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Conserved domains on  [gi|1713980362|dbj|BBC91735|]
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short-chain dehydrogenase/reductase [Streptomyces rochei]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08263 super family cl32283
short chain dehydrogenase; Provisional
8-280 5.18e-91

short chain dehydrogenase; Provisional


The actual alignment was detected with superfamily member PRK08263:

Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 271.53  E-value: 5.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08263    5 VWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK08263   85 AGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGG-ISAFPMSGIYHASKWALEGMSEAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRlMRQNTAgAAGDPHRAAEIIVRTVRRGELPSHLL 247
Cdd:PRK08263  164 AQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREELAE-QWSERS-VDGDPEAAAEALLKLVDAENPPLRLF 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1713980362 248 LGVNAATMALDHDRRRLADASAWEKVSRSADFG 280
Cdd:PRK08263  242 LGSGVLDLAKADYERRLATWEEWEAVSRAAQGA 274
 
Name Accession Description Interval E-value
PRK08263 PRK08263
short chain dehydrogenase; Provisional
8-280 5.18e-91

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 271.53  E-value: 5.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08263    5 VWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK08263   85 AGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGG-ISAFPMSGIYHASKWALEGMSEAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRlMRQNTAgAAGDPHRAAEIIVRTVRRGELPSHLL 247
Cdd:PRK08263  164 AQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREELAE-QWSERS-VDGDPEAAAEALLKLVDAENPPLRLF 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1713980362 248 LGVNAATMALDHDRRRLADASAWEKVSRSADFG 280
Cdd:PRK08263  242 LGSGVLDLAKADYERRLATWEEWEAVSRAAQGA 274
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
8-252 4.11e-77

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 234.82  E-value: 4.11e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd05374     2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVL 167
Cdd:cd05374    82 AGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLV-PTPFLGPYCASKAALEALSESL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWAGSSMTV---HDVPEAYDATVGAMnRLMRQNTAGAAGDPHRAAEIIVRTVRRGELPS 244
Cdd:cd05374   161 RLELAPFGIKVTIIEPGPVRTGFADNAAGSaleDPEISPYAPERKEI-KENAAGVGSNPGDPEKVADVIVKALTSESPPL 239

                  ....*...
gi 1713980362 245 HLLLGVNA 252
Cdd:cd05374   240 RYFLGSDA 247
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
1-239 1.53e-66

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 207.73  E-value: 1.53e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDpQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:COG4221     1 MSDKG-KVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAV 160
Cdd:COG4221    80 LDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLR-PYPGGAVYAATKAAV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMtvHDVPEAYDATVGAMNRLmrqntagaagDPHRAAEIIVRTVRR 239
Cdd:COG4221   159 RGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVF--DGDAEAAAAVYEGLEPL----------TPEDVAEAVLFALTQ 225
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
7-189 1.16e-51

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 168.18  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEkleAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGF 163
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPY-PGGSAYSASKAAVIGF 159
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTD 185
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
11-244 5.13e-10

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 58.77  E-value: 5.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRA----LVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVA---------- 76
Cdd:TIGR01500   5 VTGASRGFGRTiaqeLAKCLKSPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLkalrelprpk 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  77 RFGRIdVLVNNAG-YANVSPIETT-EDADF-RAQFETNFWGVYHVTRAALPVLRR-QGAG-TVVQFSSIGGrVGGSPGIA 151
Cdd:TIGR01500  85 GLQRL-LLINNAGtLGDVSKGFVDlSDSTQvQNYWALNLTSMLCLTSSVLKAFKDsPGLNrTVVNISSLCA-IQPFKGWA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 152 SYQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwagssMTVHDVPEAYDATVGAMNRLMRQNtaGAAGDPHRAAE 231
Cdd:TIGR01500 163 LYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTD-----MQQQVREESVDPDMRKGLQELKAK--GKLVDPKVSAQ 235
                         250
                  ....*....|...
gi 1713980362 232 IIVRTVRRGELPS 244
Cdd:TIGR01500 236 KLLSLLEKDKFKS 248
 
Name Accession Description Interval E-value
PRK08263 PRK08263
short chain dehydrogenase; Provisional
8-280 5.18e-91

short chain dehydrogenase; Provisional


Pssm-ID: 181334 [Multi-domain]  Cd Length: 275  Bit Score: 271.53  E-value: 5.18e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08263    5 VWFITGASRGFGRAWTEAALERGDRVVATARDTATLADLAEKYGDRLLPLALDVTDRAAVFAAVETAVEHFGRLDIVVNN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK08263   85 AGYGLFGMIEEVTESEARAQIDTNFFGALWVTQAVLPYLREQRSGHIIQISSIGG-ISAFPMSGIYHASKWALEGMSEAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRlMRQNTAgAAGDPHRAAEIIVRTVRRGELPSHLL 247
Cdd:PRK08263  164 AQEVAEFGIKVTLVEPGGYSTDWAGTSAKRATPLDAYDTLREELAE-QWSERS-VDGDPEAAAEALLKLVDAENPPLRLF 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1713980362 248 LGVNAATMALDHDRRRLADASAWEKVSRSADFG 280
Cdd:PRK08263  242 LGSGVLDLAKADYERRLATWEEWEAVSRAAQGA 274
PRK06180 PRK06180
short chain dehydrogenase; Provisional
5-279 5.40e-91

short chain dehydrogenase; Provisional


Pssm-ID: 180446 [Multi-domain]  Cd Length: 277  Bit Score: 271.40  E-value: 5.40e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK06180    3 SMKTWLITGVSSGFGRALAQAALAAGHRVVGTVRSEAARADFEALHPDRALARLLDVTDFDAIDAVVADAEATFGPIDVL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFS 164
Cdd:PRK06180   83 VNNAGYGHEGAIEESPLAEMRRQFEVNVFGAVAMTKAVLPGMRARRRGHIVNITSMGGLI-TMPGIGYYCGSKFALEGIS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEA-YDATVGAmNRLMRQNTAGA-AGDPHRAAEIIVRTVRRGEL 242
Cdd:PRK06180  162 ESLAKEVAPFGIHVTAVEPGSFRTDWAGRSMVRTPRSIAdYDALFGP-IRQAREAKSGKqPGDPAKAAQAILAAVESDEP 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1713980362 243 PSHLLLGvnaaTMALDHDRRRLA----DASAWEKVSRSADF 279
Cdd:PRK06180  241 PLHLLLG----SDALRLVRAKLAaldaEIDAWEAVTVSTDF 277
17beta-HSD-like_SDR_c cd05374
17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid ...
8-252 4.11e-77

17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187632 [Multi-domain]  Cd Length: 248  Bit Score: 234.82  E-value: 4.11e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd05374     2 VVLITGCSSGIGLALALALAAQGYRVIATARNPDKLESLGELLNDNLEVLELDVTDEESIKAAVKEVIERFGRIDVLVNN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVL 167
Cdd:cd05374    82 AGYGLFGPLEETSIEEVRELFEVNVFGPLRVTRAFLPLMRKQGSGRIVNVSSVAGLV-PTPFLGPYCASKAALEALSESL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWAGSSMTV---HDVPEAYDATVGAMnRLMRQNTAGAAGDPHRAAEIIVRTVRRGELPS 244
Cdd:cd05374   161 RLELAPFGIKVTIIEPGPVRTGFADNAAGSaleDPEISPYAPERKEI-KENAAGVGSNPGDPEKVADVIVKALTSESPPL 239

                  ....*...
gi 1713980362 245 HLLLGVNA 252
Cdd:cd05374   240 RYFLGSDA 247
YdfG COG4221
NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; ...
1-239 1.53e-66

NADP-dependent 3-hydroxy acid dehydrogenase YdfG [Energy production and conversion]; NADP-dependent 3-hydroxy acid dehydrogenase YdfG is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 443365 [Multi-domain]  Cd Length: 240  Bit Score: 207.73  E-value: 1.53e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDpQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:COG4221     1 MSDKG-KVALITGASSGIGAATARALAAAGARVVLAARRAERLEALAAELGGRALAVPLDVTDEAAVEAAVAAAVAEFGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAV 160
Cdd:COG4221    80 LDVLVNNAGVALLGPLEELDPEDWDRMIDVNVKGVLYVTRAALPAMRARGSGHIVNISSIAGLR-PYPGGAVYAATKAAV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMtvHDVPEAYDATVGAMNRLmrqntagaagDPHRAAEIIVRTVRR 239
Cdd:COG4221   159 RGLSESLRAELRPTGIRVTVIEPGAVDTEFLDSVF--DGDAEAAAAVYEGLEPL----------TPEDVAEAVLFALTQ 225
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
1-257 1.99e-60

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 192.39  E-value: 1.99e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDpQVWFITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:COG0300     1 MSLTG-KTVLITGASSGIGRALARALAARGARVVLVARDAerlEALAAELRAAGARVEVVALDVTDPDAVAALAEAVLAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAK 157
Cdd:COG0300    80 FGPIDVLVNNAGVGGGGPFEELDLEDLRRVFEVNVFGPVRLTRALLPLMRARGRGRIVNVSSVAGLRGL-PGMAAYAASK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEPSGFATDwagssmtvhdvpeaydatvgaMNRLMRQNTAGAAGDPHRAAEIIVRTV 237
Cdd:COG0300   159 AALEGFSESLRAELAPTGVRVTAVCPGPVDTP---------------------FTARAGAPAGRPLLSPEEVARAILRAL 217
                         250       260
                  ....*....|....*....|
gi 1713980362 238 RRGelPSHLLLGVNAATMAL 257
Cdd:COG0300   218 ERG--RAEVYVGWDARLLAR 235
PRK06482 PRK06482
SDR family oxidoreductase;
6-278 2.94e-60

SDR family oxidoreductase;


Pssm-ID: 235813 [Multi-domain]  Cd Length: 276  Bit Score: 193.02  E-value: 2.94e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   6 PQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK06482    2 SKTWFITGASSGFGRGMTERLLARGDRVAATVRRPDALDDLKARYGDRLWVLQLDVTDSAAVRAVVDRAFAALGRIDVVV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSR 165
Cdd:PRK06482   82 SNAGYGLFGAAEELSDAQIRRQIDTNLIGSIQVIRAALPHLRRQGGGRIVQVSSEGGQI-AYPGFSLYHATKWGIEGFVE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 166 VLATETAPFGVRVMVVEPSGFATDWaGSSMTVHDVPEAYDAT-VGAMNRLMRQNTAGAAGDPHRAAEIIVRTVRRGELPS 244
Cdd:PRK06482  161 AVAQEVAPFGIEFTIVEPGPARTNF-GAGLDRGAPLDAYDDTpVGDLRRALADGSFAIPGDPQKMVQAMIASADQTPAPR 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1713980362 245 HLLLGVNAATMALDHDRRRLADASAWEKVSRSAD 278
Cdd:PRK06482  240 RLTLGSDAYASIRAALSERLAALEAQKAVALSTD 273
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
1-214 1.94e-54

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 176.90  E-value: 1.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:COG1028     1 MTRLKGKVALVTGGSSGIGRAIARALAAEGARVVITDRDAEALeaaAAELRAAGGRALAVAADVTDEAAVEALVAAAVAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAK 157
Cdd:COG1028    81 FGRLDILVNNAGITPPGPLEELTEEDWDRVLDVNLKGPFLLTRAALPHMRERGGGRIVNISSIAGLR-GSPGQAAYAASK 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVgAMNRL 214
Cdd:COG1028   160 AAVVGLTRSLALELAPRGIRVNAVAPGPIDTPMTRALLGAEEVREALAARI-PLGRL 215
PRK06914 PRK06914
SDR family oxidoreductase;
4-235 2.00e-53

SDR family oxidoreductase;


Pssm-ID: 180744 [Multi-domain]  Cd Length: 280  Bit Score: 175.60  E-value: 2.00e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   4 QDPQVWFITGSSRGFGRaLVDAVLA-AGDLVVATARRPEA---LAADLAEYG--DRVLPLALDVTSPDAARAAVEAAVAr 77
Cdd:PRK06914    1 MNKKIAIVTGASSGFGL-LTTLELAkKGYLVIATMRNPEKqenLLSQATQLNlqQNIKVQQLDVTDQNSIHNFQLVLKE- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAK 157
Cdd:PRK06914   79 IGRIDLLVNNAGYANGGFVEEIPVEEYRKQFETNVFGAISVTQAVLPYMRKQKSGKIINISSISGRV-GFPGLSPYVSSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEPSGFATD-WAGSSMTVHDVPEAYDATVGAMNRLMR--QNTAGAAGDPHRAAEIIV 234
Cdd:PRK06914  158 YALEGFSESLRLELKPFGIDVALIEPGSYNTNiWEVGKQLAENQSETTSPYKEYMKKIQKhiNSGSDTFGNPIDVANLIV 237

                  .
gi 1713980362 235 R 235
Cdd:PRK06914  238 E 238
SDR_c cd05233
classical (c) SDRs; SDRs are a functionally diverse family of oxidoreductases that have a ...
10-234 3.65e-53

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


Pssm-ID: 212491 [Multi-domain]  Cd Length: 234  Bit Score: 173.24  E-value: 3.65e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALA--ADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd05233     2 LVTGASSGIGRAIARRLAREGAKVVLADRNEEALAelAAIEALGGNAVAVQADVSDEEDVEALVEEALEEFGRLDILVNN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:cd05233    82 AGIARPGPLEELTDEDWDRVLDVNLTGVFLLTRAALPHMKKQGGGRIVNISSVAGL-RPLPGQAAYAASKAALEGLTRSL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATvgamnrlmrqnTAGAAGDPHRAAEIIV 234
Cdd:cd05233   161 ALELAPYGIRVNAVAPGLVDTPMLAKLGPEEAEKELAAAI-----------PLGRLGTPEEVAEAVV 216
adh_short pfam00106
short chain dehydrogenase; This family contains a wide variety of dehydrogenases.
7-189 1.16e-51

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


Pssm-ID: 395056 [Multi-domain]  Cd Length: 195  Bit Score: 168.18  E-value: 1.16e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:pfam00106   1 KVALVTGASSGIGRAIAKRLAKEGAKVVLVDRSEEkleAVAKELGALGGKALFIQGDVTDRAQVKALVEQAVERLGRLDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGF 163
Cdd:pfam00106  81 LVNNAGITGLGPFSELSDEDWERVIDVNLTGVFNLTRAVLPAMIKGSGGRIVNISSVAGLVPY-PGGSAYSASKAAVIGF 159
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:pfam00106 160 TRSLALELAPHGIRVNAVAPGGVDTD 185
PRK06182 PRK06182
short chain dehydrogenase; Validated
8-237 5.42e-47

short chain dehydrogenase; Validated


Pssm-ID: 180448 [Multi-domain]  Cd Length: 273  Bit Score: 158.58  E-value: 5.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAaDLAEYGdrVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK06182    5 VALVTGASSGIGKATARRLAAQGYTVYGAARRVDKME-DLASLG--VHPLSLDVTDEASIKAAVDTIIAEEGRIDVLVNN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK06182   82 AGYGSYGAIEDVPIDEARRQFEVNLFGAARLTQLVLPHMRAQRSGRIINISSMGGKI-YTPLGAWYHATKFALEGFSDAL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDW---AGSSMTVHDVPEAYDATVGAMNRLMR-QNTAGAAGDPHRAAEIIVRTV 237
Cdd:PRK06182  161 RLEVAPFGIDVVVIEPGGIKTEWgdiAADHLLKTSGNGAYAEQAQAVAASMRsTYGSGRLSDPSVIADAISKAV 234
CAD_SDR_c cd08934
clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent ...
5-235 5.23e-42

clavulanic acid dehydrogenase (CAD), classical (c) SDR; CAD catalyzes the NADP-dependent reduction of clavulanate-9-aldehyde to clavulanic acid, a beta-lactamase inhibitor. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187639 [Multi-domain]  Cd Length: 243  Bit Score: 144.99  E-value: 5.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:cd08934     2 QGKVALVTGASSGIGEATARALAAEGAAVAIAARRVDrleALADELEAEGGKALVLELDVTDEQQVDAAVERTVEALGRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVD 161
Cdd:cd08934    82 DILVNNAGIMLLGPVEDADTTDWTRMIDTNLLGLMYTTHAALPHHLLRNKGTIVNISSVAGRVAV-RNSAVYNATKFGVN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATDWAGsSMTVHDVPEAYDATVGAMNRLMRQNTAGA----AGDPHRAA--EIIVR 235
Cdd:cd08934   161 AFSEGLRQEVTERGVRVVVIEPGTVDTELRD-HITHTITKEAYEERISTIRKLQAEDIAAAvryaVTAPHHVTvnEILIR 239
PRK12826 PRK12826
SDR family oxidoreductase;
7-192 1.58e-41

SDR family oxidoreductase;


Pssm-ID: 183775 [Multi-domain]  Cd Length: 251  Bit Score: 143.90  E-value: 1.58e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAA---DLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK12826    7 RVALVTGAARGIGRAIAVRLAADGAEVIVVDICGDDAAAtaeLVEAAGGKARARQVDVRDRAALKAAVAAGVEDFGRLDI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGF 163
Cdd:PRK12826   87 LVANAGIFPLTPFAEMDDEQWERVIDVNLTGTFLLTQAALPALIRAGGGRIVLTSSVAGPRVGYPGLAHYAASKAGLVGF 166
                         170       180
                  ....*....|....*....|....*....
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFATDWAG 192
Cdd:PRK12826  167 TRALALELAARNITVNSVHPGGVDTPMAG 195
fabG PRK05557
3-ketoacyl-(acyl-carrier-protein) reductase; Validated
7-214 7.31e-40

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


Pssm-ID: 235500 [Multi-domain]  Cd Length: 248  Bit Score: 139.17  E-value: 7.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRP----EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK05557    6 KVALVTGASRGIGRAIAERLAAQGANVVINYASSeagaEALVAEIGALGGKALAVQGDVSDAESVERAVDEAKAEFGGVD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDG 162
Cdd:PRK05557   86 ILVNNAGITRDNLLMRMKEEDWDRVIDTNLTGVFNLTKAVARPMMKQRSGRIINISSVVGLM-GNPGQANYAASKAGVIG 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATDwagssMT---VHDVPEAYDATVgAMNRL 214
Cdd:PRK05557  165 FTKSLARELASRGITVNAVAPGFIETD-----MTdalPEDVKEAILAQI-PLGRL 213
fabG PRK05653
3-oxoacyl-ACP reductase FabG;
10-189 4.68e-39

3-oxoacyl-ACP reductase FabG;


Pssm-ID: 235546 [Multi-domain]  Cd Length: 246  Bit Score: 137.21  E-value: 4.68e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK05653    9 LVTGASRGIGRAIALRLAADGAKVVIYDSNEeaaEALAAELRAAGGEARVLVFDVSDEAAVRALIEAAVEAFGALDILVN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGFSRV 166
Cdd:PRK05653   89 NAGITRDALLPRMSEEDWDRVIDVNLTGTFNVVRAALPPMIKARYGRIVNISSVSGVTGN-PGQTNYSAAKAGVIGFTKA 167
                         170       180
                  ....*....|....*....|...
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK05653  168 LALELASRGITVNAVAPGFIDTD 190
PRK06179 PRK06179
short chain dehydrogenase; Provisional
3-235 9.28e-39

short chain dehydrogenase; Provisional


Pssm-ID: 235725 [Multi-domain]  Cd Length: 270  Bit Score: 136.96  E-value: 9.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   3 TQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADlaeygDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK06179    1 MSNSKVALVTGASSGIGRATAEKLARAGYRVFGTSRNPARAAPI-----PGVELLELDVTDDASVQAAVDEVIARAGRID 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDG 162
Cdd:PRK06179   76 VLVNNAGVGLAGAAEESSIAQAQALFDTNVFGILRMTRAVLPHMRAQGSGRIINISSVLGFL-PAPYMALYAASKHAVEG 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRLMRQNTAGAAgDPHRAAEIIVR 235
Cdd:PRK06179  155 YSESLDHEVRQFGIRVSLVEPAYTKTNFDANAPEPDSPLAEYDRERAVVSKAVAKAVKKAD-APEVVADTVVK 226
11beta-HSD1_like_SDR_c cd05332
11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human ...
7-241 6.07e-38

11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1)-like, classical (c) SDRs; Human 11beta_HSD1 catalyzes the NADP(H)-dependent interconversion of cortisone and cortisol. This subgroup also includes human dehydrogenase/reductase SDR family member 7C (DHRS7C) and DHRS7B. These proteins have the GxxxGxG nucleotide binding motif and S-Y-K catalytic triad characteristic of the SDRs, but have an atypical C-terminal domain that contributes to homodimerization contacts. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187593 [Multi-domain]  Cd Length: 257  Bit Score: 134.64  E-value: 6.07e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGD-RVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:cd05332     4 KVVIITGASSGIGEELAYHLARLGARLVLSARREERLeevKSECLELGApSPHVVPLDMSDLEDAEQVVEEALKLFGGLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDG 162
Cdd:cd05332    84 ILINNAGISMRSLFHDTSIDVDRKIMEVNYFGPVALTKAALPHLIERSQGSIVVVSSIAGKI-GVPFRTAYAASKHALQG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATDwagSSMtvhdvpEAYDATVGAMNRLMRQNTAGAAgdPHRAAEIIVRTVRRGE 241
Cdd:cd05332   163 FFDSLRAELSEPNISVTVVCPGLIDTN---IAM------NALSGDGSMSAKMDDTTANGMS--PEECALEILKAIALRK 230
fabG PRK12825
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
7-189 9.83e-38

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


Pssm-ID: 237218 [Multi-domain]  Cd Length: 249  Bit Score: 133.84  E-value: 9.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE----YGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK12825    7 RVALVTGAARGLGRAIALRLARAGADVVVHYRSDEEAAEELVEaveaLGRRAQAVQADVTDKAALEAAVAAAVERFGRID 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDG 162
Cdd:PRK12825   87 ILVNNAGIFEDKPLADMSDDEWDEVIDVNLSGVFHLLRAVVPPMRKQRGGRIVNISSVAG-LPGWPGRSNYAAAKAGLVG 165
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK12825  166 LTKALARELAEYGITVNMVAPGDIDTD 192
HetN_like_SDR_c cd08932
HetN oxidoreductase-like, classical (c) SDR; This subgroup includes Anabaena sp. strain PCC ...
11-201 2.56e-35

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


Pssm-ID: 212493 [Multi-domain]  Cd Length: 223  Bit Score: 126.71  E-value: 2.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEyGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:cd08932     5 VTGASRGIGIEIARALARDGYRVSLGLRNPEDLAALSAS-GGDVEAVPYDARDPEDARALVDALRDRFGRIDVLVHNAGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVLATE 170
Cdd:cd08932    84 GRPTTLREGSDAELEAHFSINVIAPAELTRALLPALREAGSGRVVFLNSLSG-KRVLAGNAGYSASKFALRALAHALRQE 162
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 171 TAPFGVRVMVVEPSGFATDWAGSSMTVHDVP 201
Cdd:cd08932   163 GWDHGVRVSAVCPGFVDTPMAQGLTLVGAFP 193
FabG-like PRK07231
SDR family oxidoreductase;
11-214 4.21e-35

SDR family oxidoreductase;


Pssm-ID: 235975 [Multi-domain]  Cd Length: 251  Bit Score: 126.87  E-value: 4.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEAL--AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNA 88
Cdd:PRK07231   10 VTGASSGIGEGIARRFAAEGARVVVTDRNEEAAerVAAEILAGGRAIAVAADVSDEADVEAAVAAALERFGSVDILVNNA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GY--ANVSPIETTEDAdFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRV 166
Cdd:PRK07231   90 GTthRNGPLLDVDEAE-FDRIFAVNVKSPYLWTQAAVPAMRGEGGGAIVNVASTAG-LRPRPGLGWYNASKGAVITLTKA 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATDWAGSSMTVhDVPEAYDATVGA--MNRL 214
Cdd:PRK07231  168 LAAELGPDKIRVNAVAPVVVETGLLEAFMGE-PTPENRAKFLATipLGRL 216
fabG PRK05565
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-234 1.39e-34

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


Pssm-ID: 235506 [Multi-domain]  Cd Length: 247  Bit Score: 125.34  E-value: 1.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALvdAVLAAGD---LVVATARRPEA---LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK05565   10 VTGASGGIGRAI--AELLAKEgakVVIAYDINEEAaqeLLEEIKEEGGDAIAVKADVSSEEDVENLVEQIVEKFGKIDIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGiASYQAAKFAVDGFS 164
Cdd:PRK05565   88 VNNAGISNFGLVTDMTDEEWDRVIDVNLTGVMLLTRYALPYMIKRKSGVIVNISSIWGLIGASCE-VLYSASKGAVNAFT 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDwAGSSMTVHDVPEaydatvgamnrLMRQNTAGAAGDPHRAAEIIV 234
Cdd:PRK05565  167 KALAKELAPSGIRVNAVAPGAIDTE-MWSSFSEEDKEG-----------LAEEIPLGRLGKPEEIAKVVL 224
PRK05693 PRK05693
SDR family oxidoreductase;
8-191 2.47e-34

SDR family oxidoreductase;


Pssm-ID: 168186 [Multi-domain]  Cd Length: 274  Bit Score: 125.67  E-value: 2.47e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAAdLAEYGdrVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK05693    3 VVLITGCSSGIGRALADAFKAAGYEVWATARKAEDVEA-LAAAG--FTAVQLDVNDGAALARLAEELEAEHGGLDVLINN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRqGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK05693   80 AGYGAMGPLLDGGVEAMRRQFETNVFAVVGVTRALFPLLRR-SRGLVVNIGSVSG-VLVTPFAGAYCASKAAVHALSDAL 157
                         170       180
                  ....*....|....*....|....
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWA 191
Cdd:PRK05693  158 RLELAPFGVQVMEVQPGAIASQFA 181
BKR_SDR_c cd05333
beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; ...
7-196 3.63e-34

beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs; This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187594 [Multi-domain]  Cd Length: 240  Bit Score: 124.20  E-value: 3.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE---YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:cd05333     1 KVALVTGASRGIGRAIALRLAAEGAKVAVTDRSEEAAAETVEEikaLGGNAAALEADVSDREAVEALVEKVEAEFGPVDI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGF 163
Cdd:cd05333    81 LVNNAGITRDNLLMRMSEEDWDAVINVNLTGVFNVTQAVIRAMIKRRSGRIINISSVVGLI-GNPGQANYAASKAGVIGF 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1713980362 164 SRVLATETAPFGVRVMVVEPsGF-ATDwagssMT 196
Cdd:cd05333   160 TKSLAKELASRGITVNAVAP-GFiDTD-----MT 187
PRK07326 PRK07326
SDR family oxidoreductase;
1-194 1.10e-33

SDR family oxidoreductase;


Pssm-ID: 235990 [Multi-domain]  Cd Length: 237  Bit Score: 122.81  E-value: 1.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATAR---RPEALAADLAEYGdRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:PRK07326    1 MMSLKGKVALITGGSKGIGFAIAEALLAEGYKVAITARdqkELEEAAAELNNKG-NVLGLAADVRDEADVQRAVDAIVAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGR---VGGspgiASYQ 154
Cdd:PRK07326   80 FGGLDVLIANAGVGHFAPVEELTPEEWRLVIDTNLTGAFYTIKAAVPALKRGG-GYIINISSLAGTnffAGG----AAYN 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1713980362 155 AAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDWAGSS 194
Cdd:PRK07326  155 ASKFGLVGFSEAAMLDLRQYGIKVSTIMPGSVATHFNGHT 194
PRK08264 PRK08264
SDR family oxidoreductase;
1-189 1.32e-33

SDR family oxidoreductase;


Pssm-ID: 181335 [Multi-domain]  Cd Length: 238  Bit Score: 122.69  E-value: 1.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDpQVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAadlaEYGDRVLPLALDVTSPDAARAAVEAAvarfG 79
Cdd:PRK08264    2 MDIKG-KVVLVTGANRGIGRAFVEQLLARGaAKVYAAARDPESVT----DLGPRVVPLQLDVTDPASVAAAAEAA----S 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  80 RIDVLVNNAGYANV-SPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKF 158
Cdd:PRK08264   73 DVTILVNNAGIFRTgSLLLEGDEDALRAEMETNYFGPLAMARAFAPVLAANGGGAIVNVLSVLSWVNF-PNLGTYSASKA 151
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK08264  152 AAWSLTQALRAELAPQGTRVLGVHPGPIDTD 182
PRK12429 PRK12429
3-hydroxybutyrate dehydrogenase; Provisional
7-183 1.52e-33

