAVLGTTSVLDaLHKTCPTVRRV-----ALTSS 126
Cdd:cd05236    81 -------LGLSDEdlqtlieevniiIHCAA----TVTfDERlDEALSINVLGTLRLLE-LAKRCKKLKAFvhvstAYVNG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935 127 FAAILDPKLSFTGAKKTYTEADWSPL-TIEDAYSNPGLA------YATSKALAEkaawDFMADTKPHFSLTTICPPMVYG 199
Cdd:cd05236   149 DRQLIEEKVYPPPADPEKLIDILELMdDLELERATPKLLgghpntYTFTKALAE----RLVLKERGNLPLVIVRPSIVGA 224
                         250
                  ....*....|....*
gi 1111477935 200 PVKYPVKS-LDSVNT 213
Cdd:cd05236   225 TLKEPFPGwIDNFNG 239
UDP_GE_SDE_e cd05253
UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid ...
3-82 1.52e-03

UDP glucuronic acid epimerase, extended (e) SDRs; This subgroup contains UDP-D-glucuronic acid 4-epimerase, an extended SDR, which catalyzes the conversion of UDP-alpha-D-glucuronic acid to UDP-alpha-D-galacturonic acid. This group has the SDR's canonical catalytic tetrad and the TGxxGxxG NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187563 [Multi-domain]  Cd Length: 332  Bit Score: 40.01  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVT--------TVRSEQKaqsiRHEFqgLGEEKLDFAIVPDIAAKDAFQGLGAYG 74
Cdd:cd05253     2 KILVTGAAGFIGFHVAKRLLERGDEVVGidnlndyyDVRLKEA----RLEL--LGKSGGFKFVKGDLEDREALRRLFKDH 75

                  ....*....
gi 1111477935  75 -LEAAIHVA 82
Cdd:cd05253    76 eFDAVIHLA 84
PLN02240 PLN02240
UDP-glucose 4-epimerase
3-82 1.94e-03

UDP-glucose 4-epimerase


Pssm-ID: 177883 [Multi-domain]  Cd Length: 352  Bit Score: 39.56  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVR-SEQKAQSIRHEFQGLGE--EKLDFAIVpDIAAKDAFQGL-GAYGLEAA 78
Cdd:PLN02240    7 TILVTGGAGYIGSHTVLQLLLAGYKVVVIDNlDNSSEEALRRVKELAGDlgDNLVFHKV-DLRDKEALEKVfASTRFDAV 85

                  ....
gi 1111477935  79 IHVA 82
Cdd:PLN02240   86 IHFA 89
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
3-79 2.76e-03

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 38.60  E-value: 2.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEKLdfAIVPDIAAKDAFQGLgaygLEAAI 79
Cdd:PRK05653    7 TALVTGASRGIGRAIALRLAADGAKVVIYDSNEEAAEALAAELRAAGGEAR--VLVFDVSDEAAVRAL----IEAAV 77
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-70 8.35e-03

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 37.16  E-value: 8.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1111477935   1 MTRVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEFQGLGEEkldFAIVP-DIAAKDAFQGL 70
Cdd:COG0300     5 GKTVLITGASSGIGRALARALAARGARVVLVARDAERLEALAAELRAAGAR---VEVVAlDVTDPDAVAAL 72
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
3-45 8.49e-03

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 37.24  E-value: 8.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQRGHSVVTTVRSEQKAQSIRHEF 45
Cdd:PRK06200    8 VALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRF 50
PCBER_SDR_a cd05259
phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and ...
3-92 9.92e-03

phenylcoumaran benzylic ether reductase (PCBER) like, atypical (a) SDRs; PCBER and pinoresinol-lariciresinol reductases are NADPH-dependent aromatic alcohol reductases, and are atypical members of the SDR family. Other proteins in this subgroup are identified as eugenol synthase. These proteins contain an N-terminus characteristic of NAD(P)-binding proteins and a small C-terminal domain presumed to be involved in substrate binding, but they do not have the conserved active site Tyr residue typically found in SDRs. Numerous other members have unknown functions. The glycine rich NADP-binding motif in this subgroup is of 2 forms: GXGXXG and G[GA]XGXXG; it tends to be atypical compared with the forms generally seen in classical or extended SDRs. The usual SDR active site tetrad is not present, but a critical active site Lys at the usual SDR position has been identified in various members, though other charged and polar residues are found at this position in this subgroup. Atypical SDR-related proteins retain the Rossmann fold of the SDRs, but have limited sequence identity and generally lack the catalytic properties of the archetypical members. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187569 [Multi-domain]  Cd Length: 282  Bit Score: 37.28  E-value: 9.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1111477935   3 RVLVTGGTGFVAGHVIDALLQR-GHSVVTTVRSEQKAqsiRHEFQGLGE--EKLDFAIVPDIAakDAFQGLGAYgLEAAI 79
Cdd:cd05259     1 KIAIAGATGTLGGPIVSALLASpGFTVTVLTRPSSTS---SNEFQPSGVkvVPVDYASHESLV--AALKGVDAV-ISALG 74
                          90
                  ....*....|...
gi 1111477935  80 HVASPFHYNITDA 92
Cdd:cd05259    75 GAAIGDQLKLIDA 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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