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 237100 [Multi-domain]  Cd Length: 258  Bit Score: 123.07  E-value: 1.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK12429    5 KVALVTGAASGIGLEIALALAKEGAKVVIADLNDEAAaaaAEALQKAGGKAIGVAMDVTDEEAINAGIDYAVETFGGVDI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGF 163
Cdd:PRK12429   85 LVNNAGIQHVAPIEDFPTEKWKKMIAIMLDGAFLTTKAALPIMKAQGGGRIINMASVHGLV-GSAGKAAYVSAKHGLIGL 163
                         170       180
                  ....*....|....*....|
gi 1713980362 164 SRVLATETAPFGVRVMVVEP 183
Cdd:PRK12429  164 TKVVALEGATHGVTVNAICP 183
3beta-17beta-HSD_like_SDR_c cd05341
3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes ...
7-234 1.56e-33

3beta17beta hydroxysteroid dehydrogenase-like, classical (c) SDRs; This subgroup includes members identified as 3beta17beta hydroxysteroid dehydrogenase, 20beta hydroxysteroid dehydrogenase, and R-alcohol dehydrogenase. These proteins exhibit the canonical active site tetrad and glycine rich NAD(P)-binding motif of the classical SDRs. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187600 [Multi-domain]  Cd Length: 247  Bit Score: 122.88  E-value: 1.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05341     6 KVAIVTGGARGLGLAHARLLVAEGAKVVLSDILDEEGQAAAAELGDAARFFHLDVTDEDGWTAVVDTAREAFGRLDVLVN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRV 166
Cdd:cd05341    86 NAGILTGGTVETTTLEEWRRLLDINLTGVFLGTRAVIPPMKEAGGGSIINMSSIEGLV-GDPALAAYNASKGAVRGLTKS 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 167 LATETAP--FGVRVMVVEPSGFATdwagsSMTvHDVPEAydatvGAMNRLMRQNTAGAAGDPHRAAEIIV 234
Cdd:cd05341   165 AALECATqgYGIRVNSVHPGYIYT-----PMT-DELLIA-----QGEMGNYPNTPMGRAGEPDEIAYAVV 223
PRK12829 PRK12829
short chain dehydrogenase; Provisional
10-183 1.57e-33

short chain dehydrogenase; Provisional


Pssm-ID: 183778 [Multi-domain]  Cd Length: 264  Bit Score: 123.24  E-value: 1.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEY-GDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNA 88
Cdd:PRK12829   15 LVTGGASGIGRAIAEAFAEAGARVHVCDVSEAALAATAARLpGAKVTATVADVADPAQVERVFDTAVERFGGLDVLVNNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GYANVS-PIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK12829   95 GIAGPTgGIDEITPEQWEQTLAVNLNGQFYFARAAVPLLKASGHGGVIIALSSVAGRLGYPGRTPYAASKWAVVGLVKSL 174
                         170
                  ....*....|....*.
gi 1713980362 168 ATETAPFGVRVMVVEP 183
Cdd:PRK12829  175 AIELGPLGIRVNAILP 190
SDR_c5 cd05346
classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a ...
10-183 1.87e-33

classical (c) SDR, subgroup 5; These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187604 [Multi-domain]  Cd Length: 249  Bit Score: 122.77  E-value: 1.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADL-AEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd05346     4 LITGASSGIGEATARRFAKAGAKLILTGRRAErlqELADELgAKFPVKVLPLQLDVSDRESIEAALENLPEEFRDIDILV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYA-NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFS 164
Cdd:cd05346    84 NNAGLAlGLDPAQEADLEDWETMIDTNVKGLLNVTRLILPIMIARNQGHIINLGSIAGR-YPYAGGNVYCATKAAVRQFS 162
                         170
                  ....*....|....*....
gi 1713980362 165 RVLATETAPFGVRVMVVEP 183
Cdd:cd05346   163 LNLRKDLIGTGIRVTNIEP 181
BKR_like_SDR_like cd05344
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup ...
10-189 3.16e-33

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR)-like, SDR; This subgroup resembles the SDR family, but does not have a perfect match to the NAD-binding motif or the catalytic tetrad characteristic of the SDRs. It includes the SDRs, Q9HYA2 from Pseudomonas aeruginosa PAO1 and APE0912 from Aeropyrum pernix K1. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187602 [Multi-domain]  Cd Length: 253  Bit Score: 122.00  E-value: 3.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05344     5 LVTAASSGIGLAIARALAREGARVAICARNRENLeraASELRAGGAGVLAVVADLTDPEDIDRLVEKAGDAFGRVDILVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASyQAAKFAVDGFSRV 166
Cdd:cd05344    85 NAGGPPPGPFAELTDEDWLEAFDLKLLSVIRIVRAVLPGMKERGWGRIVNISSLTVKEPEPNLVLS-NVARAGLIGLVKT 163
                         170       180
                  ....*....|....*....|...
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05344   164 LSRELAPDGVTVNSVLPGYIDTE 186
PRK06181 PRK06181
SDR family oxidoreductase;
7-189 6.87e-33

SDR family oxidoreductase;


Pssm-ID: 235726 [Multi-domain]  Cd Length: 263  Bit Score: 121.62  E-value: 6.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK06181    2 KVVIITGASEGIGRALAVRLARAGAQLVLAARNETRLaslAQELADHGGEALVVPTDVSDAEACERLIEAAVARFGGIDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTED-ADFRAQFETNFWGVYHVTRAALPVLR-RQGAGTVVqfSSIGGRVgGSPGIASYQAAKFAVD 161
Cdd:PRK06181   82 LVNNAGITMWSRFDELTDlSVFERVMRVNYLGAVYCTHAALPHLKaSRGQIVVV--SSLAGLT-GVPTRSGYAASKHALH 158
                         170       180
                  ....*....|....*....|....*...
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK06181  159 GFFDSLRIELADDGVAVTVVCPGFVATD 186
PRK08324 PRK08324
bifunctional aldolase/short-chain dehydrogenase;
7-202 7.46e-33

bifunctional aldolase/short-chain dehydrogenase;


Pssm-ID: 236241 [Multi-domain]  Cd Length: 681  Bit Score: 127.27  E-value: 7.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYG--DRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK08324  423 KVALVTGAAGGIGKATAKRLAAEGACVVLADLDEEAAEAAAAELGgpDRALGVACDVTDEAAVQAAFEEAALAFGGVDIV 502
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFS 164
Cdd:PRK08324  503 VSNAGIAISGPIEETSDEDWRRSFDVNATGHFLVAREAVRIMKAQGLGGSIVFIASKNAVNPGPNFGAYGAAKAAELHLV 582
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1713980362 165 RVLATETAPFGVRVMVVEP------SG-FATDWAGSSMTVHDVPE 202
Cdd:PRK08324  583 RQLALELGPDGIRVNGVNPdavvrgSGiWTGEWIEARAAAYGLSE 627
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
11-226 1.04e-32

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 120.54  E-value: 1.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd05347    10 VTGASRGIGFGIASGLAEAGANIVINSRNEEKAeeaQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDFGKIDILVNN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGFSRVL 167
Cdd:cd05347    90 AGIIRRHPAEEFPEAEWRDVIDVNLNGVFFVSQAVARHMIKQGHGKIINICSLLSELGG-PPVPAYAASKGGVAGLTKAL 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDwagssMTVHDVPEAydatvgAMNRLMRQNT-AGAAGDP 226
Cdd:cd05347   169 ATEWARHGIQVNAIAPGYFATE-----MTEAVVADP------EFNDDILKRIpAGRWGQP 217
fabG PRK07666
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-191 2.57e-32

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


Pssm-ID: 236074 [Multi-domain]  Cd Length: 239  Bit Score: 119.41  E-value: 2.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAG---DLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK07666   11 LITGAGRGIGRAVAIALAKEGvnvGLLARTEENLKAVAEEVEAYGVKVVIATADVSDYEEVTAAIEQLKNELGSIDILIN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSRV 166
Cdd:PRK07666   91 NAGISKFGKFLELDPAEWEKIIQVNLMGVYYATRAVLPSMIERQSGDIINISSTAGQ-KGAAVTSAYSASKFGVLGLTES 169
                         170       180
                  ....*....|....*....|....*
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATDWA 191
Cdd:PRK07666  170 LMQEVRKHNIRVTALTPSTVATDMA 194
KDSR-like_SDR_c cd08939
3-ketodihydrosphingosine reductase (KDSR) and related proteins, classical (c) SDR; These ...
7-188 5.47e-32

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


Pssm-ID: 187643 [Multi-domain]  Cd Length: 239  Bit Score: 118.51  E-value: 5.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALA-------ADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFG 79
Cdd:cd08939     2 KHVLITGGSSGIGKALAKELVKEGANVIIVARSESKLEeaveeieAEANASGQKVSYISADLSDYEEVEQAFAQAVEKGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  80 RIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFA 159
Cdd:cd08939    82 PPDLVVNCAGISIPGLFEDLTAEEFERGMDVNYFGSLNVAHAVLPLMKEQRPGHIVFVSSQAALV-GIYGYSAYCPSKFA 160
                         170       180
                  ....*....|....*....|....*....
gi 1713980362 160 VDGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:cd08939   161 LRGLAESLRQELKPYNIRVSVVYPPDTDT 189
PRK07109 PRK07109
short chain dehydrogenase; Provisional
1-210 9.30e-32

short chain dehydrogenase; Provisional


Pssm-ID: 235935 [Multi-domain]  Cd Length: 334  Bit Score: 120.41  E-value: 9.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:PRK07109    3 LKPIGRQVVVITGASAGVGRATARAFARRGAKVVLLARGEEGLealAAEIRAAGGEALAVVADVADAEAVQAAADRAEEE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAK 157
Cdd:PRK07109   83 LGPIDTWVNNAMVTVFGPFEDVTPEEFRRVTEVTYLGVVHGTLAALRHMRPRDRGAIIQVGSALAY-RSIPLQSAYCAAK 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMV--VEPSGFAT---DWAGSSMTVHD--VPEAYDATVGA 210
Cdd:PRK07109  162 HAIRGFTDSLRCELLHDGSPVSVtmVQPPAVNTpqfDWARSRLPVEPqpVPPIYQPEVVA 221
type2_17beta_HSD-like_SDR_c cd09805
human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; ...
9-194 9.79e-32

human 17beta-hydroxysteroid dehydrogenase type 2 (type 2 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical-SDR subgroup includes the human proteins: type 2 17beta-HSD, type 6 17beta-HSD, type 2 11beta-HSD, dehydrogenase/reductase SDR family member 9, short-chain dehydrogenase/reductase family 9C member 7, 3-hydroxybutyrate dehydrogenase type 1, and retinol dehydrogenase 5. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187665 [Multi-domain]  Cd Length: 281  Bit Score: 118.92  E-value: 9.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   9 WFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAA-DLAEY-GDRVLPLALDVTSPDAARAAVEAAVARFGRIDV--L 84
Cdd:cd09805     3 VLITGCDSGFGNLLAKKLDSLGFTVLAGCLTKNGPGAkELRRVcSDRLRTLQLDVTKPEQIKRAAQWVKEHVGEKGLwgL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGY-ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRqGAGTVVQFSSIGGRVGgSPGIASYQAAKFAVDGF 163
Cdd:cd09805    83 VNNAGIlGFGGDEELLPMDDYRKCMEVNLFGTVEVTKAFLPLLRR-AKGRVVNVSSMGGRVP-FPAGGAYCASKAAVEAF 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFATDWAGSS 194
Cdd:cd09805   161 SDSLRRELQPWGVKVSIIEPGNFKTGITGNS 191
SDR_c3 cd05360
classical (c) SDR, subgroup 3; These proteins are members of the classical SDR family, with a ...
7-240 1.66e-31

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


Pssm-ID: 187618 [Multi-domain]  Cd Length: 233  Bit Score: 117.10  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:cd05360     1 QVVVITGASSGIGRATALAFAERGAKVVLAARSAEALhelAREVRELGGEAIAVVADVADAAQVERAADTAVERFGRIDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGF 163
Cdd:cd05360    81 WVNNAGVAVFGRFEDVTPEEFRRVFDVNYLGHVYGTLAALPHLRRRGGGALINVGSLLGY-RSAPLQAAYSASKHAVRGF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 164 SRVLATETAPFGVRVMV--VEPSGFAT---DWAGSSMTVHD--VPEAYdatvgamnrlmrqntagaagDPHRAAEIIVRT 236
Cdd:cd05360   160 TESLRAELAHDGAPISVtlVQPTAMNTpffGHARSYMGKKPkpPPPIY--------------------QPERVAEAIVRA 219

                  ....
gi 1713980362 237 VRRG 240
Cdd:cd05360   220 AEHP 223
PRK09072 PRK09072
SDR family oxidoreductase;
11-241 1.32e-30

SDR family oxidoreductase;


Pssm-ID: 236372 [Multi-domain]  Cd Length: 263  Bit Score: 115.42  E-value: 1.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE--YGDRVLPLALDVTSPDAARAAVEAAVArFGRIDVLVNNA 88
Cdd:PRK09072   10 LTGASGGIGQALAEALAAAGARLLLVGRNAEKLEALAARlpYPGRHRWVVADLTSEAGREAVLARARE-MGGINVLINNA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGgSPGIASYQAAKFAVDGFSRVLA 168
Cdd:PRK09072   89 GVNHFALLEDQDPEAIERLLALNLTAPMQLTRALLPLLRAQPSAMVVNVGSTFGSIG-YPGYASYCASKFALRGFSEALR 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1713980362 169 TETAPFGVRVMVVEPSGFATdwagsSMTvhdvpeayDATVGAMNRLMrqntaGAAGD-PHRAAEIIVRTVRRGE 241
Cdd:PRK09072  168 RELADTGVRVLYLAPRATRT-----AMN--------SEAVQALNRAL-----GNAMDdPEDVAAAVLQAIEKER 223
PRK07825 PRK07825
short chain dehydrogenase; Provisional
11-184 3.79e-30

short chain dehydrogenase; Provisional


Pssm-ID: 181136 [Multi-domain]  Cd Length: 273  Bit Score: 114.65  E-value: 3.79e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGdRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:PRK07825   10 ITGGARGIGLATARALAALGARVAIGDLDEALAKETAAELG-LVVGGPLDVTDPASFAAFLDAVEADLGPIDVLVNNAGV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVLATE 170
Cdd:PRK07825   89 MPVGPFLDEPDAVTRRILDVNVYGVILGSKLAAPRMVPRGRGHVVNVASLAGKI-PVPGMATYCASKHAVVGFTDAARLE 167
                         170
                  ....*....|....
gi 1713980362 171 TAPFGVRVMVVEPS 184
Cdd:PRK07825  168 LRGTGVHVSVVLPS 181
adh_short_C2 pfam13561
Enoyl-(Acyl carrier protein) reductase; This domain is found in Enoyl-(Acyl carrier protein) ...
14-189 4.99e-30

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


Pssm-ID: 433310 [Multi-domain]  Cd Length: 236  Bit Score: 113.29  E-value: 4.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  14 SSRGFGRALVDAVLAAGDLVVATARRPEAL--AADLA-EYGDRVLPLalDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:pfam13561   4 NESGIGWAIARALAEEGAEVVLTDLNEALAkrVEELAeELGAAVLPC--DVTDEEQVEALVAAAVEKFGRLDILVNNAGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 AN--VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgtVVQFSSIGGRVGGsPGIASYQAAKFAVDGFSRVLA 168
Cdd:pfam13561  82 APklKGPFLDTSREDFDRALDVNLYSLFLLAKAALPLMKEGGS--IVNLSSIGAERVV-PNYNAYGAAKAALEALTRYLA 158
                         170       180
                  ....*....|....*....|.
gi 1713980362 169 TETAPFGVRVMVVEPSGFATD 189
Cdd:pfam13561 159 VELGPRGIRVNAISPGPIKTL 179
SDR_c4 cd08929
classical (c) SDR, subgroup 4; This subgroup has a canonical active site tetrad and a typical ...
10-193 5.30e-30

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


Pssm-ID: 187634 [Multi-domain]  Cd Length: 226  Bit Score: 112.99  E-value: 5.30e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAG 89
Cdd:cd08929     4 LVTGASRGIGEATARLLHAEGYRVGICARDEARLAAAAAQELEGVLGLAGDVRDEADVRRAVDAMEEAFGGLDALVNNAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSRVLAT 169
Cdd:cd08929    84 VGVMKPVEELTPEEWRLVLDTNLTGAFYCIHKAAPALLRRGGGTIVNVGSLAGK-NAFKGGAAYNASKFGLLGLSEAAML 162
                         170       180
                  ....*....|....*....|....
gi 1713980362 170 ETAPFGVRVMVVEPSGFATDWAGS 193
Cdd:cd08929   163 DLREANIRVVNVMPGSVDTGFAGS 186
PRK12939 PRK12939
short chain dehydrogenase; Provisional
1-189 8.15e-30

short chain dehydrogenase; Provisional


Pssm-ID: 183833 [Multi-domain]  Cd Length: 250  Bit Score: 113.14  E-value: 8.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVAT---ARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:PRK12939    2 ASNLAGKRALVTGAARGLGAAFAEALAEAGATVAFNdglAAEARELAAALEAAGGRAHAIAADLADPASVQRFFDAAAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAK 157
Cdd:PRK12939   82 LGGLDGLVNNAGITNSKSATELDIDTWDAVMNVNVRGTFLMLRAALPHLRDSGRGRIVNLASDTALWGA-PKLGAYVASK 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK12939  161 GAVIGMTRSLARELGGRGITVNAIAPGLTATE 192
SDR_c7 cd05354
classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a ...
11-208 1.06e-29

classical (c) SDR, subgroup 7; These proteins are members of the classical SDR family, with a canonical active site triad (and also an active site Asn) and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187612 [Multi-domain]  Cd Length: 235  Bit Score: 112.50  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVArfgrIDVLVNNAG 89
Cdd:cd05354     8 VTGANRGIGKAFVESLLAHGaKKVYAAVRDPGSAAHLVAKYGDKVVPLRLDVTDPESIKAAAAQAKD----VDVVINNAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YANV-SPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVLA 168
Cdd:cd05354    84 VLKPaTLLEEGALEALKQEMDVNVFGLLRLAQAFAPVLKANGGGAIVNLNSVAS-LKNFPAMGTYSASKSAAYSLTQGLR 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1713980362 169 TETAPFGVRVMVVEPSGFATDwagssMTVH-DVPEAYDATV 208
Cdd:cd05354   163 AELAAQGTLVLSVHPGPIDTR-----MAAGaGGPKESPETV 198
PRK12824 PRK12824
3-oxoacyl-ACP reductase;
6-192 1.52e-29

3-oxoacyl-ACP reductase;


Pssm-ID: 183773 [Multi-domain]  Cd Length: 245  Bit Score: 112.17  E-value: 1.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   6 PQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADL-AEYG---DRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK12824    2 KKIALVTGAKRGIGSAIARELLNDGYRVIATYFSGNDCAKDWfEEYGfteDQVRLKELDVTDTEECAEALAEIEEEEGPV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVD 161
Cdd:PRK12824   82 DILVNNAGITRDSVFKRMSHQEWNDVINTNLNSVFNVTQPLFAAMCEQGYGRIINISSVNGL-KGQFGQTNYSAAKAGMI 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATDWAG 192
Cdd:PRK12824  161 GFTKALASEGARYGITVNCIAPGYIATPMVE 191
R1PA_ADH_SDR_c cd08943
rhamnulose-1-phosphate aldolase/alcohol dehydrogenase, classical (c) SDRs; This family has ...
7-185 6.61e-28

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


Pssm-ID: 187647 [Multi-domain]  Cd Length: 250  Bit Score: 107.86  E-value: 6.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL--AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:cd08943     2 KVALVTGGASGIGLAIAKRLAAEGAAVVVADIDPEIAekVAEAAQGGPRALGVQCDVTSEAQVQSAFEQAVLEFGGLDIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFS 164
Cdd:cd08943    82 VSNAGIATSSPIAETSLEDWNRSMDINLTGHFLVSREAFRIMKSQGIGGNIVFNASKNAVAPGPNAAAYSAAKAAEAHLA 161
                         170       180
                  ....*....|....*....|.
gi 1713980362 165 RVLATETAPFGVRVMVVEPSG 185
Cdd:cd08943   162 RCLALEGGEDGIRVNTVNPDA 182
SDR_c11 cd05364
classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that ...
7-234 1.17e-27

classical (c) SDR, subgroup 11; SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187622 [Multi-domain]  Cd Length: 253  Bit Score: 107.50  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALvdAVLAA--GDLVVATAR---RPEALAADLAEYG---DRVLPLALDVTSPDAARAAVEAAVARF 78
Cdd:cd05364     4 KVAIITGSSSGIGAGT--AILFArlGARLALTGRdaeRLEETRQSCLQAGvseKKILLVVADLTEEEGQDRIISTTLAKF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  79 GRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQgAGTVVQFSSI-GGRvgGSPGIASYQAAK 157
Cdd:cd05364    82 GRLDILVNNAGILAKGGGEDQDIEEYDKVMNLNLRAVIYLTKLAVPHLIKT-KGEIVNVSSVaGGR--SFPGVLYYCISK 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEPSGFATDWaGSSMTVHDvpEAYDatvGAMNRLMRQNTAGAAGDPHRAAEIIV 234
Cdd:cd05364   159 AALDQFTRCTALELAPKGVRVNSVSPGVIVTGF-HRRMGMPE--EQYI---KFLSRAKETHPLGRPGTVDEVAEAIA 229
PRK07062 PRK07062
SDR family oxidoreductase;
7-178 1.23e-27

SDR family oxidoreductase;


Pssm-ID: 180818 [Multi-domain]  Cd Length: 265  Bit Score: 107.82  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEY-----GDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK07062    9 RVAVVTGGSSGIGLATVELLLEAGASVAICGRDEERLASAEARLrekfpGARLLAARCDVLDEADVAAFAAAVEARFGGV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVD 161
Cdd:PRK07062   89 DMLVNNAGQGRVSTFADTTDDAWRDELELKYFSVINPTRAFLPLLRASAAASIVCVNSLLAL-QPEPHMVATSAARAGLL 167
                         170
                  ....*....|....*..
gi 1713980362 162 GFSRVLATETAPFGVRV 178
Cdd:PRK07062  168 NLVKSLATELAPKGVRV 184
THN_reductase-like_SDR_c cd05362
tetrahydroxynaphthalene/trihydroxynaphthalene reductase-like, classical (c) SDRs; 1,3,6, ...
7-189 1.84e-27

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


Pssm-ID: 187620 [Multi-domain]  Cd Length: 243  Bit Score: 106.59  E-value: 1.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVV---ATARR-PEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:cd05362     4 KVALVTGASRGIGRAIAKRLARDGASVVvnyASSKAaAEEVVAEIEAAGGKAIAVQADVSDPSQVARLFDAAEKAFGGVD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgtVVQFSSIGGRVgGSPGIASYQAAKFAVDG 162
Cdd:cd05362    84 ILVNNAGVMLKKPIAETSEEEFDRMFTVNTKGAFFVLQEAAKRLRDGGR--IINISSSLTAA-YTPNYGAYAGSKAAVEA 160
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05362   161 FTRVLAKELGGRGITVNAVAPGPVDTD 187
HBDH_SDR_c cd08940
d-3-hydroxybutyrate dehydrogenase (HBDH), classical (c) SDRs; DHBDH, an NAD+ -dependent enzyme, ...
7-183 2.04e-27

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


Pssm-ID: 187644 [Multi-domain]  Cd Length: 258  Bit Score: 106.76  E-value: 2.04e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEA-----LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:cd08940     3 KVALVTGSTSGIGLGIARALAAAGANIVLNGFGDAAeieavRAGLAAKHGVKVLYHGADLSKPAAIEDMVAYAQRQFGGV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVD 161
Cdd:cd08940    83 DILVNNAGIQHVAPIEDFPTEKWDAIIALNLSAVFHTTRLALPHMKKQGWGRIINIASVHGLV-ASANKSAYVAAKHGVV 161
                         170       180
                  ....*....|....*....|..
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEP 183
Cdd:cd08940   162 GLTKVVALETAGTGVTCNAICP 183
SDR_c6 cd05350
classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a ...
11-186 2.17e-27

classical (c) SDR, subgroup 6; These proteins are members of the classical SDR family, with a canonical active site tetrad and a fairly well conserved typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187608 [Multi-domain]  Cd Length: 239  Bit Score: 106.26  E-value: 2.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd05350     3 ITGASSGIGRALAREFAKAGYNVALAARRTDrldELKAELLNPNPSVEVEILDVTDEERNQLVIAELEAELGGLDLVIIN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:cd05350    83 AGVGKGTSLGDLSFKAFRETIDTNLLGAAAILEAALPQFRAKGRGHLVLISSVAA-LRGLPGAAAYSASKAALSSLAESL 161
                         170
                  ....*....|....*....
gi 1713980362 168 ATETAPFGVRVMVVEPsGF 186
Cdd:cd05350   162 RYDVKKRGIRVTVINP-GF 179
carb_red_PTCR-like_SDR_c cd05324
Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs; PTCR is a classical SDR ...
10-192 2.98e-27

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


Pssm-ID: 187585 [Multi-domain]  Cd Length: 225  Bit Score: 105.78  E-value: 2.98e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDL-VVATAR---RPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd05324     4 LVTGANRGIGFEIVRQLAKSGPGtVILTARdveRGQAAVEKLRAEGLSVRFHQLDVTDDASIEAAADFVEEKYGGLDILV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDAD-FRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGgspgiASYQAAKFAVDGFS 164
Cdd:cd05324    84 NNAGIAFKGFDDSTPTREqARETMKTNFFGTVDVTQALLPLLKKSPAGRIVNVSSGLGSLT-----SAYGVSKAALNALT 158
                         170       180
                  ....*....|....*....|....*...
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDWAG 192
Cdd:cd05324   159 RILAKELKETGIKVNACCPGWVKTDMGG 186
PRK06124 PRK06124
SDR family oxidoreductase;
7-189 3.75e-27

SDR family oxidoreductase;


Pssm-ID: 235702 [Multi-domain]  Cd Length: 256  Bit Score: 106.34  E-value: 3.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK06124   12 QVALVTGSARGLGFEIARALAGAGAHVLVNGRNAATLeaaVAALRAAGGAAEALAFDIADEEAVAAAFARIDAEHGRLDI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGF 163
Cdd:PRK06124   92 LVNNVGARDRRPLAELDDAAIRALLETDLVAPILLSRLAAQRMKRQGYGRIIAITSIAGQV-ARAGDAVYPAAKQGLTGL 170
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK06124  171 MRALAAEFGPHGITSNAIAPGYFATE 196
PRK07454 PRK07454
SDR family oxidoreductase;
1-183 5.62e-27

SDR family oxidoreductase;


Pssm-ID: 180984 [Multi-domain]  Cd Length: 241  Bit Score: 105.43  E-value: 5.62e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:PRK07454    1 MSLNSMPRALITGASSGIGKATALAFAKAGWDLALVARSQdalEALAAELRSTGVKAAAYSIDLSNPEAIAPGIAELLEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAK 157
Cdd:PRK07454   81 FGCPDVLINNAGMAYTGPLLEMPLSDWQWVIQLNLTSVFQCCSAVLPGMRARGGGLIINVSSIAAR-NAFPQWGAYCVSK 159
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK07454  160 AALAAFTKCLAEEERSHGIRVCTITL 185
PRK06138 PRK06138
SDR family oxidoreductase;
7-214 1.15e-26

SDR family oxidoreductase;


Pssm-ID: 235712 [Multi-domain]  Cd Length: 252  Bit Score: 104.85  E-value: 1.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE--YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK06138    6 RVAIVTGAGSGIGRATAKLFAREGARVVVADRDAEAAERVAAAiaAGGRAFARQGDVGSAEAVEALVDFVAARWGRLDVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGFS 164
Cdd:PRK06138   86 VNNAGFGCGGTVVTTDEADWDAVMRVNVGGVFLWAKYAIPIMQRQGGGSIVNTASQLALAGG-RGRAAYVASKGAIASLT 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDA---TVGAMNRL 214
Cdd:PRK06138  165 RAMALDHATDGIRVNAVAPGTIDTPYFRRIFARHADPEALREalrARHPMNRF 217
ChcA_like_SDR_c cd05359
1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup ...
10-224 1.52e-26

1-cyclohexenylcarbonyl_coenzyme A_reductase (ChcA)_like, classical (c) SDRs; This subgroup contains classical SDR proteins, including members identified as 1-cyclohexenylcarbonyl coenzyme A reductase. ChcA of Streptomyces collinus is implicated in the final reduction step of shikimic acid to ansatrienin. ChcA shows sequence similarity to the SDR family of NAD-binding proteins, but it lacks the conserved Tyr of the characteristic catalytic site. This subgroup also contains the NADH-dependent enoyl-[acyl-carrier-protein(ACP)] reductase FabL from Bacillus subtilis. This enzyme participates in bacterial fatty acid synthesis, in type II fatty-acid synthases and catalyzes the last step in each elongation cycle. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187617 [Multi-domain]  Cd Length: 242  Bit Score: 104.36  E-value: 1.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLA----EYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd05359     2 LVTGGSRGIGKAIALRLAERGADVVINYRKSKDAAAEVAaeieELGGKAVVVRADVSQPQDVEEMFAAVKERFGRLDVLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSiGGRVGGSPGIASYQAAKFAVDGFSR 165
Cdd:cd05359    82 SNAAAGAFRPLSELTPAHWDAKMNTNLKALVHCAQQAAKLMRERGGGRIVAISS-LGSIRALPNYLAVGTAKAALEALVR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 166 VLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRLMRQNTAGAAG 224
Cdd:cd05359   161 YLAVELGPRGIRVNAVSPGVIDTDALAHFPNREDLLEAAAANTPAGRVGTPQDVADAVG 219
type1_17beta-HSD-like_SDR_c cd09806
human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, ...
11-238 2.41e-26

human estrogenic 17beta-hydroxysteroid dehydrogenase type 1 (type 1 17beta-HSD)-like, classical (c) SDRs; 17beta-hydroxysteroid dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. This classical SDR subgroup includes human type 1 17beta-HSD, human retinol dehydrogenase 8, zebrafish photoreceptor associated retinol dehydrogenase type 2, and a chicken ovary-specific 17beta-hydroxysteroid dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187666 [Multi-domain]  Cd Length: 258  Bit Score: 104.08  E-value: 2.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALvdAVLAAGD-----LVVATAR----RPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVArfGRI 81
Cdd:cd09806     5 ITGCSSGIGLHL--AVRLASDpskrfKVYATMRdlkkKGRLWEAAGALAGGTLETLQLDVCDSKSVAAAVERVTE--RHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVD 161
Cdd:cd09806    81 DVLVCNAGVGLLGPLEALSEDAMASVFDVNVFGTVRMLQAFLPDMKRRGSGRILVTSSVGG-LQGLPFNDVYCASKFALE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEP----SGFATDWAGSSMTVHDvPEAYDATVGAMNRLMRQNTA----GAAGDPHRAAEII 233
Cdd:cd09806   160 GLCESLAVQLLPFNVHLSLIECgpvhTAFMEKVLGSPEEVLD-RTADDITTFHFFYQYLAHSKqvfrEAAQNPEEVAEVF 238

                  ....*
gi 1713980362 234 VRTVR 238
Cdd:cd09806   239 LTAIR 243
PRK05993 PRK05993
SDR family oxidoreductase;
10-188 3.07e-26

SDR family oxidoreductase;


Pssm-ID: 180343 [Multi-domain]  Cd Length: 277  Bit Score: 104.34  E-value: 3.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEygdRVLPLALDVTSPDA-ARAAVEAAVARFGRIDVLVNNA 88
Cdd:PRK05993    8 LITGCSSGIGAYCARALQSDGWRVFATCRKEEDVAALEAE---GLEAFQLDYAEPESiAALVAQVLELSGGRLDALFNNG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRV-----GgspgiaSYQAAKFAVDGF 163
Cdd:PRK05993   85 AYGQPGAVEDLPTEALRAQFEANFFGWHDLTRRVIPVMRKQGQGRIVQCSSILGLVpmkyrG------AYNASKFAIEGL 158
                         170       180
                  ....*....|....*....|....*
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK05993  159 SLTLRMELQGSGIHVSLIEPGPIET 183
PRK13394 PRK13394
3-hydroxybutyrate dehydrogenase; Provisional
1-186 4.95e-26

3-hydroxybutyrate dehydrogenase; Provisional


Pssm-ID: 184025 [Multi-domain]  Cd Length: 262  Bit Score: 103.44  E-value: 4.95e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATA---RRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:PRK13394    2 MSNLNGKTAVVTGAASGIGKEIALELARAGAAVAIADlnqDGANAVADEINKAGGKAIGVAMDVTNEDAVNAGIDKVAER 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRR-QGAGTVVQFSSIGGRVgGSPGIASYQAA 156
Cdd:PRK13394   82 FGSVDILVSNAGIQIVNPIENYSFADWKKMQAIHVDGAFLTTKAALKHMYKdDRGGVVIYMGSVHSHE-ASPLKSAYVTA 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 157 KFAVDGFSRVLATETAPFGVRVMVVEPsGF 186
Cdd:PRK13394  161 KHGLLGLARVLAKEGAKHNVRSHVVCP-GF 189
TR_SDR_c cd05329
tropinone reductase-I and II (TR-1, and TR-II)-like, classical (c) SDRs; This subgroup ...
11-213 7.38e-26

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


Pssm-ID: 187590 [Multi-domain]  Cd Length: 251  Bit Score: 102.53  E-value: 7.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDR---VLPLALDVTSPDAARAAVEAAVARF-GRIDVLVN 86
Cdd:cd05329    11 VTGGTKGIGYAIVEELAGLGAEVYTCARNQKELDECLTEWREKgfkVEGSVCDVSSRSERQELMDTVASHFgGKLNILVN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGyANVS--PIETTEDaDFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGiASYQAAKFAVDGFS 164
Cdd:cd05329    91 NAG-TNIRkeAKDYTEE-DYSLIMSTNFEAAYHLSRLAHPLLKASGNGNIVFISSVAGVIAVPSG-APYGATKGALNQLT 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDWAGSSMtvhDVPEAYDATVG--AMNR 213
Cdd:cd05329   168 RSLACEWAKDNIRVNAVAPWVIATPLVEPVI---QQKENLDKVIErtPLKR 215
PRK06841 PRK06841
short chain dehydrogenase; Provisional
7-192 7.90e-26

short chain dehydrogenase; Provisional


Pssm-ID: 180723 [Multi-domain]  Cd Length: 255  Bit Score: 102.43  E-value: 7.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK06841   16 KVAVVTGGASGIGHAIAELFAAKGARVALLDRSEDVAEVAAQLLGGNAKGLVCDVSDSQSVEAAVAAVISAFGRIDILVN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRV 166
Cdd:PRK06841   96 SAGVALLAPAEDVSEEDWDKTIDINLKGSFLMAQAVGRHMIAAGGGKIVNLASQAGVV-ALERHVAYCASKAGVVGMTKV 174
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATD-----WAG 192
Cdd:PRK06841  175 LALEWGPYGITVNAISPTVVLTElgkkaWAG 205
PRK08226 PRK08226
SDR family oxidoreductase UcpA;
1-202 2.11e-25

SDR family oxidoreductase UcpA;


Pssm-ID: 181305 [Multi-domain]  Cd Length: 263  Bit Score: 101.80  E-value: 2.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGR--ALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARF 78
Cdd:PRK08226    1 MGKLTGKTALITGALQGIGEgiARVFARHGANLILLDISPEIEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  79 GRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKF 158
Cdd:PRK08226   81 GRIDILVNNAGVCRLGSFLDMSDEDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVADPGETAYALTKA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPsGFATDWAGSSMTVHDVPE 202
Cdd:PRK08226  161 AIVGLTKSLAVEYAQSGIRVNAICP-GYVRTPMAESIARQSNPE 203
MDH-like_SDR_c cd05352
mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes ...
11-189 2.72e-25

mannitol dehydrogenase (MDH)-like, classical (c) SDRs; NADP-mannitol dehydrogenase catalyzes the conversion of fructose to mannitol, an acyclic 6-carbon sugar. MDH is a tetrameric member of the SDR family. This subgroup also includes various other tetrameric SDRs, including Pichia stipitis D-arabinitol dehydrogenase (aka polyol dehydrogenase), Candida albicans Sou1p, a sorbose reductase, and Candida parapsilosis (S)-specific carbonyl reductase (SCR, aka S-specific alcohol dehydrogenase) which catalyzes the enantioselective reduction of 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187610 [Multi-domain]  Cd Length: 252  Bit Score: 101.25  E-value: 2.72e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVV--ATARRPEALAADLA-EYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05352    13 VTGGSRGIGLAIARALAEAGaDVAIiyNSAPRAEEKAEELAkKYGVKTKAYKCDVSSQESVEKTFKQIQKDFGKIDILIA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPG-IASYQAAKFAVDGFSR 165
Cdd:cd05352    93 NAGITVHKPALDYTYEQWNKVIDVNLNGVFNCAQAAAKIFKKQGKGSLIITASMSGTIVNRPQpQAAYNASKAAVIHLAK 172
                         170       180
                  ....*....|....*....|....
gi 1713980362 166 VLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05352   173 SLAVEWAKYFIRVNSISPGYIDTD 196
SPR-like_SDR_c cd05367
sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, ...
10-244 2.74e-25

sepiapterin reductase (SPR)-like, classical (c) SDRs; Human SPR, a member of the SDR family, catalyzes the NADP-dependent reduction of sepiaptern to 7,8-dihydrobiopterin (BH2). In addition to SPRs, this subgroup also contains Bacillus cereus yueD, a benzil reductase, which catalyzes the stereospecific reduction of benzil to (S)-benzoin. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187625 [Multi-domain]  Cd Length: 241  Bit Score: 100.82  E-value: 2.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGD--LVVATARRPEALAADLAE--YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd05367     3 ILTGASRGIGRALAEELLKRGSpsVVVLLARSEEPLQELKEElrPGLRVTTVKADLSDAAGVEQLLEAIRKLDGERDLLI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYAN-VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA-GTVVQFSSiGGRVGGSPGIASYQAAKFAVDGF 163
Cdd:cd05367    83 NNAGSLGpVSKIEFIDLDELQKYFDLNLTSPVCLTSTLLRAFKKRGLkKTVVNVSS-GAAVNPFKGWGLYCSSKAARDMF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 164 SRVLATETApfGVRVMVVEPSGFATDwagssMTVHDVPEAYDATVGAMNRLMRQNtaGAAGDPHRAAEIIVRTVRRGELP 243
Cdd:cd05367   162 FRVLAAEEP--DVRVLSYAPGVVDTD-----MQREIRETSADPETRSRFRSLKEK--GELLDPEQSAEKLANLLEKDKFE 232

                  .
gi 1713980362 244 S 244
Cdd:cd05367   233 S 233
TER_DECR_SDR_a cd05369
Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER ...
7-189 3.10e-25

Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR; TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187627 [Multi-domain]  Cd Length: 249  Bit Score: 100.74  E-value: 3.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGD-RVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:cd05369     4 KVAFITGGGTGIGKAIAKAFAELGASVAIAGRKPEVLeaaAEEISSATGgRAHPIQCDVRDPEAVEAAVDETLKEFGKID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDG 162
Cdd:cd05369    84 ILINNAAGNFLAPAESLSPNGFKTVIDIDLNGTFNTTKAVGKRLIEAKHGGSILNISATYAYTGSPFQVHSAAAKAGVDA 163
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05369   164 LTRSLAVEWGPYGIRVNAIAPGPIPTT 190
BKR_2_SDR_c cd05349
putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) ...
7-183 5.82e-25

putative beta-ketoacyl acyl carrier protein [ACP]reductase (BKR), subgroup 2, classical (c) SDR; This subgroup includes Rhizobium sp. NGR234 FabG1. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187607 [Multi-domain]  Cd Length: 246  Bit Score: 100.22  E-value: 5.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd05349     1 QVVLVTGASRGLGAAIARSFAREGaRVVVNYYRSTESAEAVAAEAGERAIAIQADVRDRDQVQAMIEEAKNHFGPVDTIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNA--GYA----NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVqfsSIGGRVGGSPGIA--SYQAAK 157
Cdd:cd05349    81 NNAliDFPfdpdQRKTFDTIDWEDYQQQLEGAVKGALNLLQAVLPDFKERGSGRVI---NIGTNLFQNPVVPyhDYTTAK 157
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:cd05349   158 AALLGFTRNMAKELGPYGITVNMVSG 183
PRK07074 PRK07074
SDR family oxidoreductase;
7-183 1.01e-24

SDR family oxidoreductase;


Pssm-ID: 180823 [Multi-domain]  Cd Length: 257  Bit Score: 99.84  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGD-RVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK07074    3 RTALVTGAAGGIGQALARRFLAAGDRVLALDIDAAALAAFADALGDaRFVPVACDLTDAASLAAALANAAAERGPVDVLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGG-RVGGSPgiaSYQAAKFAVDGFS 164
Cdd:PRK07074   83 ANAGAARAASLHDTTPASWRADNALNLEAAYLCVEAVLEGMLKRSRGAVVNIGSVNGmAALGHP---AYSAAKAGLIHYT 159
                         170
                  ....*....|....*....
gi 1713980362 165 RVLATETAPFGVRVMVVEP 183
Cdd:PRK07074  160 KLLAVEYGRFGIRANAVAP 178
PRK07063 PRK07063
SDR family oxidoreductase;
7-183 1.15e-24

SDR family oxidoreductase;


Pssm-ID: 235924 [Multi-domain]  Cd Length: 260  Bit Score: 99.74  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEY--GDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK07063    8 KVALVTGAAQGIGAAIARAFAREGAAVALADLDAALAeraAAAIARDvaGARVLAVPADVTDAASVAAAVAAAEEAFGPL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGyANV--SPIETTeDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGG-RVggSPGIASYQAAKF 158
Cdd:PRK07063   88 DVLVNNAG-INVfaDPLAMT-DEDWRRCFAVDLDGAWNGCRAVLPGMVERGRGSIVNIASTHAfKI--IPGCFPYPVAKH 163
                         170       180
                  ....*....|....*....|....*
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK07063  164 GLLGLTRALGIEYAARNVRVNAIAP 188
carb_red_sniffer_like_SDR_c cd05325
carbonyl reductase sniffer-like, classical (c) SDRs; Sniffer is an NADPH-dependent carbonyl ...
10-189 1.34e-24

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


Pssm-ID: 187586 [Multi-domain]  Cd Length: 233  Bit Score: 98.91  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDL-VVATARRPEALA--ADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05325     2 LITGASRGIGLELVRQLLARGNNtVIATCRDPSAATelAALGASHSRLHILELDVTDEIAESAEAVAERLGDAGLDVLIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAG-YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVG--GSPGIASYQAAKFAVDGF 163
Cdd:cd05325    82 NAGiLHSYGPASEVDSEDLLEVFQVNVLGPLLLTQAFLPLLLKGARAKIINISSRVGSIGdnTSGGWYSYRASKAALNML 161
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05325   162 TKSLAVELKRDGITVVSLHPGWVRTD 187
meso-BDH-like_SDR_c cd05366
meso-2,3-butanediol dehydrogenase-like, classical (c) SDRs; 2,3-butanediol dehydrogenases ...
11-178 1.35e-24

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


Pssm-ID: 187624 [Multi-domain]  Cd Length: 257  Bit Score: 99.37  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAA---DLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05366     7 ITGAAQGIGRAIAERLAADGfNIVLADLNLEEAAKStiqEISEAGYNAVAVGADVTDKDDVEALIDQAVEKFGSFDVMVN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSR 165
Cdd:cd05366    87 NAGIAPITPLLTITEEDLKKVYAVNVFGVLFGIQAAARQFKKLGhGGKIINASSIAGVQ-GFPNLGAYSASKFAVRGLTQ 165
                         170
                  ....*....|...
gi 1713980362 166 VLATETAPFGVRV 178
Cdd:cd05366   166 TAAQELAPKGITV 178
SDR_c9 cd08931
classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and ...
10-189 3.03e-24

classical (c) SDR, subgroup 9; This subgroup has the canonical active site tetrad and NAD-binding motif of the classical SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187636 [Multi-domain]  Cd Length: 227  Bit Score: 97.52  E-value: 3.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYG-DRVLPLALDVTSPDA-ARAAVEAAVARFGRIDVLVNN 87
Cdd:cd08931     4 FITGAASGIGRETALLFARNGWFVGLYDIDEDGLAALAAELGaENVVAGALDVTDRAAwAAALADFAAATGGRLDALFNN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVL 167
Cdd:cd08931    84 AGVGRGGPFEDVPLAAHDRMVDINVKGVLNGAYAALPYLKATPGARVINTASSSAIY-GQPDLAVYSATKFAVRGLTEAL 162
                         170       180
                  ....*....|....*....|..
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATD 189
Cdd:cd08931   163 DVEWARHGIRVADVWPWFVDTP 184
PRK06523 PRK06523
short chain dehydrogenase; Provisional
11-189 4.04e-24

short chain dehydrogenase; Provisional


Pssm-ID: 180604 [Multi-domain]  Cd Length: 260  Bit Score: 98.05  E-value: 4.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATAR-RPEALAADlAEYgdrvlpLALDVTSPDAARAAVEAAVARFGRIDVLVNNAG 89
Cdd:PRK06523   14 VTGGTKGIGAATVARLLEAGARVVTTARsRPDDLPEG-VEF------VAADLTTAEGCAAVARAVLERLGGVDILVHVLG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 yANVSP---IETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSRV 166
Cdd:PRK06523   87 -GSSAPaggFAALTDEEWQDELNLNLLAAVRLDRALLPGMIARGSGVIIHVTSIQRRLPLPESTTAYAAAKAALSTYSKS 165
                         170       180
                  ....*....|....*....|...
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK06523  166 LSKEVAPKGVRVNTVSPGWIETE 188
PRK06200 PRK06200
2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase; Provisional
1-201 5.75e-24

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


Pssm-ID: 235739 [Multi-domain]  Cd Length: 263  Bit Score: 97.72  E-value: 5.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:PRK06200    1 MGWLHGQVALITGGGSGIGRALVERFLAEGARVAVLERSAEKLASLRQRFGDHVLVVEGDVTSYADNQRAVDQTVDAFGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAG----YANVSPI-ETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGspGIASYQA 155
Cdd:PRK06200   81 LDCFVGNAGiwdyNTSLVDIpAETLDTAFDEIFNVNVKGYLLGAKAALPALKASGGSMIFTLSNSSFYPGG--GGPLYTA 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1713980362 156 AKFAVDGFSRVLATETAPfGVRVMVVEPSGFATDWAG------SSMTVHDVP 201
Cdd:PRK06200  159 SKHAVVGLVRQLAYELAP-KIRVNGVAPGGTVTDLRGpaslgqGETSISDSP 209
PRK08220 PRK08220
2,3-dihydroxybenzoate-2,3-dehydrogenase; Validated
1-204 5.80e-24

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


Pssm-ID: 236190 [Multi-domain]  Cd Length: 252  Bit Score: 97.65  E-value: 5.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWfITGSSRGFGRALVDAVLAAGDLVVATARrpealaADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:PRK08220    4 MDFSGKTVW-VTGAAQGIGYAVALAFVEAGAKVIGFDQ------AFLTQEDYPFATFVLDVSDAAAVAQVCQRLLAETGP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVggsP--GIASYQAAKF 158
Cdd:PRK08220   77 LDVLVNAAGILRMGATDSLSDEDWQQTFAVNAGGAFNLFRAVMPQFRRQRSGAIVTVGSNAAHV---PriGMAAYGASKA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFATD-----WA---GSSMTVHDVPEAY 204
Cdd:PRK08220  154 ALTSLAKCVGLELAPYGVRCNVVSPGSTDTDmqrtlWVdedGEQQVIAGFPEQF 207
PRK05867 PRK05867
SDR family oxidoreductase;
10-189 6.69e-24

SDR family oxidoreductase;


Pssm-ID: 135631 [Multi-domain]  Cd Length: 253  Bit Score: 97.41  E-value: 6.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK05867   13 LITGASTGIGKRVALAYVEAGAQVAIAARHLDALeklADEIGTSGGKVVPVCCDVSQHQQVTSMLDQVTAELGGIDIAVC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVGGSP-GIASYQAAKFAVDGFS 164
Cdd:PRK05867   93 NAGIITVTPMLDMPLEEFQRLQNTNVTGVFLTAQAAAKAMVKQGqGGVIINTASMSGHIINVPqQVSHYCASKAAVIHLT 172
                         170       180
                  ....*....|....*....|....*
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK05867  173 KAMAVELAPHKIRVNSVSPGYILTE 197
DH-DHB-DH_SDR_c cd05331
2,3 dihydro-2,3 dihydrozybenzoate dehydrogenases, classical (c) SDRs; 2,3 dihydro-2,3 ...
10-204 7.19e-24

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


Pssm-ID: 187592 [Multi-domain]  Cd Length: 244  Bit Score: 97.15  E-value: 7.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEalaaDLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAG 89
Cdd:cd05331     2 IVTGAAQGIGRAVARHLLQAGATVIALDLPFV----LLLEYGDPLRLTPLDVADAAAVREVCSRLLAEHGPIDALVNCAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVqfsSIGGRVGGSP--GIASYQAAKFAVDGFSRVL 167
Cdd:cd05331    78 VLRPGATDPLSTEDWEQTFAVNVTGVFNLLQAVAPHMKDRRTGAIV---TVASNAAHVPriSMAAYGASKAALASLSKCL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATD-----WA---GSSMTVHDVPEAY 204
Cdd:cd05331   155 GLELAPYGVRCNVVSPGSTDTAmqrtlWHdedGAAQVIAGVPEQF 199
BKR_3_SDR_c cd05345
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) ...
11-183 7.50e-24

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 3, classical (c) SDR; This subgroup includes the putative Brucella melitensis biovar Abortus 2308 BKR, FabG, Mesorhizobium loti MAFF303099 FabG, and other classical SDRs. BKR, a member of the SDR family, catalyzes the NADPH-dependent reduction of acyl carrier protein in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of 4 elongation steps, which are repeated to extend the fatty acid chain thru the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I Fas utilizes one or 2 multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187603 [Multi-domain]  Cd Length: 248  Bit Score: 97.08  E-value: 7.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:cd05345    10 VTGAGSGFGEGIARRFAQEGARVVIADINADGAERVAADIGEAAIAIQADVTKRADVEAMVEAALSKFGRLDILVNNAGI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVS-PIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVLAT 169
Cdd:cd05345    90 THRNkPMLEVDEEEFDRVFAVNVKSIYLSAQALVPHMEEQGGGVIINIASTAG-LRPRPGLTWYNASKGWVVTATKAMAV 168
                         170
                  ....*....|....
gi 1713980362 170 ETAPFGVRVMVVEP 183
Cdd:cd05345   169 ELAPRNIRVNCLCP 182
PRK07814 PRK07814
SDR family oxidoreductase;
5-188 7.50e-24

SDR family oxidoreductase;


Pssm-ID: 181131 [Multi-domain]  Cd Length: 263  Bit Score: 97.54  E-value: 7.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK07814    9 DDQVAVVTGAGRGLGAAIALAFAEAGADVLIAARTESQLdevAEQIRAAGRRAHVVAADLAHPEATAGLAGQAVEAFGRL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALP-VLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAV 160
Cdd:PRK07814   89 DIVVNNVGGTMPNPLLSTSTKDLADAFTFNVATAHALTVAAVPlMLEHSGGGSVINISSTMGRLAG-RGFAAYGTAKAAL 167
                         170       180
                  ....*....|....*....|....*...
gi 1713980362 161 DGFSRVLATETAPfGVRVMVVEPSGFAT 188
Cdd:PRK07814  168 AHYTRLAALDLCP-RIRVNAIAPGSILT 194
PRK08219 PRK08219
SDR family oxidoreductase;
11-189 9.89e-24

SDR family oxidoreductase;


Pssm-ID: 181298 [Multi-domain]  Cd Length: 227  Bit Score: 96.16  E-value: 9.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAvLAAGDLVVATARRPEALAADLAEYgDRVLPLALDVTSPDAARAAVEAavarFGRIDVLVNNAGY 90
Cdd:PRK08219    8 ITGASRGIGAAIARE-LAPTHTLLLGGRPAERLDELAAEL-PGATPFPVDLTDPEAIAAAVEQ----LGRLDVLVHNAGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSRVLATE 170
Cdd:PRK08219   82 ADLGPVAESTVDEWRATLEVNVVAPAELTRLLLPALRAAH-GHVVFINSGAGL-RANPGWGSYAASKFALRALADALREE 159
                         170
                  ....*....|....*....
gi 1713980362 171 TAPfGVRVMVVEPSGFATD 189
Cdd:PRK08219  160 EPG-NVRVTSVHPGRTDTD 177
PRK05650 PRK05650
SDR family oxidoreductase;
10-265 2.07e-23

SDR family oxidoreductase;


Pssm-ID: 235545 [Multi-domain]  Cd Length: 270  Bit Score: 96.26  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAG-DLVVATARRP--EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK05650    4 MITGAASGLGRAIALRWAREGwRLALADVNEEggEETLKLLREAGGDGFYQRCDVRDYSQLTALAQACEEKWGGIDVIVN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGFSRV 166
Cdd:PRK05650   84 NAGVASGGFFEELSLEDWDWQIAINLMGVVKGCKAFLPLFKRQKSGRIVNIASMAGLMQG-PAMSSYNVAKAGVVALSET 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATDWAGSSMTvhdvpeaydaTVGAMNRLMRQNTAGAAGDPHRAAEIIVRTVRRGELpshl 246
Cdd:PRK05650  163 LLVELADDEIGVHVVCPSFFQTNLLDSFRG----------PNPAMKAQVGKLLEKSPITAADIADYIYQQVAKGEF---- 228
                         250
                  ....*....|....*....
gi 1713980362 247 llgvnaatMALDHDRRRLA 265
Cdd:PRK05650  229 --------LILPHEQGRRA 239
PRK06171 PRK06171
sorbitol-6-phosphate 2-dehydrogenase; Provisional
11-183 2.59e-23

sorbitol-6-phosphate 2-dehydrogenase; Provisional


Pssm-ID: 180439 [Multi-domain]  Cd Length: 266  Bit Score: 96.23  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVAtarrpealaADL---AEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK06171   14 VTGGSSGIGLAIVKELLANGANVVN---------ADIhggDGQHENYQFVPTDVSSAEEVNHTVAEIIEKFGRIDGLVNN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AG----------YANVSPIETTEdADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAK 157
Cdd:PRK06171   85 AGiniprllvdeKDPAGKYELNE-AAFDKMFNINQKGVFLMSQAVARQMVKQHDGVIVNMSSEAG-LEGSEGQSCYAATK 162
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK06171  163 AALNSFTRSWAKELGKHNIRVVGVAP 188
PRK07060 PRK07060
short chain dehydrogenase; Provisional
11-184 2.61e-23

short chain dehydrogenase; Provisional


Pssm-ID: 180817 [Multi-domain]  Cd Length: 245  Bit Score: 95.55  E-value: 2.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRvlPLALDVTSPdaarAAVEAAVARFGRIDVLVNNAGY 90
Cdd:PRK07060   14 VTGASSGIGRACAVALAQRGARVVAAARNAAALDRLAGETGCE--PLRLDVGDD----AAIRAALAAAGAFDGLVNCAGI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVLAT 169
Cdd:PRK07060   88 ASLESALDMTAEGFDRVMAVNARGAALVARHVARAMIAAGrGGSIVNVSSQAALV-GLPDHLAYCASKAALDAITRVLCV 166
                         170
                  ....*....|....*
gi 1713980362 170 ETAPFGVRVMVVEPS 184
Cdd:PRK07060  167 ELGPHGIRVNSVNPT 181
PRK08213 PRK08213
gluconate 5-dehydrogenase; Provisional
11-188 3.10e-23

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181295 [Multi-domain]  Cd Length: 259  Bit Score: 95.78  E-value: 3.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08213   17 VTGGSRGLGLQIAEALGEAGARVVLSARKAEELeeaAAHLEALGIDALWIAADVADEADIERLAEETLERFGHVDILVNN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPV-LRRQGAGTVVQFSSIGGRVGGSPGI---ASYQAAKFAVDGF 163
Cdd:PRK08213   97 AGATWGAPAEDHPVEAWDKVMNLNVRGLFLLSQAVAKRsMIPRGYGRIINVASVAGLGGNPPEVmdtIAYNTSKGAVINF 176
                         170       180
                  ....*....|....*....|....*
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK08213  177 TRALAAEWGPHGIRVNAIAPGFFPT 201
PRK12827 PRK12827
short chain dehydrogenase; Provisional
1-191 3.57e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237219 [Multi-domain]  Cd Length: 249  Bit Score: 95.17  E-value: 3.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRP-------EALAADLAEYGDRVLPLALDVTSPDAARAAVEA 73
Cdd:PRK12827    1 MASLDSRRVLITGGSGGLGRAIAVRLAADGADVIVLDIHPmrgraeaDAVAAGIEAAGGKALGLAFDVRDFAATRAALDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  74 AVARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAAL-PVLRRQGAGTVVQFSSIGGrVGGSPGIAS 152
Cdd:PRK12827   81 GVEEFGRLDILVNNAGIATDAAFAELSIEEWDDVIDVNLDGFFNVTQAALpPMIRARRGGRIVNIASVAG-VRGNRGQVN 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1713980362 153 YQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDWA 191
Cdd:PRK12827  160 YAASKAGLIGLTKTLANELAPRGITVNAVAPGAINTPMA 198
PRK08267 PRK08267
SDR family oxidoreductase;
10-184 5.10e-23

SDR family oxidoreductase;


Pssm-ID: 236210 [Multi-domain]  Cd Length: 260  Bit Score: 95.00  E-value: 5.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGD-RVLPLALDVTSPDAARAAVEA-AVARFGRIDVLVNN 87
Cdd:PRK08267    5 FITGAASGIGRATALLFAAEGWRVGAYDINEAGLAALAAELGAgNAWTGALDVTDRAAWDAALADfAAATGGRLDVLFNN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK08267   85 AGILRGGPFEDIPLEAHDRVIDINVKGVLNGAHAALPYLKATPGARVINTSSASA-IYGQPGLAVYSATKFAVRGLTEAL 163
                         170
                  ....*....|....*..
gi 1713980362 168 ATETAPFGVRVMVVEPS 184
Cdd:PRK08267  164 DLEWRRHGIRVADVMPL 180
PRK05872 PRK05872
short chain dehydrogenase; Provisional
1-189 5.56e-23

short chain dehydrogenase; Provisional


Pssm-ID: 235633 [Multi-domain]  Cd Length: 296  Bit Score: 95.81  E-value: 5.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYG--DRVLPLALDVTSPDAARAAVEAAVARF 78
Cdd:PRK05872    4 MTSLAGKVVVVTGAARGIGAELARRLHARGAKLALVDLEEAELAALAAELGgdDRVLTVVADVTDLAAMQAAAEEAVERF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  79 GRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGrVGGSPGIASYQAAKF 158
Cdd:PRK05872   84 GGIDVVVANAGIASGGSVAQVDPDAFRRVIDVNLLGVFHTVRATLPALIERR-GYVLQVSSLAA-FAAAPGMAAYCASKA 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK05872  162 GVEAFANALRLEVAHHGVTVGSAYLSWIDTD 192
fabG PRK08642
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
5-181 6.58e-23

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


Pssm-ID: 181517 [Multi-domain]  Cd Length: 253  Bit Score: 94.77  E-value: 6.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLA-EYGDRVLPLALDVTSPDAARAAVEAAVARFGR-ID 82
Cdd:PRK08642    4 SEQTVLVTGGSRGLGAAIARAFAREGARVVVNYHQSEDAAEALAdELGDRAIALQADVTDREQVQAMFATATEHFGKpIT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNA--GY----ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVqfsSIGGRVGGSPGIA--SYQ 154
Cdd:PRK08642   84 TVVNNAlaDFsfdgDARKKADDITWEDFQQQLEGSVKGALNTIQAALPGMREQGFGRII---NIGTNLFQNPVVPyhDYT 160
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 155 AAKFAVDGFSRVLATETAPFGVRVMVV 181
Cdd:PRK08642  161 TAKAALLGLTRNLAAELGPYGITVNMV 187
PRK12828 PRK12828
short chain dehydrogenase; Provisional
5-184 6.99e-23

short chain dehydrogenase; Provisional


Pssm-ID: 237220 [Multi-domain]  Cd Length: 239  Bit Score: 94.48  E-value: 6.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEY-GDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK12828    6 QGKVVAITGGFGGLGRATAAWLAARGARVALIGRGAAPLSQTLPGVpADALRIGGIDLVDPQAARRAVDEVNRQFGRLDA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGF 163
Cdd:PRK12828   86 LVNIAGAFVWGTIADGDADTWDRMYGVNVKTTLNASKAALPALTASGGGRIVNIGAGAALKAG-PGMGAYAAAKAGVARL 164
                         170       180
                  ....*....|....*....|.
gi 1713980362 164 SRVLATETAPFGVRVMVVEPS 184
Cdd:PRK12828  165 TEALAAELLDRGITVNAVLPS 185
PRK07523 PRK07523
gluconate 5-dehydrogenase; Provisional
11-188 1.04e-22

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 236040 [Multi-domain]  Cd Length: 255  Bit Score: 94.06  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAA---DLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK07523   15 VTGSSQGIGYALAEGLAQAGAEVILNGRDPAKLAAaaeSLKGQGLSAHALAFDVTDHDAVRAAIDAFEAEIGPIDILVNN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK07523   95 AGMQFRTPLEDFPADAFERLLRTNISSVFYVGQAVARHMIARGAGKIINIASVQSAL-ARPGIAPYTATKGAVGNLTKGM 173
                         170       180
                  ....*....|....*....|.
gi 1713980362 168 ATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK07523  174 ATDWAKHGLQCNAIAPGYFDT 194
PRK06172 PRK06172
SDR family oxidoreductase;
1-189 1.09e-22

SDR family oxidoreductase;


Pssm-ID: 180440 [Multi-domain]  Cd Length: 253  Bit Score: 94.05  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:PRK06172    2 SMTFSGKVALVTGGAAGIGRATALAFAREGAKVVVADRDAaggEETVALIREAGGEALFVACDVTRDAEVKALVEQTIAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAGY--ANVSPIETTEdADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQA 155
Cdd:PRK06172   82 YGRLDYAFNNAGIeiEQGRLAEGSE-AEFDAIMGVNVKGVWLCMKYQIPLMLAQGGGAIVNTASVAG-LGAAPKMSIYAA 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1713980362 156 AKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK06172  160 SKHAVIGLTKSAAIEYAKKGIRVNAVCPAVIDTD 193
PRK12937 PRK12937
short chain dehydrogenase; Provisional
7-189 1.22e-22

short chain dehydrogenase; Provisional


Pssm-ID: 171821 [Multi-domain]  Cd Length: 245  Bit Score: 93.65  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVAT----ARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK12937    6 KVAIVTGASRGIGAAIARRLAADGFAVAVNyagsAAAADELVAEIEAAGGRAIAVQADVADAAAVTRLFDAAETAFGRID 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVggsPGIASYQAAKFAVDG 162
Cdd:PRK12937   86 VLVNNAGVMPLGTIADFDLEDFDRTIATNLRGAFVVLREAARHLGQGGRIINLSTSVIALPL---PGYGPYAASKAAVEG 162
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK12937  163 LVHVLANELRGRGITVNAVAPGPVATE 189
BphB-like_SDR_c cd05348
cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2, ...
7-192 2.45e-22

cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB)-like, classical (c) SDRs; cis-biphenyl-2,3-dihydrodiol-2,3-dehydrogenase (BphB) is a classical SDR, it is of particular importance for its role in the degradation of biphenyl/polychlorinated biphenyls(PCBs); PCBs are a significant source of environmental contamination. This subgroup also includes Pseudomonas putida F1 cis-biphenyl-1,2-dihydrodiol-1,2-dehydrogenase (aka cis-benzene glycol dehydrogenase, encoded by the bnzE gene), which participates in benzene metabolism. In addition it includes Pseudomonas sp. C18 putative 1,2-dihydroxy-1,2-dihydronaphthalene dehydrogenase (aka dibenzothiophene dihydrodiol dehydrogenase, encoded by the doxE gene) which participates in an upper naphthalene catabolic pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187606 [Multi-domain]  Cd Length: 257  Bit Score: 93.19  E-value: 2.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05348     5 EVALITGGGSGLGRALVERFVAEGAKVAVLDRSAEKVAELRADFGDAVVGVEGDVRSLADNERAVARCVERFGKLDCFIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGY--ANVSPIETTE---DADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGspGIASYQAAKFAVD 161
Cdd:cd05348    85 NAGIwdYSTSLVDIPEeklDEAFDELFHINVKGYILGAKAALPALYATEGSVIFTVSNAGFYPGG--GGPLYTASKHAVV 162
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 162 GFSRVLATETAPFgVRVMVVEPSGFATDWAG 192
Cdd:cd05348   163 GLVKQLAYELAPH-IRVNGVAPGGMVTDLRG 192
PRK06484 PRK06484
short chain dehydrogenase; Validated
2-183 2.48e-22

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 96.46  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   2 STQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK06484    1 SKAQSRVVLVTGAAGGIGRAACQRFARAGDQVVVADRNVERARERADSLGPDHHALAMDVSDEAQIREGFEQLHREFGRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDA--DFRAQFETNFWGVYHVTRAALPVLRRQGAGT-VVQFSSIGGRVgGSPGIASYQAAKF 158
Cdd:PRK06484   81 DVLVNNAGVTDPTMTATLDTTleEFARLQAINLTGAYLVAREALRLMIEQGHGAaIVNVASGAGLV-ALPKRTAYSASKA 159
                         170       180
                  ....*....|....*....|....*
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK06484  160 AVISLTRSLACEWAAKGIRVNAVLP 184
PRK06484 PRK06484
short chain dehydrogenase; Validated
4-233 2.83e-22

short chain dehydrogenase; Validated


Pssm-ID: 168574 [Multi-domain]  Cd Length: 520  Bit Score: 96.07  E-value: 2.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   4 QDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK06484  267 ESPRVVAITGGARGIGRAVADRFAAAGDRLLIIDRDAEGAKKLAEALGDEHLSVQADITDEAAVESAFAQIQARWGRLDV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANV-SPIETTEDADFRAQFETNFWGVYHVTRAALPVLRrqGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDG 162
Cdd:PRK06484  347 LVNNAGIAEVfKPSLEQSAEDFTRVYDVNLSGAFACARAAARLMS--QGGVIVNLGSIAS-LLALPPRNAYCASKAAVTM 423
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATDWAgssmtvhdvpEAYDATVGA-MNRLMRQNTAGAAGDPHRAAEII 233
Cdd:PRK06484  424 LSRSLACEWAPAGIRVNTVAPGYIETPAV----------LALKASGRAdFDSIRRRIPLGRLGDPEEVAEAI 485
DltE COG3967
Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall ...
10-192 3.00e-22

Short-chain dehydrogenase involved in D-alanine esterification of teichoic acids [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443167 [Multi-domain]  Cd Length: 246  Bit Score: 92.92  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYgDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAG 89
Cdd:COG3967     9 LITGGTSGIGLALAKRLHARGNTVIITGRREEKLEEAAAAN-PGLHTIVLDVADPASIAALAEQVTAEFPDLNVLINNAG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 ----YANVSPIETTEDAdfRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSR 165
Cdd:COG3967    88 imraEDLLDEAEDLADA--EREITTNLLGPIRLTAAFLPHLKAQPEAAIVNVSSGLAFV-PLAVTPTYSATKAALHSYTQ 164
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 166 VLATETAPFGVRVMVVEPSGFATDWAG 192
Cdd:COG3967   165 SLRHQLKDTSVKVIELAPPAVDTDLTG 191
PRK09242 PRK09242
SDR family oxidoreductase;
1-183 3.27e-22

SDR family oxidoreductase;


Pssm-ID: 181721 [Multi-domain]  Cd Length: 257  Bit Score: 92.89  E-value: 3.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEY-----GDRVLPLALDVTSPDAARAAVEAAV 75
Cdd:PRK09242    4 RWRLDGQTALITGASKGIGLAIAREFLGLGADVLIVARDADALAQARDELaeefpEREVHGLAADVSDDEDRRAILDWVE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  76 ARFGRIDVLVNNAGyANVS--PIETTEDaDFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGiASY 153
Cdd:PRK09242   84 DHWDGLHILVNNAG-GNIRkaAIDYTED-EWRGIFETNLFSAFELSRYAHPLLKQHASSAIVNIGSVSGLTHVRSG-APY 160
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 154 QAAKFAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK09242  161 GMTKAALLQMTRNLAVEWAEDGIRVNAVAP 190
RDH_SDR_c cd08933
retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members ...
7-188 3.84e-22

retinal dehydrogenase-like, classical (c) SDR; These classical SDRs includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. 17beta-dehydrogenases are a group of isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the short-chain dehydrogenases/reductase family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187638 [Multi-domain]  Cd Length: 261  Bit Score: 92.98  E-value: 3.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLAL----DVTSPDAARAAVEAAVARFGRID 82
Cdd:cd08933    10 KVVIVTGGSRGIGRGIVRAFVENGAKVVFCARGEAAGQALESELNRAGPGSCKfvpcDVTKEEDIKTLISVTVERFGRID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYAnvSPIETTEDA---DFRAQFETNFWGVYHVTRAALPVLrRQGAGTVVQFSSIGGRVGGSPGiASYQAAKFA 159
Cdd:cd08933    90 CLVNNAGWH--PPHQTTDETsaqEFRDLLNLNLISYFLASKYALPHL-RKSQGNIINLSSLVGSIGQKQA-APYVATKGA 165
                         170       180
                  ....*....|....*....|....*....
gi 1713980362 160 VDGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:cd08933   166 ITAMTKALAVDESRYGVRVNCISPGNIWT 194
PRK07478 PRK07478
short chain dehydrogenase; Provisional
1-216 4.88e-22

short chain dehydrogenase; Provisional


Pssm-ID: 180993 [Multi-domain]  Cd Length: 254  Bit Score: 92.30  E-value: 4.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVAR 77
Cdd:PRK07478    1 MMRLNGKVAIITGASSGIGRAAAKLFAREGAKVVVGARRQAELdqlVAEIRAEGGEAVALAGDVRDEAYAKALVALAVER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  78 FGRIDVLVNNAG-YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAA 156
Cdd:PRK07478   81 FGGLDIAFNNAGtLGEMGPVAEMSLEGWRETLATNLTSAFLGAKHQIPAMLARGGGSLIFTSTFVGHTAGFPGMAAYAAS 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1713980362 157 KFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwAGSSMTvhDVPEAYDATVG--AMNRLMR 216
Cdd:PRK07478  161 KAGLIGLTQVLAAEYGAQGIRVNALLPGGTDTP-MGRAMG--DTPEALAFVAGlhALKRMAQ 219
PRK12935 PRK12935
acetoacetyl-CoA reductase; Provisional
1-202 5.69e-22

acetoacetyl-CoA reductase; Provisional


Pssm-ID: 183832 [Multi-domain]  Cd Length: 247  Bit Score: 91.99  E-value: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVV----ATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVA 76
Cdd:PRK12935    1 MVQLNGKVAIVTGGAKGIGKAITVALAQEGAKVVinynSSKEAAENLVNELGKEGHDVYAVQADVSKVEDANRLVEEAVN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  77 RFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSpGIASYQAA 156
Cdd:PRK12935   81 HFGKVDILVNNAGITRDRTFKKLNREDWERVIDVNLSSVFNTTSAVLPYITEAEEGRIISISSIIGQAGGF-GQTNYSAA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1713980362 157 KFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwagssmTVHDVPE 202
Cdd:PRK12935  160 KAGMLGFTKSLALELAKTNVTVNAICPGFIDTE------MVAEVPE 199
secoisolariciresinol-DH_like_SDR_c cd05326
secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; ...
5-214 6.98e-22

secoisolariciresinol dehydrogenase (secoisolariciresinol-DH)-like, classical (c) SDRs; Podophyllum secoisolariciresinol-DH is a homo tetrameric, classical SDR that catalyzes the NAD-dependent conversion of (-)-secoisolariciresinol to (-)-matairesinol via a (-)-lactol intermediate. (-)-Matairesinol is an intermediate to various 8'-lignans, including the cancer-preventive mammalian lignan, and those involved in vascular plant defense. This subgroup also includes rice momilactone A synthase which catalyzes the conversion of 3beta-hydroxy-9betaH-pimara-7,15-dien-19,6beta-olide into momilactone A, Arabidopsis ABA2 which during abscisic acid (ABA) biosynthesis, catalyzes the conversion of xanthoxin to abscisic aldehyde and, maize Tasselseed2 which participate in the maize sex determination pathway. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187587 [Multi-domain]  Cd Length: 249  Bit Score: 91.75  E-value: 6.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLA-LDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:cd05326     3 DGKVAIITGGASGIGEATARLFAKHGARVVIADIDDDAGQAVAAELGDPDISFVhCDVTVEADVRAAVDTAVARFGRLDI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSP--IETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSpGIASYQAAKFAVD 161
Cdd:cd05326    83 MFNNAGVLGAPCysILETSLEEFERVLDVNVYGAFLGTKHAARVMIPAKKGSIVSVASVAGVVGGL-GPHAYTASKHAVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDvpEAYDATVGAMNRL 214
Cdd:cd05326   162 GLTRSAATELGEHGIRVNCVSPYGVATPLLTAGFGVED--EAIEEAVRGAANL 212
PRK06500 PRK06500
SDR family oxidoreductase;
11-188 7.35e-22

SDR family oxidoreductase;


Pssm-ID: 235816 [Multi-domain]  Cd Length: 249  Bit Score: 91.94  E-value: 7.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:PRK06500   11 ITGGTSGIGLETARQFLAEGARVAITGRDPASLEAARAELGESALVIRADAGDVAAQKALAQALAEAFGRLDAVFINAGV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgtVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVLATE 170
Cdd:PRK06500   91 AKFAPLEDWDEAMFDRSFNTNVKGPYFLIQALLPLLANPAS--IVLNGSINAHI-GMPNSSVYAASKAALLSLAKTLSGE 167
                         170
                  ....*....|....*...
gi 1713980362 171 TAPFGVRVMVVEPSGFAT 188
Cdd:PRK06500  168 LLPRGIRVNAVSPGPVQT 185
RhlG_SDR_c cd08942
RhlG and related beta-ketoacyl reductases, classical (c) SDRs; Pseudomonas aeruginosa RhlG is ...
11-206 1.06e-21

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


Pssm-ID: 187646 [Multi-domain]  Cd Length: 250  Bit Score: 91.39  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEA---LAADLAEYGDrVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd08942    11 VTGGSRGIGRMIAQGFLEAGARVIISARKAEAcadAAEELSAYGE-CIAIPADLSSEEGIEALVARVAERSDRLDVLVNN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA----GTVVQFSSIGGRVGGSPGIASYQAAKFAVDGF 163
Cdd:cd08942    90 AGATWGAPLEAFPESGWDKVMDINVKSVFFLTQALLPLLRAAATaenpARVINIGSIAGIVVSGLENYSYGASKAAVHQL 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFAtdwagSSMTVH--DVPEAYDA 206
Cdd:cd08942   170 TRKLAKELAGEHITVNAIAPGRFP-----SKMTAFllNDPAALEA 209
7_alpha_HSDH_SDR_c cd05365
7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial ...
11-230 1.16e-21

7 alpha-hydroxysteroid dehydrogenase (7 alpha-HSDH), classical (c) SDRs; This bacterial subgroup contains 7 alpha-HSDHs, including Escherichia coli 7 alpha-HSDH. 7 alpha-HSDH, a member of the SDR family, catalyzes the NAD+ -dependent dehydrogenation of a hydroxyl group at position 7 of the steroid skeleton of bile acids. In humans the two primary bile acids are cholic and chenodeoxycholic acids, these are formed from cholesterol in the liver. Escherichia coli 7 alpha-HSDH dehydroxylates these bile acids in the human intestine. Mammalian 7 alpha-HSDH activity has been found in livers. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187623 [Multi-domain]  Cd Length: 242  Bit Score: 91.09  E-value: 1.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVAT---ARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd05365     4 VTGGAAGIGKAIAGTLAKAGASVVIAdlkSEGAEAVAAAIQQAGGQAIGLECNVTSEQDLEAVVKATVSQFGGITILVNN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIET-TEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRV 166
Cdd:cd05365    84 AGGGGPKPFDMpMTEEDFEWAFKLNLFSAFRLSQLCAPHMQKAGGGAILNISSMSSEN-KNVRIAAYGSSKAAVNHMTRN 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATDWAGSSMTvhdvPEaydatvgaMNRLMRQNT-AGAAGDPHRAA 230
Cdd:cd05365   163 LAFDLGPKGIRVNAVAPGAVKTDALASVLT----PE--------IERAMLKHTpLGRLGEPEDIA 215
PRK07856 PRK07856
SDR family oxidoreductase;
7-192 1.24e-21

SDR family oxidoreductase;


Pssm-ID: 236116 [Multi-domain]  Cd Length: 252  Bit Score: 91.15  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARR-PEALAADLAEYgdrvlpLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK07856    7 RVVLVTGGTRGIGAGIARAFLAAGATVVVCGRRaPETVDGRPAEF------HAADVRDPDQVAALVDAIVERHGRLDVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQ-GAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFS 164
Cdd:PRK07856   81 NNAGGSPYALAAEASPRFHEKIVELNLLAPLLVAQAANAVMQQQpGGGSIVNIGSVSGR-RPSPGTAAYGAAKAGLLNLT 159
                         170       180
                  ....*....|....*....|....*...
gi 1713980362 165 RVLATETAPfGVRVMVVEPSGFATDWAG 192
Cdd:PRK07856  160 RSLAVEWAP-KVRVNAVVVGLVRTEQSE 186
PRK06701 PRK06701
short chain dehydrogenase; Provisional
7-183 1.31e-21

short chain dehydrogenase; Provisional


Pssm-ID: 235853 [Multi-domain]  Cd Length: 290  Bit Score: 92.02  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALvdAVLAA---GDLVVA----------TARRPEAlaadlaeYGDRVLPLALDVTSPDAARAAVEA 73
Cdd:PRK06701   47 KVALITGGDSGIGRAV--AVLFAkegADIAIVyldehedaneTKQRVEK-------EGVKCLLIPGDVSDEAFCKDAVEE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  74 AVARFGRIDVLVNNAGYA-NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgtVVQFSSIGGrVGGSPGIAS 152
Cdd:PRK06701  118 TVRELGRLDILVNNAAFQyPQQSLEDITAEQLDKTFKTNIYSYFHMTKAALPHLKQGSA--IINTGSITG-YEGNETLID 194
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 153 YQAAKFAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK06701  195 YSATKGAIHAFTRSLAQSLVQKGIRVNAVAP 225
PRK06947 PRK06947
SDR family oxidoreductase;
11-234 1.45e-21

SDR family oxidoreductase;


Pssm-ID: 180771 [Multi-domain]  Cd Length: 248  Bit Score: 91.02  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRAlvDAVLAA------GDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK06947    7 ITGASRGIGRA--TAVLAAargwsvGINYARDAAAAEETADAVRAAGGRACVVAGDVANEADVIAMFDAVQSAFGRLDAL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAG-YANVSPIETTEDADFRAQFETNFWGVYHVTRAA---LPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAV 160
Cdd:PRK06947   85 VNNAGiVAPSMPLADMDAARLRRMFDTNVLGAYLCAREAarrLSTDRGGRGGAIVNVSSIASRLGSPNEYVDYAGSKGAV 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEPSGFATDwagssmtVHdvpeAYDATVGAMNRLMRQNTAGAAGDPHRAAEIIV 234
Cdd:PRK06947  165 DTLTLGLAKELGPHGVRVNAVRPGLIETE-------IH----ASGGQPGRAARLGAQTPLGRAGEADEVAETIV 227
PRK06398 PRK06398
aldose dehydrogenase; Validated
7-233 1.54e-21

aldose dehydrogenase; Validated


Pssm-ID: 235794 [Multi-domain]  Cd Length: 258  Bit Score: 91.05  E-value: 1.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARR-PEALAADLaeygdrvlpLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK06398    7 KVAIVTGGSQGIGKAVVNRLKEEGSNVINFDIKePSYNDVDY---------FKVDVSNKEQVIKGIDYVISKYGRIDILV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSR 165
Cdd:PRK06398   78 NNAGIESYGAIHAVEEDEWDRIINVNVNGIFLMSKYTIPYMLKQDKGVIINIASVQSFA-VTRNAAAYVTSKHAVLGLTR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1713980362 166 VLATETAPFgVRVMVVEPSGFAT---DWAgSSMTVHDVPEAYDATVgamNRLMRQNTAGAAGDPHRAAEII 233
Cdd:PRK06398  157 SIAVDYAPT-IRCVAVCPGSIRTpllEWA-AELEVGKDPEHVERKI---REWGEMHPMKRVGKPEEVAYVV 222
DHRS6_like_SDR_c cd05368
human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are ...
5-220 1.85e-21

human DHRS6-like, classical (c) SDRs; Human DHRS6, and similar proteins. These proteins are classical SDRs, with a canonical active site tetrad and a close match to the typical Gly-rich NAD-binding motif. Human DHRS6 is a cytosolic type 2 (R)-hydroxybutyrate dehydrogenase, which catalyses the conversion of (R)-hydroxybutyrate to acetoacetate. Also included in this subgroup is Escherichia coli UcpA (upstream cys P). Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. Note: removed : needed to make this chiodl smaller when drew final trees: rmeoved text form description: Other proteins in this subgroup include Thermoplasma acidophilum aldohexose dehydrogenase, which has high dehydrogenase activity against D-mannose, Bacillus subtilis BacC involved in the biosynthesis of the dipeptide bacilysin and its antibiotic moiety anticapsin, Sphingomonas paucimobilis strain B90 LinC, involved in the degradation of hexachlorocyclohexane isomers...... P).


Pssm-ID: 187626 [Multi-domain]  Cd Length: 241  Bit Score: 90.61  E-value: 1.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAadLAEYGDRVLPLALDVTSPDAARAAVEAavarFGRIDVL 84
Cdd:cd05368     1 DGKVALITAAAQGIGRAIALAFAREGANVIATDINEEKLK--ELERGPGITTRVLDVTDKEQVAALAKE----EGRIDVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFS 164
Cdd:cd05368    75 FNCAGFVHHGSILDCEDDDWDFAMNLNVRSMYLMIKAVLPKMLARKDGSIINMSSVASSIKGVPNRFVYSTTKAAVIGLT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRLMRQNTA 220
Cdd:cd05368   155 KSVAADFAQQGIRCNAICPGTVDTPSLEERIQAQPDPEEALKAFAARQPLGRLATP 210
PRK07890 PRK07890
short chain dehydrogenase; Provisional
11-184 2.02e-21

short chain dehydrogenase; Provisional


Pssm-ID: 181159 [Multi-domain]  Cd Length: 258  Bit Score: 90.79  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRAL-VDAVLAAGDLVVA--TARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK07890   10 VSGVGPGLGRTLaVRAARAGADVVLAarTAERLDEVAAEIDDLGRRALAVPTDITDEDQCANLVALALERFGRVDALVNN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 A-GYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSRV 166
Cdd:PRK07890   90 AfRVPSMKPLADADFAHWRAVIELNVLGTLRLTQAFTPALAESG-GSIVMINSMVLR-HSQPKYGAYKMAKGALLAASQS 167
                         170
                  ....*....|....*...
gi 1713980362 167 LATETAPFGVRVMVVEPS 184
Cdd:PRK07890  168 LATELGPQGIRVNSVAPG 185
fabG PRK06463
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-189 2.07e-21

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


Pssm-ID: 180576 [Multi-domain]  Cd Length: 255  Bit Score: 90.61  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGdrVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:PRK06463   12 ITGGTRGIGRAIAEAFLREGAKVAVLYNSAENEAKELREKG--VFTIKCDVGNRDQVKKSKEVVEKEFGRVDVLVNNAGI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSRVLATE 170
Cdd:PRK06463   90 MYLMPFEEFDEEKYNKMIKINLNGAIYTTYEFLPLLKLSKNGAIVNIASNAGIGTAAEGTTFYAITKAGIIILTRRLAFE 169
                         170
                  ....*....|....*....
gi 1713980362 171 TAPFGVRVMVVEPSGFATD 189
Cdd:PRK06463  170 LGKYGIRVNAVAPGWVETD 188
PRK06113 PRK06113
7-alpha-hydroxysteroid dehydrogenase; Validated
5-196 2.51e-21

7-alpha-hydroxysteroid dehydrogenase; Validated


Pssm-ID: 135765 [Multi-domain]  Cd Length: 255  Bit Score: 90.68  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVAT---ARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK06113   10 DGKCAIITGAGAGIGKEIAITFATAGASVVVSdinADAANHVVDEIQQLGGQAFACRCDITSEQELSALADFALSKLGKV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDaDFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVD 161
Cdd:PRK06113   90 DILVNNAGGGGPKPFDMPMA-DFRRAYELNVFSFFHLSQLVAPEMEKNGGGVILTITSMAAE-NKNINMTSYASSKAAAS 167
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMT 196
Cdd:PRK06113  168 HLVRNMAFDLGEKNIRVNGIAPGAILTDALKSVIT 202
PRK08017 PRK08017
SDR family oxidoreductase;
10-183 3.16e-21

SDR family oxidoreductase;


Pssm-ID: 181198 [Multi-domain]  Cd Length: 256  Bit Score: 90.15  E-value: 3.16e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAAdLAEYGdrVLPLALDVTSPDAARAAVEAAVARF-GRIDVLVNNA 88
Cdd:PRK08017    6 LITGCSSGIGLEAALELKRRGYRVLAACRKPDDVAR-MNSLG--FTGILLDLDDPESVERAADEVIALTdNRLYGLFNNA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVLA 168
Cdd:PRK08017   83 GFGVYGPLSTISRQQMEQQFSTNFFGTHQLTMLLLPAMLPHGEGRIVMTSSVMGLI-STPGRGAYAASKYALEAWSDALR 161
                         170
                  ....*....|....*
gi 1713980362 169 TETAPFGVRVMVVEP 183
Cdd:PRK08017  162 MELRHSGIKVSLIEP 176
PRK07774 PRK07774
SDR family oxidoreductase;
5-183 3.62e-21

SDR family oxidoreductase;


Pssm-ID: 236094 [Multi-domain]  Cd Length: 250  Bit Score: 89.80  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAG-DLVVA--TARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK07774    5 DDKVAIVTGAAGGIGQAYAEALAREGaSVVVAdiNAEGAERVAKQIVADGGTAIAVQVDVSDPDSAKAMADATVSAFGGI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNA---GYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPgiasYQAAKF 158
Cdd:PRK07774   85 DYLVNNAaiyGGMKLDLLITVPWDYYKKFMSVNLDGALVCTRAVYKHMAKRGGGAIVNQSSTAAWLYSNF----YGLAKV 160
                         170       180
                  ....*....|....*....|....*
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK07774  161 GLNGLTQQLARELGGMNIRVNAIAP 185
DHB_DH-like_SDR_c cd08937
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; ...
7-185 8.55e-21

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase (DHB DH)-like, classical (c) SDR; DHB DH (aka 1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase) catalyzes the NAD-dependent conversion of 1,2-dihydroxycyclohexa-3,4-diene carboxylate to a catechol. This subgroup also contains Pseudomonas putida F1 CmtB, 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase, the second enzyme in the pathway for catabolism of p-cumate catabolism. This subgroup shares the glycine-rich NAD-binding motif of the classical SDRs and shares the same catalytic triad; however, the upstream Asn implicated in cofactor binding or catalysis in other SDRs is generally substituted by a Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187642 [Multi-domain]  Cd Length: 256  Bit Score: 89.12  E-value: 8.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRP--EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:cd08937     5 KVVVVTGAAQGIGRGVAERLAGEGARVLLVDRSElvHEVLAEILAAGDAAHVHTADLETYAGAQGVVRAAVERFGRVDVL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVS-PIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSpgiASYQAAKFAVDGF 163
Cdd:cd08937    85 INNVGGTIWAkPYEHYEEEQIEAEIRRSLFPTLWCCRAVLPHMLERQQGVIVNVSSIATRGIYR---IPYSAAKGGVNAL 161
                         170       180
                  ....*....|....*....|..
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSG 185
Cdd:cd08937   162 TASLAFEHARDGIRVNAVAPGG 183
GlcDH_SDR_c cd05358
glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR ...
7-189 1.72e-20

glucose 1 dehydrogenase (GlcDH), classical (c) SDRs; GlcDH, is a tetrameric member of the SDR family, it catalyzes the NAD(P)-dependent oxidation of beta-D-glucose to D-glucono-delta-lactone. GlcDH has a typical NAD-binding site glycine-rich pattern as well as the canonical active site tetrad (YXXXK motif plus upstream Ser and Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187616 [Multi-domain]  Cd Length: 253  Bit Score: 88.21  E-value: 1.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE----YGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:cd05358     4 KVALVTGASSGIGKAIAIRLATAGANVVVNYRSKEDAAEEVVEeikaVGGKAIAVQADVSKEEDVVALFQSAIKEFGTLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA-GTVVQFSSIGGRVgGSPGIASYQAAKFAVD 161
Cdd:cd05358    84 ILVNNAGLQGDASSHEMTLEDWNKVIDVNLTGQFLCAREAIKRFRKSKIkGKIINMSSVHEKI-PWPGHVNYAASKGGVK 162
                         170       180
                  ....*....|....*....|....*...
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05358   163 MMTKTLAQEYAPKGIRVNAIAPGAINTP 190
PRK08643 PRK08643
(S)-acetoin forming diacetyl reductase;
7-178 1.80e-20

(S)-acetoin forming diacetyl reductase;


Pssm-ID: 181518 [Multi-domain]  Cd Length: 256  Bit Score: 88.24  E-value: 1.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAG------DLVVATArrpEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:PRK08643    3 KVALVTGAGQGIGFAIAKRLVEDGfkvaivDYNEETA---QAAADKLSKDGGKAIAVKADVSDRDQVFAAVRQVVDTFGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVgGSPGIASYQAAKFA 159
Cdd:PRK08643   80 LNVVVNNAGVAPTTPIETITEEQFDKVYNINVGGVIWGIQAAQEAFKKLGhGGKIINATSQAGVV-GNPELAVYSSTKFA 158
                         170
                  ....*....|....*....
gi 1713980362 160 VDGFSRVLATETAPFGVRV 178
Cdd:PRK08643  159 VRGLTQTAARDLASEGITV 177
XR_like_SDR_c cd05351
xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins ...
11-189 1.83e-20

xylulose reductase-like, classical (c) SDRs; Members of this subgroup include proteins identified as L-xylulose reductase (XR) and carbonyl reductase; they are members of the SDR family. XR, catalyzes the NADP-dependent reduction of L-xyulose and other sugars. Tetrameric mouse carbonyl reductase is involved in the metabolism of biogenic and xenobiotic carbonyl compounds. This subgroup also includes tetrameric chicken liver D-erythrulose reductase, which catalyzes the reduction of D-erythrulose to D-threitol. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser).


Pssm-ID: 187609 [Multi-domain]  Cd Length: 244  Bit Score: 87.91  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAAdLAEYGDRVLPLALDVTSPDAARAAVEAAvarfGRIDVLVNNAGY 90
Cdd:cd05351    12 VTGAGKGIGRATVKALAKAGARVVAVSRTQADLDS-LVRECPGIEPVCVDLSDWDATEEALGSV----GPVDLLVNNAAV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA-GTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVLAT 169
Cdd:cd05351    87 AILQPFLEVTKEAFDRSFDVNVRAVIHVSQIVARGMIARGVpGSIVNVSSQASQR-ALTNHTVYCSTKAALDMLTKVMAL 165
                         170       180
                  ....*....|....*....|
gi 1713980362 170 ETAPFGVRVMVVEPSGFATD 189
Cdd:cd05351   166 ELGPHKIRVNSVNPTVVMTD 185
PRK07024 PRK07024
SDR family oxidoreductase;
5-240 2.94e-20

SDR family oxidoreductase;


Pssm-ID: 235910 [Multi-domain]  Cd Length: 257  Bit Score: 87.68  E-value: 2.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGD--RVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK07024    1 MPLKVFITGASSGIGQALAREYARQGATLGLVARRTDALQAFAARLPKaaRVSVYAADVRDADALAAAAADFIAAHGLPD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDAD-FRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVD 161
Cdd:PRK07024   81 VVIANAGISVGTLTEEREDLAvFREVMDTNYFGMVATFQPFIAPMRAARRGTLVGIASVAG-VRGLPGAGAYSASKAAAI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATdwagsSMTVHDvpeAYdatvgAMNRLMrqntagaagDPHRAAEIIVRTVRRG 240
Cdd:PRK07024  160 KYLESLRVELRPAGVRVVTIAPGYIRT-----PMTAHN---PY-----PMPFLM---------DADRFAARAARAIARG 216
PRK06935 PRK06935
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-188 3.51e-20

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 180761 [Multi-domain]  Cd Length: 258  Bit Score: 87.48  E-value: 3.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAE-YGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK06935   14 DGKVAIVTGGNTGLGQGYAVALAKAGaDIIITTHGTNWDETRRLIEkEGRKVTFVQVDLTKPESAEKVVKEALEEFGKID 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSI----GGRVggspgIASYQAAKF 158
Cdd:PRK06935   94 ILVNNAGTIRRAPLLEYKDEDWNAVMDINLNSVYHLSQAVAKVMAKQGSGKIINIASMlsfqGGKF-----VPAYTASKH 168
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK06935  169 GVAGLTKAFANELAAYNIQVNAIAPGYIKT 198
DHRS1_HSDL2-like_SDR_c cd05338
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) and human hydroxysteroid ...
7-184 3.80e-20

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


Pssm-ID: 187597 [Multi-domain]  Cd Length: 246  Bit Score: 87.06  E-value: 3.80e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLA---------------EYGDRVLPLALDVTSPDAARAAV 71
Cdd:cd05338     4 KVAFVTGASRGIGRAIALRLAKAGATVVVAAKTASEGDNGSAkslpgtieetaeeieAAGGQALPIVVDVRDEDQVRALV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  72 EAAVARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIA 151
Cdd:cd05338    84 EATVDQFGRLDILVNNAGAIWLSLVEDTPAKRFDLMQRVNLRGTYLLSQAALPHMVKAGQGHILNISPPLS-LRPARGDV 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1713980362 152 SYQAAKFAVDGFSRVLATETAPFGVRVMVVEPS 184
Cdd:cd05338   163 AYAAGKAGMSRLTLGLAAELRRHGIAVNSLWPS 195
fabG PRK06550
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
10-195 4.09e-20

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


Pssm-ID: 180617 [Multi-domain]  Cd Length: 235  Bit Score: 86.56  E-value: 4.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYgdrvlpLALDVTSPdaaraaVEAAVARFGRIDVLVNNAG 89
Cdd:PRK06550    9 LITGAASGIGLAQARAFLAQGAQVYGVDKQDKPDLSGNFHF------LQLDLSDD------LEPLFDWVPSVDILCNTAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 ----YAnvsPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIAsYQAAKFAVDGFSR 165
Cdd:PRK06550   77 ilddYK---PLLDTSLEEWQHIFDTNLTSTFLLTRAYLPQMLERKSGIIINMCSIASFVAGGGGAA-YTASKHALAGFTK 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1713980362 166 VLATETAPFGVRVMVVEPSGF-----ATDWAGSSM 195
Cdd:PRK06550  153 QLALDYAKDGIQVFGIAPGAVktpmtAADFEPGGL 187
PKR_SDR_c cd08945
Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR ...
4-183 4.15e-20

Polyketide ketoreductase, classical (c) SDR; Polyketide ketoreductase (KR) is a classical SDR with a characteristic NAD-binding pattern and active site tetrad. Aromatic polyketides include various aromatic compounds of pharmaceutical interest. Polyketide KR, part of the type II polyketide synthase (PKS) complex, is comprised of stand-alone domains that resemble the domains found in fatty acid synthase and multidomain type I PKS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187649 [Multi-domain]  Cd Length: 258  Bit Score: 87.21  E-value: 4.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   4 QDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAA---DLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:cd08945     1 QDSEVALVTGATSGIGLAIARRLGKEGLRVFVCARGEEGLATtvkELREAGVEADGRTCDVRSVPEIEALVAAAVARYGP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPV--LRRQGAGTVVQFSSIGGRVGGSPGiASYQAAKF 158
Cdd:cd08945    81 IDVLVNNAGRSGGGATAELADELWLDVVETNLTGVFRVTKEVLKAggMLERGTGRIINIASTGGKQGVVHA-APYSASKH 159
                         170       180
                  ....*....|....*....|....*
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:cd08945   160 GVVGFTKALGLELARTGITVNAVCP 184
SDR_c1 cd05355
classical (c) SDR, subgroup 1; These proteins are members of the classical SDR family, with a ...
11-202 4.44e-20

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


Pssm-ID: 187613 [Multi-domain]  Cd Length: 270  Bit Score: 87.35  E-value: 4.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAEY----GDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd05355    31 ITGGDSGIGRAVAIAFAREGaDVAINYLPEEEDDAEETKKLieeeGRKCLLIPGDLGDESFCRDLVKEVVKEFGKLDILV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSP-IETTEDADFRAQFETNFWGVYHVTRAALPVLRRqgAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFS 164
Cdd:cd05355   111 NNAAYQHPQEsIEDITTEQLEKTFRTNIFSMFYLTKAALPHLKK--GSSIINTTSVTAYK-GSPHLLDYAATKGAIVAFT 187
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPE 202
Cdd:cd05355   188 RGLSLQLAEKGIRVNAVAPGPIWTPLIPSSFPEEKVSE 225
PRK07201 PRK07201
SDR family oxidoreductase;
11-176 4.50e-20

SDR family oxidoreductase;


Pssm-ID: 235962 [Multi-domain]  Cd Length: 657  Bit Score: 90.01  E-value: 4.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALA---ADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK07201  376 ITGASSGIGRATAIKVAEAGATVFLVARNGEALDelvAEIRAKGGTAHAYTCDLTDSAAVDHTVKDILAEHGHVDYLVNN 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDA--DFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGFSR 165
Cdd:PRK07201  456 AGRSIRRSVENSTDRfhDYERTMAVNYFGAVRLILGLLPHMRERRFGHVVNVSSIGVQTNA-PRFSAYVASKAALDAFSD 534
                         170
                  ....*....|.
gi 1713980362 166 VLATETAPFGV 176
Cdd:PRK07201  535 VAASETLSDGI 545
cyclohexanol_reductase_SDR_c cd05330
cyclohexanol reductases, including levodione reductase, classical (c) SDRs; Cyloclohexanol ...
7-258 5.43e-20

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


Pssm-ID: 187591 [Multi-domain]  Cd Length: 257  Bit Score: 86.81  E-value: 5.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGD-----RVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:cd05330     4 KVVLITGGGSGLGLATAVRLAKEGAKLSLVDLNEEGLEAAKAALLEiapdaEVLLIKADVSDEAQVEAYVDATVEQFGRI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGY-ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAV 160
Cdd:cd05330    84 DGFFNNAGIeGKQNLTEDFGADEFDKVVSINLRGVFYGLEKVLKVMREQGSGMIVNTASVGG-IRGVGNQSGYAAAKHGV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDvPEAYDAtvgAMNRLMRQNTAGAAGDPHRAAEIIvrtvrrG 240
Cdd:cd05330   163 VGLTRNSAVEYGQYGIRINAIAPGAILTPMVEGSLKQLG-PENPEE---AGEEFVSVNPMKRFGEPEEVAAVV------A 232
                         250
                  ....*....|....*...
gi 1713980362 241 ELPSHLLLGVNAATMALD 258
Cdd:cd05330   233 FLLSDDAGYVNAAVVPID 250
SDR_c12 cd08944
classical (c) SDR, subgroup 12; These are classical SDRs, with the canonical active site ...
7-234 1.33e-19

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


Pssm-ID: 187648 [Multi-domain]  Cd Length: 246  Bit Score: 85.62  E-value: 1.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd08944     4 KVAIVTGAGAGIGAACAARLAREGARVVVADIDGGAAQAVVAQIAGGALALRVDVTDEQQVAALFERAVEEFGGLDLLVN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSP-IETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSR 165
Cdd:cd08944    84 NAGAMHLTPaIIDTDLAVWDQTMAINLRGTFLCCRHAAPRMIARGGGSIVNLSSIAGQ-SGDPGYGAYGASKAAIRNLTR 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 166 VLATETAPFGVRVMVVEPSGFATDwagssMTVHDVPEAYDATVGAMNRLMRQNTAGAAGDPHRAAEIIV 234
Cdd:cd08944   163 TLAAELRHAGIRCNALAPGLIDTP-----LLLAKLAGFEGALGPGGFHLLIHQLQGRLGRPEDVAAAVV 226
PRK09291 PRK09291
SDR family oxidoreductase;
11-188 2.39e-19

SDR family oxidoreductase;


Pssm-ID: 181762 [Multi-domain]  Cd Length: 257  Bit Score: 85.05  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATAR-RPE--ALAADLAEYGDRVLPLALDVTSP-DAARAAVEAavarfgrIDVLVN 86
Cdd:PRK09291    7 ITGAGSGFGREVALRLARKGHNVIAGVQiAPQvtALRAEAARRGLALRVEKLDLTDAiDRAQAAEWD-------VDVLLN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKFAVDGFSRV 166
Cdd:PRK09291   80 NAGIGEAGAVVDIPVELVRELFETNVFGPLELTQGFVRKMVARGKGKVVFTSSMAGLITG-PFTGAYCASKHALEAIAEA 158
                         170       180
                  ....*....|....*....|..
gi 1713980362 167 LATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK09291  159 MHAELKPFGIQVATVNPGPYLT 180
PRK06139 PRK06139
SDR family oxidoreductase;
11-259 3.08e-19

SDR family oxidoreductase;


Pssm-ID: 235713 [Multi-domain]  Cd Length: 330  Bit Score: 85.93  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDR---VLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK06139   12 ITGASSGIGQATAEAFARRGARLVLAARDEEALQAVAEECRALgaeVLVVPTDVTDADQVKALATQAASFGGRIDVWVNN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK06139   92 VGVGAVGRFEETPIEAHEQVIQTNLIGYMRDAHAALPIFKKQGHGIFINMISLGGFA-AQPYAAAYSASKFGLRGFSEAL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 168 ATETAPF-GVRVMVVEPsgfatdwagssmTVHDVPEAYDatvGAmNRLMRQNTA-GAAGDPHRAAEIIVRTVRRGElpSH 245
Cdd:PRK06139  171 RGELADHpDIHVCDVYP------------AFMDTPGFRH---GA-NYTGRRLTPpPPVYDPRRVAKAVVRLADRPR--AT 232
                         250
                  ....*....|....
gi 1713980362 246 LLLGVNAATMALDH 259
Cdd:PRK06139  233 TTVGAAARLARLAH 246
PRK06125 PRK06125
short chain dehydrogenase; Provisional
11-189 3.21e-19

short chain dehydrogenase; Provisional


Pssm-ID: 235703 [Multi-domain]  Cd Length: 259  Bit Score: 84.71  E-value: 3.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATAR---RPEALAADL-AEYGDRVLPLALDVTSPDAARAAVEAAvarfGRIDVLVN 86
Cdd:PRK06125   12 ITGASKGIGAAAAEAFAAEGCHLHLVARdadALEALAADLrAAHGVDVAVHALDLSSPEAREQLAAEA----GDIDILVN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGR------VGGSPGIAsyqaakfAV 160
Cdd:PRK06125   88 NAGAIPGGGLDDVDDAAWRAGWELKVFGYIDLTRLAYPRMKARGSGVIVNVIGAAGEnpdadyICGSAGNA-------AL 160
                         170       180
                  ....*....|....*....|....*....
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK06125  161 MAFTRALGGKSLDDGVRVVGVNPGPVATD 189
ADH_SDR_c_like cd05323
insect type alcohol dehydrogenase (ADH)-like, classical (c) SDRs; This subgroup contains ...
11-184 3.49e-19

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


Pssm-ID: 187584 [Multi-domain]  Cd Length: 244  Bit Score: 84.27  E-value: 3.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADL---AEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd05323     5 ITGGASGIGLATAKLLLKKGAKVAILDRNENPGAAAElqaINPKVKATFVQCDVTSWEQLAAAFKKAIEKFGRVDILINN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSP--IETTEDADFRAQFETNFWGVYHVTRAALPVLRR---QGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDG 162
Cdd:cd05323    85 AGILDEKSylFAGKLPPPWEKTIDVNLTGVINTTYLALHYMDKnkgGKGGVIVNIGSVAG-LYPAPQFPVYSASKHGVVG 163
                         170       180
                  ....*....|....*....|...
gi 1713980362 163 FSRVLA-TETAPFGVRVMVVEPS 184
Cdd:cd05323   164 FTRSLAdLLEYKTGVRVNAICPG 186
benD PRK12823
1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional
7-185 4.54e-19

1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase; Provisional


Pssm-ID: 183772 [Multi-domain]  Cd Length: 260  Bit Score: 84.23  E-value: 4.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRP--EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK12823    9 KVVVVTGAAQGIGRGVALRAAAEGARVVLVDRSElvHEVAAELRAAGGEALALTADLETYAGAQAAMAAAVEAFGRIDVL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYA-NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvggspGI--ASYQAAKFAVD 161
Cdd:PRK12823   89 INNVGGTiWAKPFEEYEEEQIEAEIRRSLFPTLWCCRAVLPHMLAQGGGAIVNVSSIATR-----GInrVPYSAAKGGVN 163
                         170       180
                  ....*....|....*....|....
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSG 185
Cdd:PRK12823  164 ALTASLAFEYAEHGIRVNAVAPGG 187
PRK08628 PRK08628
SDR family oxidoreductase;
8-188 6.01e-19

SDR family oxidoreductase;


Pssm-ID: 181508 [Multi-domain]  Cd Length: 258  Bit Score: 83.85  E-value: 6.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDLVVATAR--RPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK08628    9 VVIVTGGASGIGAAISLRLAEEGAIPVIFGRsaPDDEFAEELRALQPRAEFVQVDLTDDAQCRDAVEQTVAKFGRIDGLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDAdFRAQFETNFWGVYHVTRAALPVLrRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSR 165
Cdd:PRK08628   89 NNAGVNDGVGLEAGREA-FVASLERNLIHYYVMAHYCLPHL-KASRGAIVNISSKTA-LTGQGGTSGYAAAKGAQLALTR 165
                         170       180
                  ....*....|....*....|...
gi 1713980362 166 VLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK08628  166 EWAVALAKDGVRVNAVIPAEVMT 188
PRK10538 PRK10538
bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase ...
10-183 1.39e-18

bifunctional NADP-dependent 3-hydroxy acid dehydrogenase/3-hydroxypropionate dehydrogenase YdfG;


Pssm-ID: 182531 [Multi-domain]  Cd Length: 248  Bit Score: 82.88  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAG 89
Cdd:PRK10538    4 LVTGATAGFGECITRRFIQQGHKVIATGRRQERLQELKDELGDNLYIAQLDVRNRAAIEEMLASLPAEWRNIDVLVNNAG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YA-NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGR---VGGSpgiaSYQAAKFAVDGFSR 165
Cdd:PRK10538   84 LAlGLEPAHKASVEDWETMIDTNNKGLVYMTRAVLPGMVERNHGHIINIGSTAGSwpyAGGN----VYGATKAFVRQFSL 159
                         170
                  ....*....|....*...
gi 1713980362 166 VLATETAPFGVRVMVVEP 183
Cdd:PRK10538  160 NLRTDLHGTAVRVTDIEP 177
SDR_c8 cd08930
classical (c) SDR, subgroup 8; This subgroup has a fairly well conserved active site tetrad ...
10-186 1.51e-18

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


Pssm-ID: 187635 [Multi-domain]  Cd Length: 250  Bit Score: 82.77  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVAT---ARRPEALAADLA-EYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd08930     6 LITGAAGLIGKAFCKALLSAGARLILAdinAPALEQLKEELTnLYKNRVIALELDITSKESIKELIESYLEKFGRIDILI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYAN---VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGG------RVGGSPGIAS---Y 153
Cdd:cd08930    86 NNAYPSPkvwGSRFEEFPYEQWNEVLNVNLGGAFLCSQAFIKLFKKQGKGSIINIASIYGviapdfRIYENTQMYSpveY 165
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1713980362 154 QAAKFAVDGFSRVLATETAPFGVRVMVVEPSGF 186
Cdd:cd08930   166 SVIKAGIIHLTKYLAKYYADTGIRVNAISPGGI 198
PRK12936 PRK12936
3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed
10-222 1.65e-18

3-ketoacyl-(acyl-carrier-protein) reductase NodG; Reviewed


Pssm-ID: 171820 [Multi-domain]  Cd Length: 245  Bit Score: 82.66  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAG 89
Cdd:PRK12936   10 LVTGASGGIGEEIARLLHAQGAIVGLHGTRVEKLEALAAELGERVKIFPANLSDRDEVKALGQKAEADLEGVDILVNNAG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVLAT 169
Cdd:PRK12936   90 ITKDGLFVRMSDEDWDSVLEVNLTATFRLTRELTHPMMRRRYGRIINITSVVG-VTGNPGQANYCASKAGMIGFSKSLAQ 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1713980362 170 ETAPFGVRVMVVEPsGFATdwagSSMTVHDVPEAYDATVGAMNrlMRQNTAGA 222
Cdd:PRK12936  169 EIATRNVTVNCVAP-GFIE----SAMTGKLNDKQKEAIMGAIP--MKRMGTGA 214
PRK07035 PRK07035
SDR family oxidoreductase;
7-192 2.25e-18

SDR family oxidoreductase;


Pssm-ID: 180802 [Multi-domain]  Cd Length: 252  Bit Score: 82.37  E-value: 2.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK07035    9 KIALVTGASRGIGEAIAKLLAQQGAHVIVSSRKLDgcqAVADAIVAAGGKAEALACHIGEMEQIDALFAHIRERHGRLDI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGyAN--VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGG-RVGGSPGIasYQAAKFAV 160
Cdd:PRK07035   89 LVNNAA-ANpyFGHILDTDLGAFQKTVDVNIRGYFFMSVEAGKLMKEQGGGSIVNVASVNGvSPGDFQGI--YSITKAAV 165
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEPSGFATDWAG 192
Cdd:PRK07035  166 ISMTKAFAKECAPFGIRVNALLPGLTDTKFAS 197
PRK07067 PRK07067
L-iditol 2-dehydrogenase;
11-183 2.28e-18

L-iditol 2-dehydrogenase;


Pssm-ID: 235925 [Multi-domain]  Cd Length: 257  Bit Score: 82.38  E-value: 2.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:PRK07067   11 LTGAASGIGEAVAERYLAEGARVVIADIKPARARLAALEIGPAAIAVSLDVTRQDSIDRIVAAAVERFGGIDILFNNAAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVGGSPgIASYQAAKFAVDGFSRVLAT 169
Cdd:PRK07067   91 FDMAPILDISRDSYDRLFAVNVKGLFFLMQAVARHMVEQGrGGKIINMASQAGRRGEAL-VSHYCATKAAVISYTQSAAL 169
                         170
                  ....*....|....
gi 1713980362 170 ETAPFGVRVMVVEP 183
Cdd:PRK07067  170 ALIRHGINVNAIAP 183
PRK08063 PRK08063
enoyl-[acyl-carrier-protein] reductase FabL;
7-189 2.48e-18

enoyl-[acyl-carrier-protein] reductase FabL;


Pssm-ID: 236145 [Multi-domain]  Cd Length: 250  Bit Score: 82.07  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPEA---LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK08063    5 KVALVTGSSRGIGKAIALRLAEEGyDIAVNYARSRKAaeeTAEEIEALGRKALAVKANVGDVEKIKEMFAQIDEEFGRLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIG-GRVggSPGIASYQAAKFAVD 161
Cdd:PRK08063   85 VFVNNAASGVLRPAMELEESHWDWTMNINAKALLFCAQEAAKLMEKVGGGKIISLSSLGsIRY--LENYTTVGVSKAALE 162
                         170       180
                  ....*....|....*....|....*...
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK08063  163 ALTRYLAVELAPKGIAVNAVSGGAVDTD 190
PRK12384 PRK12384
sorbitol-6-phosphate dehydrogenase; Provisional
7-178 2.83e-18

sorbitol-6-phosphate dehydrogenase; Provisional


Pssm-ID: 183489 [Multi-domain]  Cd Length: 259  Bit Score: 82.01  E-value: 2.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAG-DLVVA--TARRPEALAADLA-EYG-DRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK12384    3 QVAVVIGGGQTLGAFLCHGLAEEGyRVAVAdiNSEKAANVAQEINaEYGeGMAYGFGADATSEQSVLALSRGVDEIFGRV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVgGSPGIASYQAAKFAV 160
Cdd:PRK12384   83 DLLVYNAGIAKAAFITDFQLGDFDRSLQVNLVGYFLCAREFSRLMIRDGiQGRIIQINSKSGKV-GSKHNSGYSAAKFGG 161
                         170
                  ....*....|....*...
gi 1713980362 161 DGFSRVLATETAPFGVRV 178
Cdd:PRK12384  162 VGLTQSLALDLAEYGITV 179
PRK08265 PRK08265
short chain dehydrogenase; Provisional
1-183 3.94e-18

short chain dehydrogenase; Provisional


Pssm-ID: 236209 [Multi-domain]  Cd Length: 261  Bit Score: 81.98  E-value: 3.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:PRK08265    1 MIGLAGKVAIVTGGATLIGAAVARALVAAGARVAIVDIDADNGAAVAASLGERARFIATDITDDAAIERAVATVVARFGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGYANVSPIETTEdADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGRVGGSpGIASYQAAKFAV 160
Cdd:PRK08265   81 VDILVNLACTYLDDGLASSR-ADWLAALDVNLVSAAMLAQAAHPHLARGG-GAIVNFTSISAKFAQT-GRWLYPASKAAI 157
                         170       180
                  ....*....|....*....|...
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK08265  158 RQLTRSMAMDLAPDGIRVNSVSP 180
SDR_c2 cd05370
classical (c) SDR, subgroup 2; Short-chain dehydrogenases/reductases (SDRs, aka ...
11-189 4.30e-18

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


Pssm-ID: 187628 [Multi-domain]  Cd Length: 228  Bit Score: 81.20  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDrVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAG- 89
Cdd:cd05370    10 ITGGTSGIGLALARKFLEAGNTVIITGRREERLAEAKKELPN-IHTIVLDVGDAESVEALAEALLSEYPNLDILINNAGi 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 ---YANVSPIETTEDADfrAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRV 166
Cdd:cd05370    89 qrpIDLRDPASDLDKAD--TEIDTNLIGPIRLIKAFLPHLKKQPEATIVNVSSGLAFV-PMAANPVYCATKAALHSYTLA 165
                         170       180
                  ....*....|....*....|...
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05370   166 LRHQLKDTGVEVVEIVPPAVDTE 188
fabG PRK06077
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
1-195 4.45e-18

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


Pssm-ID: 235693 [Multi-domain]  Cd Length: 252  Bit Score: 81.69  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPqVWFITGSSRGFGRALVDAVLAAGDLVVATA-RRPEALAADLAEY----GDRVLPLAlDVTSPDAARAAVEAAV 75
Cdd:PRK06077    2 YSLKDK-VVVVTGSGRGIGRAIAVRLAKEGSLVVVNAkKRAEEMNETLKMVkengGEGIGVLA-DVSTREGCETLAKATI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  76 ARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRqgAGTVVQFSSIGGrVGGSPGIASYQA 155
Cdd:PRK06077   80 DRYGVADILVNNAGLGLFSPFLNVDDKLIDKHISTDFKSVIYCSQELAKEMRE--GGAIVNIASVAG-IRPAYGLSIYGA 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1713980362 156 AKFAVDGFSRVLATETAPfGVRVMVVEPsGFATDWAGSSM 195
Cdd:PRK06077  157 MKAAVINLTKYLALELAP-KIRVNAIAP-GFVKTKLGESL 194
PRK07832 PRK07832
SDR family oxidoreductase;
10-240 5.17e-18

SDR family oxidoreductase;


Pssm-ID: 181139 [Multi-domain]  Cd Length: 272  Bit Score: 81.63  E-value: 5.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDR----VLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK07832    4 FVTGAASGIGRATALRLAAQGAELFLTDRDADGLAQTVADARALggtvPEHRALDISDYDAVAAFAADIHAAHGSMDVVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFS 164
Cdd:PRK07832   84 NIAGISAWGTVDRLTHEQWRRMVDVNLMGPIHVIETFVPPMVAAGrGGHLVNVSSAAGLV-ALPWHAAYSASKFGLRGLS 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDWAGssmTVHDVpeAYDATVGAMNRLMRQnTAGAAGDPHRAAEIIVRTVRRG 240
Cdd:PRK07832  163 EVLRFDLARHGIGVSVVVPGAVKTPLVN---TVEIA--GVDREDPRVQKWVDR-FRGHAVTPEKAAEKILAGVEKN 232
SDR_c10 cd05373
classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an ...
11-192 6.73e-18

classical (c) SDR, subgroup 10; This subgroup resembles the classical SDRs, but has an incomplete match to the canonical glycine rich NAD-binding motif and lacks the typical active site tetrad (instead of the critical active site Tyr, it has Phe, but contains the nearby Lys). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187631 [Multi-domain]  Cd Length: 238  Bit Score: 80.89  E-value: 6.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAE-YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05373     4 VVGAGDGLGAAIARRFAAEGFSVALAARREaklEALLVDIIRdAGGSAKAVPTDARDEDEVIALFDLIEEEIGPLEVLVY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVqFSSIGGRVGGSPGIASYQAAKFAVDGFSRV 166
Cdd:cd05373    84 NAGANVWFPILETTPRVFEKVWEMAAFGGFLAAREAAKRMLARGRGTII-FTGATASLRGRAGFAAFAGAKFALRALAQS 162
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 167 LATETAPFGVRVM-VVEPSGFATDWAG 192
Cdd:cd05373   163 MARELGPKGIHVAhVIIDGGIDTDFIR 189
PRK06114 PRK06114
SDR family oxidoreductase;
5-188 1.28e-17

SDR family oxidoreductase;


Pssm-ID: 180408 [Multi-domain]  Cd Length: 254  Bit Score: 80.21  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEY----GDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:PRK06114    7 DGQVAFVTGAGSGIGQRIAIGLAQAGADVALFDLRTDDGLAETAEHieaaGRRAIQIAADVTSKADLRAAVARTEAELGA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSpGI--ASYQAAKF 158
Cdd:PRK06114   87 LTLAVNAAGIANANPAEEMEEEQWQTVMDINLTGVFLSCQAEARAMLENGGGSIVNIASMSGIIVNR-GLlqAHYNASKA 165
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK06114  166 GVIHLSKSLAMEWVGRGIRVNSISPGYTAT 195
PRK06198 PRK06198
short chain dehydrogenase; Provisional
1-165 2.45e-17

short chain dehydrogenase; Provisional


Pssm-ID: 180462 [Multi-domain]  Cd Length: 260  Bit Score: 79.66  E-value: 2.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVA 76
Cdd:PRK06198    1 MGRLDGKVALVTGGTQGLGAAIARAFAERGaAGLVICGRNAEkgeAQAAELEALGAKAVFVQADLSDVEDCRRVVAAADE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  77 RFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA-GTVVQFSSIGGRvGGSPGIASYQA 155
Cdd:PRK06198   81 AFGRLDALVNAAGLTDRGTILDTSPELFDRHFAVNVRAPFFLMQEAIKLMRRRKAeGTIVNIGSMSAH-GGQPFLAAYCA 159
                         170
                  ....*....|
gi 1713980362 156 AKFAVDGFSR 165
Cdd:PRK06198  160 SKGALATLTR 169
retinol-DH_like_SDR_c_like cd05327
retinol dehydrogenase (retinol-DH), Light dependent Protochlorophyllide (Pchlide) ...
7-189 4.93e-17

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


Pssm-ID: 212492 [Multi-domain]  Cd Length: 269  Bit Score: 78.81  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEY--GDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:cd05327     2 KVVVITGANSGIGKETARELAKRGAHVIIACRNEekgEEAAAEIKKEtgNAKVEVIQLDLSSLASVRQFAEEFLARFPRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANvSPIETTEDaDFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSP------------- 148
Cdd:cd05327    82 DILINNAGIMA-PPRRLTKD-GFELQFAVNYLGHFLLTNLLLPVLKASAPSRIVNVSSIAHRAGPIDfndldlennkeys 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1713980362 149 GIASYQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05327   160 PYKAYGQSKLANILFTRELARRLEGTGVTVNALHPGVVRTE 200
hydroxyacyl-CoA-like_DH_SDR_c-like cd05353
(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids ...
12-196 6.99e-17

(3R)-hydroxyacyl-CoA dehydrogenase-like, classical(c)-like SDRs; Beta oxidation of fatty acids in eukaryotes occurs by a four-reaction cycle, that may take place in mitochondria or in peroxisomes. (3R)-hydroxyacyl-CoA dehydrogenase is part of rat peroxisomal multifunctional MFE-2, it is a member of the NAD-dependent SDRs, but contains an additional small C-terminal domain that completes the active site pocket and participates in dimerization. The atypical, additional C-terminal extension allows for more extensive dimerization contact than other SDRs. MFE-2 catalyzes the second and third reactions of the peroxisomal beta oxidation cycle. Proteins in this subgroup have a typical catalytic triad, but have a His in place of the usual upstream Asn. This subgroup also contains members identified as 17-beta-hydroxysteroid dehydrogenases, including human peroxisomal 17-beta-hydroxysteroid dehydrogenase type 4 (17beta-HSD type 4, aka MFE-2, encoded by HSD17B4 gene) which is involved in fatty acid beta-oxidation and steroid metabolism. This subgroup also includes two SDR domains of the Neurospora crassa and Saccharomyces cerevisiae multifunctional beta-oxidation protein (MFP, aka Fox2). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187611 [Multi-domain]  Cd Length: 250  Bit Score: 78.13  E-value: 6.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  12 TGSSRGFGRALVDAVLAAGDLVVAtarrpealAADLAEYGDRVLPLALDvtspdaaraaveaavaRFGRIDVLVNNAGYA 91
Cdd:cd05353    44 SGKSSSAADKVVDEIKAAGGKAVA--------NYDSVEDGEKIVKTAID----------------AFGRVDILVNNAGIL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  92 NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRVLATET 171
Cdd:cd05353   100 RDRSFAKMSEEDWDLVMRVHLKGSFKVTRAAWPYMRKQKFGRIINTSSAAG-LYGNFGQANYSAAKLGLLGLSNTLAIEG 178
                         170       180
                  ....*....|....*....|....*
gi 1713980362 172 APFGVRVMVVEPSgfatdwAGSSMT 196
Cdd:cd05353   179 AKYNITCNTIAPA------AGSRMT 197
Ycik_SDR_c cd05340
Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related ...
7-188 1.56e-16

Escherichia coli K-12 YCIK-like, classical (c) SDRs; Escherichia coli K-12 YCIK and related proteins have a canonical classical SDR nucleotide-binding motif and active site tetrad. They are predicted oxoacyl-(acyl carrier protein/ACP) reductases. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187599 [Multi-domain]  Cd Length: 236  Bit Score: 76.85  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALA------ADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGR 80
Cdd:cd05340     5 RIILVTGASDGIGREAALTYARYGATVILLGRNEEKLRqvadhiNEEGGRQPQWFILDLLTCTSENCQQLAQRIAVNYPR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 IDVLVNNAGY-ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSpGIASYQAAKFA 159
Cdd:cd05340    85 LDGVLHNAGLlGDVCPLSEQNPQVWQDV*QVNVNATFMLTQALLPLLLKSDAGSLVFTSSSVGRQGRA-NWGAYAVSKFA 163
                         170       180
                  ....*....|....*....|....*....
gi 1713980362 160 VDGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:cd05340   164 TEGL*QVLADEYQQRNLRVNCINPGGTRT 192
PRK05866 PRK05866
SDR family oxidoreductase;
11-178 1.68e-16

SDR family oxidoreductase;


Pssm-ID: 235631 [Multi-domain]  Cd Length: 293  Bit Score: 77.86  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAA---DLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK05866   45 LTGASSGIGEAAAEQFARRGATVVAVARREDLLDAvadRITRAGGDAMAVPCDLSDLDAVDALVADVEKRIGGVDILINN 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDA--DFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSR 165
Cdd:PRK05866  125 AGRSIRRPLAESLDRwhDVERTMVLNYYAPLRLIRGLAPGMLERGDGHIINVATWGVLSEASPLFSVYNASKAALSAVSR 204
                         170
                  ....*....|...
gi 1713980362 166 VLATETAPFGVRV 178
Cdd:PRK05866  205 VIETEWGDRGVHS 217
HSD10-like_SDR_c cd05371
17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as ...
7-188 4.21e-16

17hydroxysteroid dehydrogenase type 10 (HSD10)-like, classical (c) SDRs; HSD10, also known as amyloid-peptide-binding alcohol dehydrogenase (ABAD), was previously identified as a L-3-hydroxyacyl-CoA dehydrogenase, HADH2. In fatty acid metabolism, HADH2 catalyzes the third step of beta-oxidation, the conversion of a hydroxyl to a keto group in the NAD-dependent oxidation of L-3-hydroxyacyl CoA. In addition to alcohol dehydrogenase and HADH2 activites, HSD10 has steroid dehydrogenase activity. Although the mechanism is unclear, HSD10 is implicated in the formation of amyloid beta-petide in the brain (which is linked to the development of Alzheimer's disease). Although HSD10 is normally concentrated in the mitochondria, in the presence of amyloid beta-peptide it translocates into the plasma membrane, where it's action may generate cytotoxic aldehydes and may lower estrogen levels through its use of 17-beta-estradiol as a substrate. HSD10 is a member of the SRD family, but differs from other SDRs by the presence of two insertions of unknown function. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187629 [Multi-domain]  Cd Length: 252  Bit Score: 76.17  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAlAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05371     3 LVAVVTGGASGLGLATVERLLAQGAKVVILDLPNSP-GETVAKLGDNCRFVPVDVTSEKDVKAALALAKAKFGRLDIVVN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPI------ETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA------GTVVQFSSIGGRvGGSPGIASYQ 154
Cdd:cd05371    82 CAGIAVAAKTynkkgqQPHSLELFQRVINVNLIGTFNVIRLAAGAMGKNEPdqggerGVIINTASVAAF-EGQIGQAAYS 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1713980362 155 AAKFAVDGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:cd05371   161 ASKGGIVGMTLPIARDLAPQGIRVVTIAPGLFDT 194
17beta-HSDXI-like_SDR_c cd05339
human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid ...
10-183 5.33e-16

human 17-beta-hydroxysteroid dehydrogenase XI-like, classical (c) SDRs; 17-beta-hydroxysteroid dehydrogenases (17betaHSD) are a group of isozymes that catalyze activation and inactivation of estrogen and androgens. 17betaHSD type XI, a classical SDR, preferentially converts 3alpha-Adiol to androsterone but not numerous other tested steroids. This subgroup of classical SDRs also includes members identified as retinol dehydrogenases, which convert retinol to retinal, a property that overlaps with 17betaHSD activity. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187598 [Multi-domain]  Cd Length: 243  Bit Score: 75.74  E-value: 5.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05339     3 LITGGGSGIGRLLALEFAKRGAKVVILDINEkgaEETANNVRKAGGKVHYYKCDVSKREEVYEAAKKIKKEVGDVTILIN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRV 166
Cdd:cd05339    83 NAGVVSGKKLLELPDEEIEKTFEVNTLAHFWTTKAFLPDMLERNHGHIVTIASVAGLI-SPAGLADYCASKAAAVGFHES 161
                         170       180
                  ....*....|....*....|
gi 1713980362 167 LATETAPF---GVRVMVVEP 183
Cdd:cd05339   162 LRLELKAYgkpGIKTTLVCP 181
RhaD COG3347
Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase ...
7-181 6.19e-16

Rhamnose utilisation protein RhaD, predicted bifunctional aldolase and dehydrogenase [Carbohydrate transport and metabolism];


Pssm-ID: 442576 [Multi-domain]  Cd Length: 674  Bit Score: 77.65  E-value: 6.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPD-----AARAAVEAAVARFGRI 81
Cdd:COG3347   426 RVALVTGGAGGIGRATAARLAAEGAAVVVADLDGEAAEAAAAELGGGYGADAVDATDVDvtaeaAVAAAFGFAGLDIGGS 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVD 161
Cdd:COG3347   506 DIGVANAGIASSSPEEETRLSFWLNNFAHLSTGQFLVARAAFQGTGGQGLGGSSVFAVSKNAAAAAYGAAAAATAKAAAQ 585
                         170       180
                  ....*....|....*....|
gi 1713980362 162 GFSRVLATETAPFGVRVMVV 181
Cdd:COG3347   586 HLLRALAAEGGANGINANRV 605
PLN02253 PLN02253
xanthoxin dehydrogenase
7-191 6.69e-16

xanthoxin dehydrogenase


Pssm-ID: 177895 [Multi-domain]  Cd Length: 280  Bit Score: 76.02  E-value: 6.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEA--LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PLN02253   19 KVALVTGGATGIGESIVRLFHKHGAKVCIVDLQDDLgqNVCDSLGGEPNVCFFHCDVTVEDDVSRAVDFTVDKFGTLDIM 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGY--ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSpGIASYQAAKFAVDG 162
Cdd:PLN02253   99 VNNAGLtgPPCPDIRNVELSEFEKVFDVNVKGVFLGMKHAARIMIPLKKGSIVSLCSVASAIGGL-GPHAYTGSKHAVLG 177
                         170       180
                  ....*....|....*....|....*....
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATDWA 191
Cdd:PLN02253  178 LTRSVAAELGKHGIRVNCVSPYAVPTALA 206
PRK07577 PRK07577
SDR family oxidoreductase;
11-189 9.35e-16

SDR family oxidoreductase;


Pssm-ID: 181044 [Multi-domain]  Cd Length: 234  Bit Score: 74.76  E-value: 9.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRP------EALAADLAEYGDRVLPLALDVTSpdaaraaveaavarfGRIDVL 84
Cdd:PRK07577    8 VTGATKGIGLALSLRLANLGHQVIGIARSAiddfpgELFACDLADIEQTAATLAQINEI---------------HPVDAI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGgrVGGSPGIASYQAAKFAVDGFS 164
Cdd:PRK07577   73 VNNVGIALPQPLGKIDLAALQDVYDLNVRAAVQVTQAFLEGMKLREQGRIVNICSRA--IFGALDRTSYSAAKSALVGCT 150
                         170       180
                  ....*....|....*....|....*
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK07577  151 RTWALELAEYGITVNAVAPGPIETE 175
PRK07831 PRK07831
SDR family oxidoreductase;
17-184 9.90e-16

SDR family oxidoreductase;


Pssm-ID: 236110 [Multi-domain]  Cd Length: 262  Bit Score: 75.07  E-value: 9.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  17 GFGRALVDAVLAAGDLVVAT---ARRPEALAADLAE--YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGYA 91
Cdd:PRK07831   29 GIGSATARRALEEGARVVISdihERRLGETADELAAelGLGRVEAVVCDVTSEAQVDALIDAAVERLGRLDVLVNNAGLG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  92 NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVV--QFSSIGGRvgGSPGIASYQAAKFAVDGFSRVLAT 169
Cdd:PRK07831  109 GQTPVVDMTDDEWSRVLDVTLTGTFRATRAALRYMRARGHGGVIvnNASVLGWR--AQHGQAHYAAAKAGVMALTRCSAL 186
                         170
                  ....*....|....*
gi 1713980362 170 ETAPFGVRVMVVEPS 184
Cdd:PRK07831  187 EAAEYGVRINAVAPS 201
PRK06057 PRK06057
short chain dehydrogenase; Provisional
11-178 1.44e-15

short chain dehydrogenase; Provisional


Pssm-ID: 180371 [Multi-domain]  Cd Length: 255  Bit Score: 74.77  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGdrVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGy 90
Cdd:PRK06057   12 ITGGGSGIGLATARRLAAEGATVVVGDIDPEAGKAAADEVG--GLFVPTDVTDEDAVNALFDTAAETYGSVDIAFNNAG- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 anVSP-----IETTE-DADFRAQfETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFS 164
Cdd:PRK06057   89 --ISPpeddsILNTGlDAWQRVQ-DVNLTSVYLCCKAALPHMVRQGKGSIINTASFVAVMGSATSQISYTASKGGVLAMS 165
                         170
                  ....*....|....
gi 1713980362 165 RVLATETAPFGVRV 178
Cdd:PRK06057  166 RELGVQFARQGIRV 179
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
11-189 1.65e-15

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 74.80  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:cd08935    10 ITGGTGVLGGAMARALAQAGAKVAALGRNQEKGdkvAKEITALGGRAIALAADVLDRASLERAREEIVAQFGTVDILING 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGyANvSPIETTEDADFRAQFETNFW-----GVYHVTR-----AALP------VLRRQGAGTVVQFSSIGGRVGGSPgIA 151
Cdd:cd08935    90 AG-GN-HPDATTDPEHYEPETEQNFFdldeeGWEFVFDlnlngSFLPsqvfgkDMLEQKGGSIINISSMNAFSPLTK-VP 166
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1713980362 152 SYQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd08935   167 AYSAAKAAVSNFTQWLAVEFATTGVRVNAIAPGFFVTP 204
PRK12745 PRK12745
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
6-243 2.63e-15

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


Pssm-ID: 237188 [Multi-domain]  Cd Length: 256  Bit Score: 73.84  E-value: 2.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   6 PQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEA----LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK12745    2 RPVALVTGGRRGIGLGIARALAAAGFDLAINDRPDDEelaaTQQELRALGVEVIFFPADVADLSAHEAMLDAAQAAWGRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSP---IETTEDAdFRAQFETNFWGVYHVTRA------ALPVLRRQGAGTVVQFSSIGGrVGGSPGIAS 152
Cdd:PRK12745   82 DCLVNNAGVGVKVRgdlLDLTPES-FDRVLAINLRGPFFLTQAvakrmlAQPEPEELPHRSIVFVSSVNA-IMVSPNRGE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 153 YQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwagssMTVhDVPEAYDATVGAMNRLMRQntAGAAGDPHRAaei 232
Cdd:PRK12745  160 YCISKAGLSMAAQLFAARLAEEGIGVYEVRPGLIKTD-----MTA-PVTAKYDALIAKGLVPMPR--WGEPEDVARA--- 228
                         250
                  ....*....|.
gi 1713980362 233 iVRTVRRGELP 243
Cdd:PRK12745  229 -VAALASGDLP 238
SDH_SDR_c cd05363
Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter ...
5-183 3.28e-15

Sorbitol dehydrogenase (SDH), classical (c) SDR; This bacterial subgroup includes Rhodobacter sphaeroides SDH, and other SDHs. SDH preferentially interconverts D-sorbitol (D-glucitol) and D-fructose, but also interconverts L-iditol/L-sorbose and galactitol/D-tagatose. SDH is NAD-dependent and is a dimeric member of the SDR family. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187621 [Multi-domain]  Cd Length: 254  Bit Score: 73.42  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:cd05363     2 DGKTALITGSARGIGRAFAQAYVREGARVAIADINLEAARATAAEIGPAACAISLDVTDQASIDRCVAALVDRWGSIDIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVGGSPgIASYQAAKFAVDGF 163
Cdd:cd05363    82 VNNAALFDLAPIVDITRESYDRLFAINVSGTLFMMQAVARAMIAQGrGGKIINMASQAGRRGEAL-VGVYCATKAAVISL 160
                         170       180
                  ....*....|....*....|
gi 1713980362 164 SRVLATETAPFGVRVMVVEP 183
Cdd:cd05363   161 TQSAGLNLIRHGINVNAIAP 180
PRK07069 PRK07069
short chain dehydrogenase; Validated
10-178 3.66e-15

short chain dehydrogenase; Validated


Pssm-ID: 180822 [Multi-domain]  Cd Length: 251  Bit Score: 73.21  E-value: 3.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLV----VATARRPEALAADL-AEYGDRV-LPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK07069    3 FITGAAGGLGRAIARRMAEQGAKVfltdINDAAGLDAFAAEInAAHGEGVaFAAVQDVTDEAQWQALLAQAADAMGGLSV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGF 163
Cdd:PRK07069   83 LVNNAGVGSFGAIEQIELDEWRRVMAINVESIFLGCKHALPYLRASQPASIVNISSVAAFK-AEPDYTAYNASKAAVASL 161
                         170
                  ....*....|....*
gi 1713980362 164 SRVLATETAPFGVRV 178
Cdd:PRK07069  162 TKSIALDCARRGLDV 176
PRK12938 PRK12938
3-ketoacyl-ACP reductase;
7-233 5.85e-15

3-ketoacyl-ACP reductase;


Pssm-ID: 171822 [Multi-domain]  Cd Length: 246  Bit Score: 72.74  E-value: 5.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVA----TARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK12938    4 RIAYVTGGMGGIGTSICQRLHKDGFKVVAgcgpNSPRRVKWLEDQKALGFDFIASEGNVGDWDSTKAAFDKVKAEVGEID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDG 162
Cdd:PRK12938   84 VLVNNAGITRDVVFRKMTREDWTAVIDTNLTSLFNVTKQVIDGMVERGWGRIINISSVNGQ-KGQFGQTNYSTAKAGIHG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATDWAGSsmTVHDVPEAYDATVgAMNRLmrqntagaaGDPHRAAEII 233
Cdd:PRK12938  163 FTMSLAQEVATKGVTVNTVSPGYIGTDMVKA--IRPDVLEKIVATI-PVRRL---------GSPDEIGSIV 221
BKR_1_SDR_c cd05337
putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) ...
11-243 6.82e-15

putative beta-ketoacyl acyl carrier protein [ACP] reductase (BKR), subgroup 1, classical (c) SDR; This subgroup includes Escherichia coli CFT073 FabG. The Escherichai coli K12 BKR, FabG, belongs to a different subgroup. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187596 [Multi-domain]  Cd Length: 255  Bit Score: 72.88  E-value: 6.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAE---YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05337     6 VTGASRGIGRAIATELAARGfDIAINDLPDDDQATEVVAEvlaAGRRAIYFQADIGELSDHEALLDQAWEDFGRLDCLVN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYAnVSP----IETTEDAdFRAQFETNFWGVYHVTRA-ALPVLRRQGA-----GTVVQFSSIGGrVGGSPGIASYQAA 156
Cdd:cd05337    86 NAGIA-VRPrgdlLDLTEDS-FDRLIAINLRGPFFLTQAvARRMVEQPDRfdgphRSIIFVTSINA-YLVSPNRGEYCIS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 157 KFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwagssMTVhDVPEAYDATVGAmnRLMRQNTAGAAGDPHRAaeiiVRT 236
Cdd:cd05337   163 KAGLSMATRLLAYRLADEGIAVHEIRPGLIHTD-----MTA-PVKEKYDELIAA--GLVPIRRWGQPEDIAKA----VRT 230

                  ....*..
gi 1713980362 237 VRRGELP 243
Cdd:cd05337   231 LASGLLP 237
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
7-178 7.06e-15

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 72.88  E-value: 7.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPEAL-AADL--AEYGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:cd05322     3 QVAVVIGGGQTLGEFLCHGLAEAGyDVAVADINSENAEkVADEinAEYGEKAYGFGADATNEQSVIALSKGVDEIFKRVD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVgGSPGIASYQAAKFAVD 161
Cdd:cd05322    83 LLVYSAGIAKSAKITDFELGDFDRSLQVNLVGYFLCAREFSKLMIRDGiQGRIIQINSKSGKV-GSKHNSGYSAAKFGGV 161
                         170
                  ....*....|....*..
gi 1713980362 162 GFSRVLATETAPFGVRV 178
Cdd:cd05322   162 GLTQSLALDLAEHGITV 178
PR_SDR_c cd05357
pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR ...
11-184 1.36e-14

pteridine reductase (PR), classical (c) SDRs; Pteridine reductases (PRs), members of the SDR family, catalyzes the NAD-dependent reduction of folic acid, dihydrofolate and related compounds. In Leishmania, pteridine reductase (PTR1) acts to circumvent the anti-protozoan drugs that attack dihydrofolate reductase activity. Proteins in this subgroup have an N-terminal NAD-binding motif and a YxxxK active site motif, but have an Asp instead of the usual upstream catalytic Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187615 [Multi-domain]  Cd Length: 234  Bit Score: 71.54  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEA----LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd05357     5 VTGAAKRIGRAIAEALAAEGYRVVVHYNRSEAeaqrLKDELNALRNSAVLVQADLSDFAACADLVAAAFRAFGRCDVLVN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSRV 166
Cdd:cd05357    85 NASAFYPTPLGQGSEDAWAELFGINLKAPYLLIQAFARRLAGSRNGSIINIIDAMTD-RPLTGYFAYCMSKAALEGLTRS 163
                         170
                  ....*....|....*...
gi 1713980362 167 LATETAPFgVRVMVVEPS 184
Cdd:cd05357   164 AALELAPN-IRVNGIAPG 180
PRK07097 PRK07097
gluconate 5-dehydrogenase; Provisional
7-188 1.38e-14

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 235933 [Multi-domain]  Cd Length: 265  Bit Score: 72.02  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEY---GDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK07097   11 KIALITGASYGIGFAIAKAYAKAGATIVFNDINQELVDKGLAAYrelGIEAHGYVCDVTDEDGVQAMVSQIEKEVGVIDI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGF 163
Cdd:PRK07097   91 LVNNAGIIKRIPMLEMSAEDFRQVIDIDLNAPFIVSKAVIPSMIKKGHGKIINICSMMSEL-GRETVSAYAAAKGGLKML 169
                         170       180
                  ....*....|....*....|....*
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK07097  170 TKNIASEYGEANIQCNGIGPGYIAT 194
PRK08278 PRK08278
SDR family oxidoreductase;
10-138 1.46e-14

SDR family oxidoreductase;


Pssm-ID: 181349 [Multi-domain]  Cd Length: 273  Bit Score: 71.86  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEA----------LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFG 79
Cdd:PRK08278   10 FITGASRGIGLAIALRAARDGANIVIAAKTAEPhpklpgtihtAAEEIEAAGGQALPLVGDVRDEDQVAAAVAKAVERFG 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362  80 RIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFS 138
Cdd:PRK08278   90 GIDICVNNASAINLTGTEDTPMKRFDLMQQINVRGTFLVSQACLPHLKKSENPHILTLS 148
Mgc4172-like_SDR_c cd05343
human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These ...
7-222 1.48e-14

human Mgc4172-like, classical (c) SDRs; Human Mgc4172-like proteins, putative SDRs. These proteins are members of the SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187601 [Multi-domain]  Cd Length: 250  Bit Score: 71.77  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEYG-DRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:cd05343     7 RVALVTGASVGIGAAVARALVQHGMKVVGCARRVdkiEALAAECQSAGyPTLFPYQCDLSNEEQILSMFSAIRTQHQGVD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA--GTVVQFSSIGG-RVGGSPGIASYQAAKFA 159
Cdd:cd05343    87 VCINNAGLARPEPLLSGKTEGWKEMFDVNVLALSICTREAYQSMKERNVddGHIININSMSGhRVPPVSVFHFYAATKHA 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1713980362 160 VDGFSRVLATE--TAPFGVRVMVVEPSGFATDWAgsSMTVHDVPEAYDATVGAMNRLMRQNTAGA 222
Cdd:cd05343   167 VTALTEGLRQElrEAKTHIRATSISPGLVETEFA--FKLHDNDPEKAAATYESIPCLKPEDVANA 229
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
11-189 2.20e-14

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 71.47  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08277   15 ITGGGGVLGGAMAKELARAGAKVAILDRNQEkaeAVVAEIKAAGGEALAVKADVLDKESLEQARQQILEDFGPCDILING 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AG------------YANVSPIETTED---ADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGgrvGGSP--GI 150
Cdd:PRK08277   95 AGgnhpkattdnefHELIEPTKTFFDldeEGFEFVFDLNLLGTLLPTQVFAKDMVGRKGGNIINISSMN---AFTPltKV 171
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1713980362 151 ASYQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK08277  172 PAYSAAKAAISNFTQWLAVHFAKVGIRVNAIAPGFFLTE 210
PRK08936 PRK08936
glucose-1-dehydrogenase; Provisional
7-188 6.79e-14

glucose-1-dehydrogenase; Provisional


Pssm-ID: 181585 [Multi-domain]  Cd Length: 261  Bit Score: 70.14  E-value: 6.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE----YGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK08936    8 KVVVITGGSTGLGRAMAVRFGKEKAKVVINYRSDEEEANDVAEeikkAGGEAIAVKGDVTVESDVVNLIQTAVKEFGTLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVGGsPGIASYQAAKFAVD 161
Cdd:PRK08936   88 VMINNAGIENAVPSHEMSLEDWNKVINTNLTGAFLGSREAIKYFVEHDiKGNIINMSSVHEQIPW-PLFVHYAASKGGVK 166
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK08936  167 LMTETLAMEYAPKGIRVNNIGPGAINT 193
PRK12743 PRK12743
SDR family oxidoreductase;
6-188 1.27e-13

SDR family oxidoreductase;


Pssm-ID: 237187 [Multi-domain]  Cd Length: 256  Bit Score: 69.29  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   6 PQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPE----ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK12743    2 AQVAIVTASDSGIGKACALLLAQQGFDIGITWHSDEegakETAEEVRSHGVRAEIRQLDLSDLPEGAQALDKLIQRLGRI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVgGSPGIASYQAAKFAV 160
Cdd:PRK12743   82 DVLVNNAGAMTKAPFLDMDFDEWRKIFTVDVDGAFLCSQIAARHMVKQGqGGRIINITSVHEHT-PLPGASAYTAAKHAL 160
                         170       180
                  ....*....|....*....|....*...
gi 1713980362 161 DGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK12743  161 GGLTKAMALELVEHGILVNAVAPGAIAT 188
SDR cd02266
Short-chain dehydrogenases/reductases (SDR); SDRs are a functionally diverse family of ...
80-189 2.18e-13

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


Pssm-ID: 187535 [Multi-domain]  Cd Length: 186  Bit Score: 67.16  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  80 RIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFA 159
Cdd:cd02266    31 RRDVVVHNAAILDDGRLIDLTGSRIERAIRANVVGTRRLLEAARELMKAKRLGRFILISSVAG-LFGAPGLGGYAASKAA 109
                          90       100       110
                  ....*....|....*....|....*....|
gi 1713980362 160 VDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd02266   110 LDGLAQQWASEGWGNGLPATAVACGTWAGS 139
PRK06949 PRK06949
SDR family oxidoreductase;
7-189 3.47e-13

SDR family oxidoreductase;


Pssm-ID: 180773 [Multi-domain]  Cd Length: 258  Bit Score: 67.86  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK06949   10 KVALVTGASSGLGARFAQVLAQAGAKVVLASRRVErlkELRAEIEAEGGAAHVVSLDVTDYQSIKAAVAHAETEAGTIDI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTR--AALPVLRRQGAGT------VVQFSSIGG-RVggSPGIASYQ 154
Cdd:PRK06949   90 LVNNSGVSTTQKLVDVTPADFDFVFDTNTRGAFFVAQevAKRMIARAKGAGNtkpggrIINIASVAGlRV--LPQIGLYC 167
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1713980362 155 AAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK06949  168 MSKAAVVHMTRAMALEWGRHGINVNAICPGYIDTE 202
PRK07677 PRK07677
short chain dehydrogenase; Provisional
7-183 4.37e-13

short chain dehydrogenase; Provisional


Pssm-ID: 181077 [Multi-domain]  Cd Length: 252  Bit Score: 67.40  E-value: 4.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAA---DLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK07677    2 KVVIITGGSSGMGKAMAKRFAEEGANVVITGRTKEKLEEaklEIEQFPGQVLTVQMDVRNPEDVQKMVEQIDEKFGRIDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGagtvvQFSSIGGRV-----GGSPGIASYQAAKF 158
Cdd:PRK07677   82 LINNAAGNFICPAEDLSVNGWNSVIDIVLNGTFYCSQAVGKYWIEKG-----IKGNIINMVatyawDAGPGVIHSAAAKA 156
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 159 AVDGFSRVLATE-TAPFGVRVMVVEP 183
Cdd:PRK07677  157 GVLAMTRTLAVEwGRKYGIRVNAIAP 182
PRK08085 PRK08085
gluconate 5-dehydrogenase; Provisional
11-189 4.59e-13

gluconate 5-dehydrogenase; Provisional


Pssm-ID: 181225 [Multi-domain]  Cd Length: 254  Bit Score: 67.47  E-value: 4.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVV---ATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08085   14 ITGSAQGIGFLLATGLAEYGAEIIindITAERAELAVAKLRQEGIKAHAAPFNVTHKQEVEAAIEHIEKDIGPIDVLINN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPgIASYQAAKFAVDGFSRVL 167
Cdd:PRK08085   94 AGIQRRHPFTEFPEQEWNDVIAVNQTAVFLVSQAVARYMVKRQAGKIINICSMQSELGRDT-ITPYAASKGAVKMLTRGM 172
                         170       180
                  ....*....|....*....|..
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK08085  173 CVELARHNIQVNGIAPGYFKTE 194
17beta-HSD1_like_SDR_c cd05356
17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) ...
11-189 8.48e-13

17-beta-hydroxysteroid dehydrogenases (17beta-HSDs) types -1, -3, and -12, -like, classical (c) SDRs; This subgroup includes various 17-beta-hydroxysteroid dehydrogenases and 3-ketoacyl-CoA reductase, these are members of the SDR family, and contain the canonical active site tetrad and glycine-rich NAD-binding motif of the classical SDRs. 3-ketoacyl-CoA reductase (KAR, aka 17beta-HSD type 12, encoded by HSD17B12) acts in fatty acid elongation; 17beta- hydroxysteroid dehydrogenases are isozymes that catalyze activation and inactivation of estrogen and androgens, and include members of the SDR family. 17beta-estradiol dehydrogenase (aka 17beta-HSD type 1, encoded by HSD17B1) converts estrone to estradiol. Estradiol is the predominant female sex hormone. 17beta-HSD type 3 (aka testosterone 17-beta-dehydrogenase 3, encoded by HSD17B3) catalyses the reduction of androstenedione to testosterone, it also accepts estrogens as substrates. This subgroup also contains a putative steroid dehydrogenase let-767 from Caenorhabditis elegans, mutation in which results in hypersensitivity to cholesterol limitation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.


Pssm-ID: 187614 [Multi-domain]  Cd Length: 239  Bit Score: 66.47  E-value: 8.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAE-YGDRVLPLALDVTSPDAAraaveaavarFGR------ 80
Cdd:cd05356     6 VTGATDGIGKAYAEELAKRGFNVILISRTQEkldAVAKEIEEkYGVETKTIAADFSAGDDI----------YERiekele 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  81 ---IDVLVNNAGYANVSPIETTEDADFRAQ--FETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGgSPGIASYQA 155
Cdd:cd05356    76 gldIGILVNNVGISHSIPEYFLETPEDELQdiINVNVMATLKMTRLILPGMVKRKKGAIVNISSFAGLIP-TPLLATYSA 154
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1713980362 156 AKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd05356   155 SKAFLDFFSRALYEEYKSQGIDVQSLLPYLVATK 188
PRK08251 PRK08251
SDR family oxidoreductase;
11-213 1.12e-12

SDR family oxidoreductase;


Pssm-ID: 181324 [Multi-domain]  Cd Length: 248  Bit Score: 66.11  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEY--GDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK08251    7 ITGASSGLGAGMAREFAAKGRDLALCARRTdrlEELKAELLARypGIKVAVAALDVNDHDQVFEVFAEFRDELGGLDRVI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTE-DADfRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFS 164
Cdd:PRK08251   87 VNAGIGKGARLGTGKfWAN-KATAETNFVAALAQCEAAMEIFREQGSGHLVLISSVSAVRGLPGVKAAYAASKAGVASLG 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFATDW---AGSSMTVHDVPEAYDATVGAMNR 213
Cdd:PRK08251  166 EGLRAELAKTPIKVSTIEPGYIRSEMnakAKSTPFMVDTETGVKALVKAIEK 217
PRK05876 PRK05876
short chain dehydrogenase; Provisional
11-228 1.34e-12

short chain dehydrogenase; Provisional


Pssm-ID: 135637 [Multi-domain]  Cd Length: 275  Bit Score: 66.52  E-value: 1.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVVATARRP--EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK05876   11 ITGGASGIGLATGTEFARRGaRVVLGDVDKPglRQAVNHLRAEGFDVHGVMCDVRHREEVTHLADEAFRLLGHVDVVFSN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK05876   91 AGIVVGGPIVEMTHDDWRWVIDVDLWGSIHTVEAFLPRLLEQGTGGHVVFTASFAGLVPNAGLGAYGVAKYGVVGLAETL 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRLMRQNTAGAAGDPHR 228
Cdd:PRK05876  171 AREVTADGIGVSVLCPMVVETNLVANSERIRGAACAQSSTTGSPGPLPLQDDNLGVDDIAQ 231
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-189 1.79e-12

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


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 65.55  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALA---ADLAEYGdRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK05786   10 IIGVSEGLGYAVAYFALKEGAQVCINSRNENKLKrmkKTLSKYG-NIHYVVGDVSSTESARNVIEKAAKVLNAIDGLVVT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIEttEDADFRAQFETNFWGVYHVTRAALPVLRRqgAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK05786   89 VGGYVEDTVE--EFSGLEEMLTNHIKIPLYAVNASLRFLKE--GSSIVLVSSMSGIYKASPDQLSYAVAKAGLAKAVEIL 164
                         170       180
                  ....*....|....*....|..
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK05786  165 ASELLGRGIRVNGIAPTTISGD 186
Tthb094_like_SDR_c cd11730
Tthb094 and related proteins, classical (c) SDRs; Tthb094 from Thermus Thermophilus is a ...
10-191 3.55e-12

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


Pssm-ID: 212496 [Multi-domain]  Cd Length: 206  Bit Score: 64.08  E-value: 3.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPlaLDVTSpdaaRAAVEAAVARFGRIDVLVNNAG 89
Cdd:cd11730     2 LILGATGGIGRALARALAGRGWRLLLSGRDAGALAGLAAEVGALARP--ADVAA----ELEVWALAQELGPLDLLVYAAG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVvqfssIGGRVG--GSPGIASYQAAKFAVDGFSRVL 167
Cdd:cd11730    76 AILGKPLARTKPAAWRRILDANLTGAALVLKHALALLAAGARLVF-----LGAYPElvMLPGLSAYAAAKAALEAYVEVA 150
                         170       180
                  ....*....|....*....|....*
gi 1713980362 168 ATETApfGVRVMVVEPSGFATD-WA 191
Cdd:cd11730   151 RKEVR--GLRLTLVRPPAVDTGlWA 173
PRK07041 PRK07041
SDR family oxidoreductase;
11-234 4.02e-12

SDR family oxidoreductase;


Pssm-ID: 235914 [Multi-domain]  Cd Length: 230  Bit Score: 64.29  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGD--RVLPLALDVTSPDAARAAVEAAvarfGRIDVLVNNA 88
Cdd:PRK07041    2 VVGGSSGIGLALARAFAAEGARVTIASRSRDRLAAAARALGGgaPVRTAALDITDEAAVDAFFAEA----GPFDHVVITA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GYANVSPIETTEDADFRAQFETNFWGVYHVTRAAlpvlrRQGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSRVLA 168
Cdd:PRK07041   78 ADTPGGPVRALPLAAAQAAMDSKFWGAYRVARAA-----RIAPGGSLTFVSGFAAVRPSASGVLQGAINAALEALARGLA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1713980362 169 TETAPfgVRVMVVEPSGFATD-WAGSSmtvhdvPEAYDATVGAM-NRLmrqnTAGAAGDPHRAAEIIV 234
Cdd:PRK07041  153 LELAP--VRVNTVSPGLVDTPlWSKLA------GDAREAMFAAAaERL----PARRVGQPEDVANAIL 208
PRK06128 PRK06128
SDR family oxidoreductase;
11-188 4.12e-12

SDR family oxidoreductase;


Pssm-ID: 180413 [Multi-domain]  Cd Length: 300  Bit Score: 65.27  E-value: 4.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAEY----GDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK06128   60 ITGADSGIGRATAIAFAREGaDIALNYLPEEEQDAAEVVQLiqaeGRKAVALPGDLKDEAFCRQLVERAVKELGGLDILV 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAG-YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRrQGAgTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFS 164
Cdd:PRK06128  140 NIAGkQTAVKDIADITTEQFDATFKTNVYAMFWLCKAAIPHLP-PGA-SIINTGSIQS-YQPSPTLLDYASTKAAIVAFT 216
                         170       180
                  ....*....|....*....|....
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK06128  217 KALAKQVAEKGIRVNAVAPGPVWT 240
PRK07775 PRK07775
SDR family oxidoreductase;
11-200 4.20e-12

SDR family oxidoreductase;


Pssm-ID: 181113 [Multi-domain]  Cd Length: 274  Bit Score: 65.16  E-value: 4.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRP---EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK07775   15 VAGASSGIGAATAIELAAAGFPVALGARRVekcEELVDKIRADGGEAVAFPLDVTDPDSVKSFVAQAEEALGEIEVLVSG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFSRVL 167
Cdd:PRK07775   95 AGDTYFGKLHEISTEQFESQVQIHLVGANRLATAVLPGMIERRRGDLIFVGSDVALR-QRPHMGAYGAAKAGLEAMVTNL 173
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1713980362 168 ATETAPFGVRVMVVEPSGFATDwAGSSMTVHDV 200
Cdd:PRK07775  174 QMELEGTGVRASIVHPGPTLTG-MGWSLPAEVI 205
fabG PRK08217
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-203 4.88e-12

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


Pssm-ID: 181297 [Multi-domain]  Cd Length: 253  Bit Score: 64.60  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08217   10 ITGGAQGLGRAMAEYLAQKGAKLALIDLNQEKLeeaVAECGALGTEVRGYAANVTDEEDVEATFAQIAEDFGQLNGLINN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTED---------ADFRAQFETNFWGVYHVTR-AALPVLRRQGAGTVVQFSSIGgrVGGSPGIASYQAAK 157
Cdd:PRK08217   90 AGILRDGLLVKAKDgkvtskmslEQFQSVIDVNLTGVFLCGReAAAKMIESGSKGVIINISSIA--RAGNMGQTNYSASK 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEPSGFATDwagssMTVHDVPEA 203
Cdd:PRK08217  168 AGVAAMTVTWAKELARYGIRVAAIAPGVIETE-----MTAAMKPEA 208
PRK06123 PRK06123
SDR family oxidoreductase;
7-189 5.15e-12

SDR family oxidoreductase;


Pssm-ID: 180411 [Multi-domain]  Cd Length: 248  Bit Score: 64.41  E-value: 5.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARR----PEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRID 82
Cdd:PRK06123    3 KVMIITGASRGIGAATALLAAERGYAVCLNYLRnrdaAEAVVQAIRRQGGEALAVAADVADEADVLRLFEAVDRELGRLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  83 VLVNNAGYANVSP-IETTEDADFRAQFETNFWGVYHVTRAALPVLR-RQGA--GTVVQFSSIGGRVGGSPGIASYQAAKF 158
Cdd:PRK06123   83 ALVNNAGILEAQMrLEQMDAARLTRIFATNVVGSFLCAREAVKRMStRHGGrgGAIVNVSSMAARLGSPGEYIDYAASKG 162
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK06123  163 AIDTMTIGLAKEVAAEGIRVNAVRPGVIYTE 193
PRK12859 PRK12859
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-190 8.63e-12

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


Pssm-ID: 183797 [Multi-domain]  Cd Length: 256  Bit Score: 64.04  E-value: 8.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSR--GFGRALVDAVLAAGDLVVAT--------------ARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAA 74
Cdd:PRK12859   11 VTGVSRldGIGAAICKELAEAGADIFFTywtaydkempwgvdQDEQIQLQEELLKNGVKVSSMELDLTQNDAPKELLNKV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  75 VARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSiGGRVGGSPGIASYQ 154
Cdd:PRK12859   91 TEQLGYPHILVNNAAYSTNNDFSNLTAEELDKHYMVNVRATTLLSSQFARGFDKKSGGRIINMTS-GQFQGPMVGELAYA 169
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1713980362 155 AAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDW 190
Cdd:PRK12859  170 ATKGAIDALTSSLAAEVAHLGITVNAINPGPTDTGW 205
PRK05855 PRK05855
SDR family oxidoreductase;
11-240 2.14e-11

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 64.23  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALA--ADLAE-YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK05855  320 VTGAGSGIGRETALAFAREGAEVVASDIDEAAAErtAELIRaAGAVAHAYRVDVSDADAMEAFAEWVRAEHGVPDIVVNN 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFSRV 166
Cdd:PRK05855  400 AGIGMAGGFLDTSAEDWDRVLDVNLWGVIHGCRLFGRQMVERGtGGHIVNVASAAA-YAPSRSLPAYATSKAAVLMLSEC 478
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1713980362 167 LATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNRLMRQNTAGaagdPHRAAEIIVRTVRRG 240
Cdd:PRK05855  479 LRAELAAAGIGVTAICPGFVDTNIVATTRFAGADAEDEARRRGRADKLYQRRGYG----PEKVAKAIVDAVKRN 548
PRK12748 PRK12748
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-201 2.21e-11

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


Pssm-ID: 237189 [Multi-domain]  Cd Length: 256  Bit Score: 62.78  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSR--GFGRALVDAVLAAGDLVVAT------------ARRPEA--LAADLAEYGDRVLPLALDVTSPDAARAAVEAA 74
Cdd:PRK12748   10 VTGASRlnGIGAAVCRRLAAKGIDIFFTywspydktmpwgMHDKEPvlLKEEIESYGVRCEHMEIDLSQPYAPNRVFYAV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  75 VARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNfwgvyhvTRAALpVLRRQGA--------GTVVQFSSiGGRVGG 146
Cdd:PRK12748   90 SERLGDPSILINNAAYSTHTRLEELTAEQLDKHYAVN-------VRATM-LLSSAFAkqydgkagGRIINLTS-GQSLGP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1713980362 147 SPGIASYQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVP 201
Cdd:PRK12748  161 MPDELAYAATKGAIEAFTKSLAPELAEKGITVNAVNPGPTDTGWITEELKHHLVP 215
PRK09730 PRK09730
SDR family oxidoreductase;
11-189 3.69e-11

SDR family oxidoreductase;


Pssm-ID: 182051 [Multi-domain]  Cd Length: 247  Bit Score: 61.79  E-value: 3.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAAD----LAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK09730    6 VTGGSRGIGRATALLLAQEGYTVAVNYQQNLHAAQEvvnlITQAGGKAFVLQADISDENQVVAMFTAIDQHDEPLAALVN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYA-NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVL-RRQGA--GTVVQFSSIGGRVGGSPGIASYQAAKFAVDG 162
Cdd:PRK09730   86 NAGILfTQCTVENLTAERINRVLSTNVTGYFLCCREAVKRMaLKHGGsgGAIVNVSSAASRLGAPGEYVDYAASKGAIDT 165
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK09730  166 LTTGLSLEVAAQGIRVNCVRPGFIYTE 192
PRK06194 PRK06194
hypothetical protein; Provisional
7-171 4.13e-11

hypothetical protein; Provisional


Pssm-ID: 180458 [Multi-domain]  Cd Length: 287  Bit Score: 62.34  E-value: 4.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK06194    7 KVAVITGAASGFGLAFARIGAALGMKLVLADVQQDALdraVAELRAQGAEVLGVRTDVSDAAQVEALADAALERFGAVHL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGA------GTVVQFSSIGGRVgGSPGIASYQAAK 157
Cdd:PRK06194   87 LFNNAGVGAGGLVWENSLADWEWVLGVNLWGVIHGVRAFTPLMLAAAEkdpayeGHIVNTASMAGLL-APPAMGIYNVSK 165
                         170
                  ....*....|....
gi 1713980362 158 FAVdgfsrVLATET 171
Cdd:PRK06194  166 HAV-----VSLTET 174
DHRS1-like_SDR_c cd09763
human dehydrogenase/reductase (SDR family) member 1 (DHRS1) -like, classical (c) SDRs; This ...
7-189 4.57e-11

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


Pssm-ID: 187664 [Multi-domain]  Cd Length: 265  Bit Score: 61.69  E-value: 4.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRP----EALAADLAEYGDRVLPLALDVTSPDAARAA-VEAAVARFGRI 81
Cdd:cd09763     4 KIALVTGASRGIGRGIALQLGEAGATVYITGRTIlpqlPGTAEEIEARGGKCIPVRCDHSDDDEVEALfERVAREQQGRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAgYANVSPIETTEDADFRAQFETNfW---------GVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIAs 152
Cdd:cd09763    84 DILVNNA-YAAVQLILVGVAKPFWEEPPTI-WddinnvglrAHYACSVYAAPLMVKAGKGLIVIISSTGG-LEYLFNVA- 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1713980362 153 YQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:cd09763   160 YGVGKAAIDRMAADMAHELKPHGVAVVSLWPGFVRTE 196
PRK06196 PRK06196
oxidoreductase; Provisional
11-188 4.73e-11

oxidoreductase; Provisional


Pssm-ID: 235736 [Multi-domain]  Cd Length: 315  Bit Score: 62.39  E-value: 4.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYgDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:PRK06196   31 VTGGYSGLGLETTRALAQAGAHVIVPARRPDVAREALAGI-DGVEVVMLDLADLESVRAFAERFLDSGRRIDILINNAGV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 AnVSPIETTEDAdFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRV------------GGSPGIAsYQAAKF 158
Cdd:PRK06196  110 M-ACPETRVGDG-WEAQFATNHLGHFALVNLLWPALAAGAGARVVALSSAGHRRspirwddphftrGYDKWLA-YGQSKT 186
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK06196  187 ANALFAVHLDKLGKDQGVRAFSVHPGGILT 216
HSDL2_SDR_c cd09762
human hydroxysteroid dehydrogenase-like protein 2 (HSDL2), classical (c) SDRs; This subgroup ...
10-128 5.03e-11

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


Pssm-ID: 187663 [Multi-domain]  Cd Length: 243  Bit Score: 61.31  E-value: 5.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEA----------LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFG 79
Cdd:cd09762     7 FITGASRGIGKAIALKAARDGANVVIAAKTAEPhpklpgtiytAAEEIEAAGGKALPCIVDIRDEDQVRAAVEKAVEKFG 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1713980362  80 RIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRR 128
Cdd:cd09762    87 GIDILVNNASAISLTGTLDTPMKRYDLMMGVNTRGTYLCSKACLPYLKK 135
PRK07576 PRK07576
short chain dehydrogenase; Provisional
10-183 6.84e-11

short chain dehydrogenase; Provisional


Pssm-ID: 236056 [Multi-domain]  Cd Length: 264  Bit Score: 61.51  E-value: 6.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPE---ALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK07576   13 VVVGGTSGINLGIAQAFARAGANVAVASRSQEkvdAAVAQLQQAGPEGLGVSADVRDYAAVEAAFAQIADEFGPIDVLVS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgTVVQFSSiGGRVGGSPGIASYQAAKFAVDGFSRV 166
Cdd:PRK07576   93 GAAGNFPAPAAGMSANGFKTVVDIDLLGTFNVLKAAYPLLRRPGA-SIIQISA-PQAFVPMPMQAHVCAAKAGVDMLTRT 170
                         170
                  ....*....|....*..
gi 1713980362 167 LATETAPFGVRVMVVEP 183
Cdd:PRK07576  171 LALEWGPEGIRVNSIVP 187
PRK08993 PRK08993
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
7-189 8.44e-11

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 181605 [Multi-domain]  Cd Length: 253  Bit Score: 61.04  E-value: 8.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK08993   11 KVAVVTGCDTGLGQGMALGLAEAGcDIVGINIVEPTETIEQVTALGRRFLSLTADLRKIDGIPALLERAVAEFGHIDILV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGyanvspIETTEDA-DFRAQ-----FETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVGGSPgIASYQAAKF 158
Cdd:PRK08993   91 NNAG------LIRREDAiEFSEKdwddvMNLNIKSVFFMSQAAAKHFIAQGnGGKIINIASMLSFQGGIR-VPSYTASKS 163
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1713980362 159 AVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK08993  164 GVMGVTRLMANEWAKHNINVNAIAPGYMATN 194
PRK09135 PRK09135
pteridine reductase; Provisional
1-183 1.08e-10

pteridine reductase; Provisional


Pssm-ID: 181668 [Multi-domain]  Cd Length: 249  Bit Score: 60.71  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRP----EALAADL-AEYGDRVLPLALDVTSPDAARAAVEAAV 75
Cdd:PRK09135    1 MMTDSAKVALITGGARRIGAAIARTLHAAGYRVAIHYHRSaaeaDALAAELnALRPGSAAALQADLLDPDALPELVAACV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  76 ARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGRvggSP--GIASY 153
Cdd:PRK09135   81 AAFGRLDALVNNASSFYPTPLGSITEAQWDDLFASNLKAPFFLSQAAAPQLRKQR-GAIVNITDIHAE---RPlkGYPVY 156
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 154 QAAKFAVDGFSRVLATETAPfGVRVMVVEP 183
Cdd:PRK09135  157 CAAKAALEMLTRSLALELAP-EVRVNAVAP 185
CR_SDR_c cd08936
Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine ...
1-183 1.50e-10

Porcine peroxisomal carbonyl reductase like, classical (c) SDR; This subgroup contains porcine peroxisomal carbonyl reductase and similar proteins. The porcine enzyme efficiently reduces retinals. This subgroup also includes human dehydrogenase/reductase (SDR family) member 4 (DHRS4), and human DHRS4L1. DHRS4 is a peroxisomal enzyme with 3beta-hydroxysteroid dehydrogenase activity; it catalyzes the reduction of 3-keto-C19/C21-steroids into 3beta-hydroxysteroids more efficiently than it does the retinal reduction. The human DHRS4 gene cluster contains DHRS4, DHRS4L2 and DHRS4L1. DHRS4L2 and DHRS4L1 are paralogs of DHRS4, DHRS4L2 being the most recent member. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187641 [Multi-domain]  Cd Length: 256  Bit Score: 60.25  E-value: 1.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDP---QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDRVLPLALDVTSPDAARAAVEAA 74
Cdd:cd08936     2 VTRRDPlanKVALVTASTDGIGLAIARRLAQDGAHVVVSSRKQQNVdraVATLQGEGLSVTGTVCHVGKAEDRERLVATA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  75 VARFGRIDVLVNNAGyanVSP-----IETTEDAdFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPG 149
Cdd:cd08936    82 VNLHGGVDILVSNAA---VNPffgniLDSTEEV-WDKILDVNVKATALMTKAVVPEMEKRGGGSVVIVSSVAA-FHPFPG 156
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1713980362 150 IASYQAAKFAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:cd08936   157 LGPYNVSKTALLGLTKNLAPELAPRNIRVNCLAP 190
PRK07985 PRK07985
SDR family oxidoreductase;
10-183 2.21e-10

SDR family oxidoreductase;


Pssm-ID: 181188 [Multi-domain]  Cd Length: 294  Bit Score: 60.01  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVV-----ATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK07985   53 LVTGGDSGIGRAAAIAYAREGADVAisylpVEEEDAQDVKKIIEECGRKAVLLPGDLSDEKFARSLVHEAHKALGGLDIM 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAG-YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRqGAgTVVQFSSIGGrVGGSPGIASYQAAKFAVDGF 163
Cdd:PRK07985  133 ALVAGkQVAIPDIADLTSEQFQKTFAINVFALFWLTQEAIPLLPK-GA-SIITTSSIQA-YQPSPHLLDYAATKAAILNY 209
                         170       180
                  ....*....|....*....|
gi 1713980362 164 SRVLATETAPFGVRVMVVEP 183
Cdd:PRK07985  210 SRGLAKQVAEKGIRVNIVAP 229
PRK06953 PRK06953
SDR family oxidoreductase;
11-161 4.51e-10

SDR family oxidoreductase;


Pssm-ID: 180774 [Multi-domain]  Cd Length: 222  Bit Score: 58.54  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAAdLAEYGDRVlpLALDVTSPDAARAAVEAAVARfgRIDVLVNNAGY 90
Cdd:PRK06953    6 IVGASRGIGREFVRQYRADGWRVIATARDAAALAA-LQALGAEA--LALDVADPASVAGLAWKLDGE--ALDAAVYVAGV 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1713980362  91 --ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGRVGGSPGIAS--YQAAKFAVD 161
Cdd:PRK06953   81 ygPRTEGVEPITREDFDAVMHTNVLGPMQLLPILLPLVEAAG-GVLAVLSSRMGSIGDATGTTGwlYRASKAALN 154
PRK12742 PRK12742
SDR family oxidoreductase;
11-189 4.58e-10

SDR family oxidoreductase;


Pssm-ID: 183714 [Multi-domain]  Cd Length: 237  Bit Score: 58.62  E-value: 4.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVAT-ARRPEALAADLAEYGDRVLplALDVTSPDAARAAVEAavarFGRIDVLVNNAG 89
Cdd:PRK12742   11 VLGGSRGIGAAIVRRFVTDGANVRFTyAGSKDAAERLAQETGATAV--QTDSADRDAVIDVVRK----SGALDILVVNAG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YANVSPIETTEDADFRAQFETNFWGVYHvtrAALPVLRR-QGAGTVVQFSSIGGRVGGSPGIASYQAAKFAVDGFSRVLA 168
Cdd:PRK12742   85 IAVFGDALELDADDIDRLFKINIHAPYH---ASVEAARQmPEGGRIIIIGSVNGDRMPVAGMAAYAASKSALQGMARGLA 161
                         170       180
                  ....*....|....*....|.
gi 1713980362 169 TETAPFGVRVMVVEPSGFATD 189
Cdd:PRK12742  162 RDFGPRGITINVVQPGPIDTD 182
sepiapter_red TIGR01500
sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain ...
11-244 5.13e-10

sepiapterin reductase; This model describes sepiapterin reductase, a member of the short chain dehydrogenase/reductase family. The enzyme catalyzes the last step in the biosynthesis of tetrahydrobiopterin. A similar enzyme in Bacillus cereus was isolated for its ability to convert benzil to (S)-benzoin, a property sepiapterin reductase also shares. Cutoff scores for this model are set such that benzil reductase scores between trusted and noise cutoffs.


Pssm-ID: 273660 [Multi-domain]  Cd Length: 256  Bit Score: 58.77  E-value: 5.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRA----LVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVA---------- 76
Cdd:TIGR01500   5 VTGASRGFGRTiaqeLAKCLKSPGSVLVLSARNDEALRQLKAEIGAERSGLRVVRVSLDLGAEAGLEQLLkalrelprpk 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  77 RFGRIdVLVNNAG-YANVSPIETT-EDADF-RAQFETNFWGVYHVTRAALPVLRR-QGAG-TVVQFSSIGGrVGGSPGIA 151
Cdd:TIGR01500  85 GLQRL-LLINNAGtLGDVSKGFVDlSDSTQvQNYWALNLTSMLCLTSSVLKAFKDsPGLNrTVVNISSLCA-IQPFKGWA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 152 SYQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwagssMTVHDVPEAYDATVGAMNRLMRQNtaGAAGDPHRAAE 231
Cdd:TIGR01500 163 LYCAGKAARDMLFQVLALEEKNPNVRVLNYAPGVLDTD-----MQQQVREESVDPDMRKGLQELKAK--GKLVDPKVSAQ 235
                         250
                  ....*....|...
gi 1713980362 232 IIVRTVRRGELPS 244
Cdd:TIGR01500 236 KLLSLLEKDKFKS 248
PRK12481 PRK12481
2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;
5-189 5.37e-10

2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD;


Pssm-ID: 171531 [Multi-domain]  Cd Length: 251  Bit Score: 58.76  E-value: 5.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   5 DPQVWFITGSSRGFGRALVDAVLAAG-DLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK12481    7 NGKVAIITGCNTGLGQGMAIGLAKAGaDIVGVGVAEAPETQAQVEALGRKFHFITADLIQQKDIDSIVSQAVEVMGHIDI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQG-AGTVVQFSSIGGRVGGSPgIASYQAAKFAVDG 162
Cdd:PRK12481   87 LINNAGIIRRQDLLEFGNKDWDDVININQKTVFFLSQAVAKQFVKQGnGGKIINIASMLSFQGGIR-VPSYTASKSAVMG 165
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK12481  166 LTRALATELSQYNINVNAIAPGYMATD 192
PRK08589 PRK08589
SDR family oxidoreductase;
11-188 7.18e-10

SDR family oxidoreductase;


Pssm-ID: 181491 [Multi-domain]  Cd Length: 272  Bit Score: 58.64  E-value: 7.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVAT--ARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNA 88
Cdd:PRK08589   11 ITGASTGIGQASAIALAQEGAYVLAVdiAEAVSETVDKIKSNGGKAKAYHVDISDEQQVKDFASEIKEQFGRVDVLFNNA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GYANVS------PIETtedadFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGRvGGSPGIASYQAAKFAVDG 162
Cdd:PRK08589   91 GVDNAAgriheyPVDV-----FDKIMAVDMRGTFLMTKMLLPLMMEQG-GSIINTSSFSGQ-AADLYRSGYNAAKGAVIN 163
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK08589  164 FTKSIAIEYGRDGIRANAIAPGTIET 189
haloalcohol_DH_SDR_c-like cd05361
haloalcohol dehalogenase, classical (c) SDRs; Dehalogenases cleave carbon-halogen bonds. ...
79-222 1.13e-09

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


Pssm-ID: 187619 [Multi-domain]  Cd Length: 242  Bit Score: 57.59  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  79 GRIDVLVNNAGYAN-VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAK 157
Cdd:cd05361    71 GAIDVLVSNDYIPRpMNPIDGTSEADIRQAFEALSIFPFALLQAAIAQMKKAGGGSIIFITSAVPK-KPLAYNSLYGPAR 149
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1713980362 158 FAVDGFSRVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDA--TVGAMNRLMRQNTAGA 222
Cdd:cd05361   150 AAAVALAESLAKELSRDNILVYAIGPNFFNSPTYFPTSDWENNPELRERvkRDVPLGRLGRPDEMGA 216
PRK08177 PRK08177
SDR family oxidoreductase;
11-194 1.34e-09

SDR family oxidoreductase;


Pssm-ID: 236173 [Multi-domain]  Cd Length: 225  Bit Score: 56.96  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDvtspDAARAAVEAAVARFGRIDVLVNNAGY 90
Cdd:PRK08177    6 IIGASRGLGLGLVDRLLERGWQVTATVRGPQQDTALQALPGVHIEKLDMN----DPASLDQLLQRLQGQRFDLLFVNAGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 ---ANVSPIETTEdADFRAQFETNFWGVYHVTRAALPVLRRqGAGTVVQFSSIGGRV--GGSPGIASYQAAKFAVDGFSR 165
Cdd:PRK08177   82 sgpAHQSAADATA-AEIGQLFLTNAIAPIRLARRLLGQVRP-GQGVLAFMSSQLGSVelPDGGEMPLYKASKAALNSMTR 159
                         170       180
                  ....*....|....*....|....*....
gi 1713980362 166 VLATETAPFGVRVMVVEPSGFATDWAGSS 194
Cdd:PRK08177  160 SFVAELGEPTLTVLSMHPGWVKTDMGGDN 188
PRK07791 PRK07791
short chain dehydrogenase; Provisional
1-184 1.35e-09

short chain dehydrogenase; Provisional


Pssm-ID: 236099 [Multi-domain]  Cd Length: 286  Bit Score: 57.76  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVV------------ATARRPEALAADLAEYGDRVLPLALDVTSPDAAR 68
Cdd:PRK07791    1 MGLLDGRVVIVTGAGGGIGRAHALAFAAEGARVVvndigvgldgsaSGGSAAQAVVDEIVAAGGEAVANGDDIADWDGAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  69 AAVEAAVARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLR------RQGAGTVVQFSSiGG 142
Cdd:PRK07791   81 NLVDAAVETFGGLDVLVNNAGILRDRMIANMSEEEWDAVIAVHLKGHFATLRHAAAYWRaeskagRAVDARIINTSS-GA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1713980362 143 RVGGSPGIASYQAAKFAVDGFSRVLATETAPFGVRVMVVEPS 184
Cdd:PRK07791  160 GLQGSVGQGNYSAAKAGIAALTLVAAAELGRYGVTVNAIAPA 201
PRK09186 PRK09186
flagellin modification protein A; Provisional
7-185 1.49e-09

flagellin modification protein A; Provisional


Pssm-ID: 236399 [Multi-domain]  Cd Length: 256  Bit Score: 57.31  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVAT---ARRPEALAADLA-EYGDRVLPL-ALDVTSPDAARAAVEAAVARFGRI 81
Cdd:PRK09186    5 KTILITGAGGLIGSALVKAILEAGGIVIAAdidKEALNELLESLGkEFKSKKLSLvELDITDQESLEEFLSKSAEKYGKI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNA-----GYANVspIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVG-------GSPG 149
Cdd:PRK09186   85 DGAVNCAyprnkDYGKK--FFDVSLDDFNENLSLHLGSSFLFSQQFAKYFKKQGGGNLVNISSIYGVVApkfeiyeGTSM 162
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1713980362 150 IAS--YQAAKFAVDGFSRVLATETAPFGVRVMVVEPSG 185
Cdd:PRK09186  163 TSPveYAAIKAGIIHLTKYLAKYFKDSNIRVNCVSPGG 200
PRK06924 PRK06924
(S)-benzoin forming benzil reductase;
11-189 4.14e-09

(S)-benzoin forming benzil reductase;


Pssm-ID: 180753 [Multi-domain]  Cd Length: 251  Bit Score: 55.85  E-value: 4.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE-YGDRVLPLALDVTSpdaARAAVEAAVARFGRIDV------ 83
Cdd:PRK06924    6 ITGTSQGLGEAIANQLLEKGTHVISISRTENKELTKLAEqYNSNLTFHSLDLQD---VHELETNFNEILSSIQEdnvssi 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 -LVNNAGYanVSPIETTEDADfRAQFETNfwgvYHVTRAAlPVL----------RRQGAGTVVQFSSiGGRVGGSPGIAS 152
Cdd:PRK06924   83 hLINNAGM--VAPIKPIEKAE-SEELITN----VHLNLLA-PMIltstfmkhtkDWKVDKRVINISS-GAAKNPYFGWSA 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1713980362 153 YQAAKFAVDGFSRVLATETA--PFGVRVMVVEPSGFATD 189
Cdd:PRK06924  154 YCSSKAGLDMFTQTVATEQEeeEYPVKIVAFSPGVMDTN 192
PRK08945 PRK08945
putative oxoacyl-(acyl carrier protein) reductase; Provisional
11-185 4.49e-09

putative oxoacyl-(acyl carrier protein) reductase; Provisional


Pssm-ID: 236357 [Multi-domain]  Cd Length: 247  Bit Score: 55.65  E-value: 4.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVV---ATARRPEALAADLAEYGDR---VLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK08945   17 VTGAGDGIGREAALTYARHGATVIllgRTEEKLEAVYDEIEAAGGPqpaIIPLDLLTATPQNYQQLADTIEEQFGRLDGV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAG-YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSpGIASYQAAKFAVDGF 163
Cdd:PRK08945   97 LHNAGlLGELGPMEQQDPEVWQDVMQVNVNATFMLTQALLPLLLKSPAASLVFTSSSVGRQGRA-NWGAYAVSKFATEGM 175
                         170       180
                  ....*....|....*....|..
gi 1713980362 164 SRVLATETAPFGVRVMVVEPSG 185
Cdd:PRK08945  176 MQVLADEYQGTNLRVNCINPGG 197
3alpha_HSD_SDR_c cd05328
alpha hydroxysteroid dehydrogenase (3alpha_HSD), classical (c) SDRs; Bacterial 3-alpha_HSD, ...
11-213 4.78e-09

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


Pssm-ID: 187589 [Multi-domain]  Cd Length: 250  Bit Score: 55.96  E-value: 4.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLAlDVTSpdaaraaveaavARFGRIDVLVNNAGy 90
Cdd:cd05328     4 ITGAASGIGAATAELLEDAGHTVIGIDLREADVIADLSTPEGRAAAIA-DVLA------------RCSGVLDGLVNCAG- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 anVSPIETTEDAdfraqFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGG--------------------------RV 144
Cdd:cd05328    70 --VGGTTVAGLV-----LKVNYFGLRALMEALLPRLRKGHGPAAVVVSSIAGagwaqdklelakalaagtearavalaEH 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362 145 GGSPGIASYQAAKFAVDGFSRVLA-TETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDATVGAMNR 213
Cdd:cd05328   143 AGQPGYLAYAGSKEALTVWTRRRAaTWLYGAGVRVNTVAPGPVETPILQAFLQDPRGGESVDAFVTPMGR 212
PRK12746 PRK12746
SDR family oxidoreductase;
1-189 5.73e-09

SDR family oxidoreductase;


Pssm-ID: 183718 [Multi-domain]  Cd Length: 254  Bit Score: 55.81  E-value: 5.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALA----ADLAEYGDRVLPLALDVTSPDAARAAVEAAVA 76
Cdd:PRK12746    1 MKNLDGKVALVTGASRGIGRAIAMRLANDGALVAIHYGRNKQAAdetiREIESNGGKAFLIEADLNSIDGVKKLVEQLKN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  77 RF------GRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQgaGTVVQFSSIGGRVGGSPGI 150
Cdd:PRK12746   81 ELqirvgtSEIDILVNNAGIGTQGTIENTTEEIFDEIMAVNIKAPFFLIQQTLPLLRAE--GRVINISSAEVRLGFTGSI 158
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1713980362 151 AsYQAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATD 189
Cdd:PRK12746  159 A-YGLSKGALNTMTLPLAKHLGERGITVNTIMPGYTKTD 196
WcaG COG0451
Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis];
10-186 1.12e-08

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


Pssm-ID: 440220 [Multi-domain]  Cd Length: 295  Bit Score: 54.98  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEAlAADLAEYgDRVLPLALDVTSPDaaraaveAAVARFGRIDVLVNNAG 89
Cdd:COG0451     3 LVTGGAGFIGSHLARRLLARGHEVVGLDRSPPG-AANLAAL-PGVEFVRGDLRDPE-------ALAAALAGVDAVVHLAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 YANVSPiettedADFRAQFETNFWGVYHVTRAAlpvlRRQGAGTVVQFSSIG--GRVGG-----SP--GIASYQAAKFAV 160
Cdd:COG0451    74 PAGVGE------EDPDETLEVNVEGTLNLLEAA----RAAGVKRFVYASSSSvyGDGEGpidedTPlrPVSPYGASKLAA 143
                         170       180
                  ....*....|....*....|....*.
gi 1713980362 161 DgfsRVLATETAPFGVRVMVVEPSGF 186
Cdd:COG0451   144 E---LLARAYARRYGLPVTILRPGNV 166
KR_2_SDR_x cd08953
ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain ...
8-165 2.22e-08

ketoreductase (KR), subgroup 2, complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. This subfamily includes both KR domains of the Bacillus subtilis Pks J,-L, and PksM, and all three KR domains of PksN, components of the megacomplex bacillaene synthase, which synthesizes the antibiotic bacillaene. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187656 [Multi-domain]  Cd Length: 436  Bit Score: 54.68  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   8 VWFITGSSRGFGRALVDAVLAAGDL-VVATARRPEALAAD--------LAEYGDRVLPLALDVTSPDAARAAVEAAVARF 78
Cdd:cd08953   207 VYLVTGGAGGIGRALARALARRYGArLVLLGRSPLPPEEEwkaqtlaaLEALGARVLYISADVTDAAAVRRLLEKVRERY 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  79 GRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAalpvLRRQGAGTVVQFSSIGGRVGGsPGIASYQAAKF 158
Cdd:cd08953   287 GAIDGVIHAAGVLRDALLAQKTAEDFEAVLAPKVDGLLNLAQA----LADEPLDFFVLFSSVSAFFGG-AGQADYAAANA 361

                  ....*..
gi 1713980362 159 AVDGFSR 165
Cdd:cd08953   362 FLDAFAA 368
A3DFK9-like_SDR_c cd09761
Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, ...
7-183 4.57e-08

Clostridium thermocellum A3DFK9-like, a putative carbohydrate or polyalcohol metabolizing SDR, classical (c) SDRs; This subgroup includes a putative carbohydrate or polyalcohol metabolizing SDR (A3DFK9) from Clostridium thermocellum. Its members have a TGXXXGXG classical-SDR glycine-rich NAD-binding motif, and some have a canonical SDR active site tetrad (A3DFK9 lacks the upstream Asn). SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187662 [Multi-domain]  Cd Length: 242  Bit Score: 52.97  E-value: 4.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVaTARRPEALAADLAEY-GDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:cd09761     2 KVAIVTGGGHGIGKQICLDFLEAGDKVV-FADIDEERGADFAEAeGPNLFFVHGDVADETLVKFVVYAMLEKLGRIDVLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIggRVGGS-PGIASYQAAKFAVDGFS 164
Cdd:cd09761    81 NNAARGSKGILSSLLLEEWDRILSVNLTGPYELSRYCRDELIKNK-GRIINIAST--RAFQSePDSEAYAASKGGLVALT 157
                         170
                  ....*....|....*....
gi 1713980362 165 RVLATETAPFgVRVMVVEP 183
Cdd:cd09761   158 HALAMSLGPD-IRVNCISP 175
DHPR_SDR_c_like cd05334
dihydropteridine reductase (DHPR), classical (c) SDRs; Dihydropteridine reductase is an ...
11-184 5.60e-08

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


Pssm-ID: 187595 [Multi-domain]  Cd Length: 221  Bit Score: 52.33  E-value: 5.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARR-PEALAADLAeygdrVLPLALDVTSPDAARAAVEAAvarFGRIDVLVNNAG 89
Cdd:cd05334     6 VYGGRGALGSAVVQAFKSRGWWVASIDLAeNEEADASII-----VLDSDSFTEQAKQVVASVARL---SGKVDALICVAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 -YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRrqGAGTVVqFSSIGGRVGGSPGIASYQAAKFAVDGFSRVLA 168
Cdd:cd05334    78 gWAGGSAKSKSFVKNWDLMWKQNLWTSFIASHLATKHLL--SGGLLV-LTGAKAALEPTPGMIGYGAAKAAVHQLTQSLA 154
                         170
                  ....*....|....*...
gi 1713980362 169 TET--APFGVRVMVVEPS 184
Cdd:cd05334   155 AENsgLPAGSTANAILPV 172
PRK05875 PRK05875
short chain dehydrogenase; Provisional
9-206 7.24e-08

short chain dehydrogenase; Provisional


Pssm-ID: 180300 [Multi-domain]  Cd Length: 276  Bit Score: 52.50  E-value: 7.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   9 WFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDR-----VLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:PRK05875   10 YLVTGGGSGIGKGVAAGLVAAGAAVMIVGRNPDKLAAAAEEIEALkgagaVRYEPADVTDEDQVARAVDAATAWHGRLHG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYA-NVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDG 162
Cdd:PRK05875   90 VVHCAGGSeTIGPITQIDSDAWRRTVDLNVNGTMYVLKHAARELVRGGGGSFVGISSIAAS-NTHRWFGAYGVTKSAVDH 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1713980362 163 FSRVLATETAPFGVRVMVVEPSGFATDWAGSSMTVHDVPEAYDA 206
Cdd:PRK05875  169 LMKLAADELGPSWVRVNSIRPGLIRTDLVAPITESPELSADYRA 212
PRK06197 PRK06197
short chain dehydrogenase; Provisional
4-146 2.76e-07

short chain dehydrogenase; Provisional


Pssm-ID: 235737 [Multi-domain]  Cd Length: 306  Bit Score: 50.79  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   4 QDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARRPE----ALAADLAEYGDRVLPL-ALDVTSPDAARAAVEAAVARF 78
Cdd:PRK06197   14 QSGRVAVVTGANTGLGYETAAALAAKGAHVVLAVRNLDkgkaAAARITAATPGADVTLqELDLTSLASVRAAADALRAAY 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1713980362  79 GRIDVLVNNAGYAnVSPIETTEDAdFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGG 146
Cdd:PRK06197   94 PRIDLLINNAGVM-YTPKQTTADG-FELQFGTNHLGHFALTGLLLDRLLPVPGSRVVTVSSGGHRIRA 159
Lin1944_like_SDR_c cd11731
Lin1944 and related proteins, classical (c) SDRs; Lin1944 protein from Listeria Innocua is a ...
13-190 5.98e-07

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


Pssm-ID: 212497 [Multi-domain]  Cd Length: 198  Bit Score: 49.12  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  13 GSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEyGDRVLPLALDVtspdaaraaveaavarfGRIDVLVNNAGYAN 92
Cdd:cd11731     5 GATGTIGLAVAQLLSAHGHEVITAGRSSGDYQVDITD-EASIKALFEKV-----------------GHFDAIVSTAGDAE 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  93 VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgtvvqFSSIGGRVGGSP--GIASYQAAKFAVDGFSRVLATE 170
Cdd:cd11731    67 FAPLAELTDADFQRGLNSKLLGQINLVRHGLPYLNDGGS-----ITLTSGILAQRPipGGAAAATVNGALEGFVRAAAIE 141
                         170       180
                  ....*....|....*....|
gi 1713980362 171 TaPFGVRVMVVEPSGFATDW 190
Cdd:cd11731   142 L-PRGIRINAVSPGVVEESL 160
fabG PRK07792
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-214 7.21e-07

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


Pssm-ID: 181120 [Multi-domain]  Cd Length: 306  Bit Score: 49.78  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVV----ATARRPEALAADLAEYGDRVLPLALDVtSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK07792   17 VTGAAAGLGRAEALGLARLGATVVvndvASALDASDVLDEIRAAGAKAVAVAGDI-SQRATADELVATAVGLGGLDIVVN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLR---RQGAGTV----VQFSSIGGRVgGSPGIASYQAAKFA 159
Cdd:PRK07792   96 NAGITRDRMLFNMSDEEWDAVIAVHLRGHFLLTRNAAAYWRakaKAAGGPVygriVNTSSEAGLV-GPVGQANYGAAKAG 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1713980362 160 VDGFSRVLATETAPFGVRVMVVEPSgfatdwAGSSMTVHDVPEAYDATVGAMNRL 214
Cdd:PRK07792  175 ITALTLSAARALGRYGVRANAICPR------ARTAMTADVFGDAPDVEAGGIDPL 223
PRK12747 PRK12747
short chain dehydrogenase; Provisional
7-214 9.21e-07

short chain dehydrogenase; Provisional


Pssm-ID: 183719 [Multi-domain]  Cd Length: 252  Bit Score: 48.92  E-value: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVA--TARRPEA--LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARF---- 78
Cdd:PRK12747    5 KVALVTGASRGIGRAIAKRLANDGALVAIhyGNRKEEAeeTVYEIQSNGGSAFSIGANLESLHGVEALYSSLDNELqnrt 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  79 --GRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQgaGTVVQFSSIGGRVgGSPGIASYQAA 156
Cdd:PRK12747   85 gsTKFDILINNAGIGPGAFIEETTEQFFDRMVSVNAKAPFFIIQQALSRLRDN--SRIINISSAATRI-SLPDFIAYSMT 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1713980362 157 KFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwAGSSMTVHDVPEAYDATVGAMNRL 214
Cdd:PRK12747  162 KGAINTMTFTLAKQLGARGITVNAILPGFIKTD-MNAELLSDPMMKQYATTISAFNRL 218
PRK08416 PRK08416
enoyl-ACP reductase;
10-223 9.29e-07

enoyl-ACP reductase;


Pssm-ID: 181417 [Multi-domain]  Cd Length: 260  Bit Score: 49.00  E-value: 9.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAE-----YGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVL 84
Cdd:PRK08416   12 VISGGTRGIGKAIVYEFAQSGVNIAFTYNSNVEEANKIAEdleqkYGIKAKAYPLNILEPETYKELFKKIDEDFDRVDFF 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNA---GYANVSPIettedADFRAQFETNFWGVYHVTRAALPV--------LRRQGAGTVVQFSSIGGRVgGSPGIASY 153
Cdd:PRK08416   92 ISNAiisGRAVVGGY-----TKFMRLKPKGLNNIYTATVNAFVVgaqeaakrMEKVGGGSIISLSSTGNLV-YIENYAGH 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1713980362 154 QAAKFAVDGFSRVLATETAPFGVRVMVVEPSGFATDwAGSSMTVHDVPEAYDATVGAMNRLMR-QNTAGAA 223
Cdd:PRK08416  166 GTSKAAVETMVKYAATELGEKNIRVNAVSGGPIDTD-ALKAFTNYEEVKAKTEELSPLNRMGQpEDLAGAC 235
fabG PRK08261
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
11-186 9.33e-07

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


Pssm-ID: 236207 [Multi-domain]  Cd Length: 450  Bit Score: 49.83  E-value: 9.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDaVLAA-GDLVVAtARRPEAlAADLAEYGDRV--LPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08261  215 VTGAARGIGAAIAE-VLARdGAHVVC-LDVPAA-GEALAAVANRVggTALALDITAPDAPARIAEHLAERHGGLDIVVHN 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AG------YANVSPiettedADFRAQFETNFWGVYHVTRAALP--VLRRQGAgtVVQFSSIGGrVGGSPGIASYQAAKFA 159
Cdd:PRK08261  292 AGitrdktLANMDE------ARWDSVLAVNLLAPLRITEALLAagALGDGGR--IVGVSSISG-IAGNRGQTNYAASKAG 362
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 160 VDGFSRVLATETAPFGVRVMVVEPsGF 186
Cdd:PRK08261  363 VIGLVQALAPLLAERGITINAVAP-GF 388
pter_reduc_Leis TIGR02685
pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including ...
11-183 9.59e-07

pteridine reductase; Pteridine reductase is an enzyme used by trypanosomatids (including Trypanosoma cruzi and Leishmania major) to obtain reduced pteridines by salvage rather than biosynthetic pathways. Enzymes in T. cruzi described as pteridine reductase 1 (PTR1) and pteridine reductase 2 (PTR2) have different activity profiles. PTR1 is more active with with fully oxidized biopterin and folate than with reduced forms, while PTR2 reduces dihydrobiopterin and dihydrofolate but not oxidized pteridines. T. cruzi PTR1 and PTR2 are more similar to each other in sequence than either is to the pteridine reductase of Leishmania major, and all are included in this family.


Pssm-ID: 131732 [Multi-domain]  Cd Length: 267  Bit Score: 49.16  E-value: 9.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLP---------LALDVTSPDAARAAVEAAVARFGRI 81
Cdd:TIGR02685   6 VTGAAKRIGSSIAVALHQEGYRVVLHYHRSAAAASTLAAELNARRPnsavtcqadLSNSATLFSRCEAIIDACFRAFGRC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVSPIETTEDADFRAQ-----------FETNFWGVYHVTRAalpVLRRQGAGTVVQFSSIGGRVG----- 145
Cdd:TIGR02685  86 DVLVNNASAFYPTPLLRGDAGEGVGDkkslevqvaelFGSNAIAPYFLIKA---FAQRQAGTRAEQRSTNLSIVNlcdam 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1713980362 146 ---GSPGIASYQAAKFAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:TIGR02685 163 tdqPLLGFTMYTMAKHALEGLTRSAALELAPLQIRVNGVAP 203
KR pfam08659
KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the ...
11-165 1.23e-06

KR domain; This enzymatic domain is part of bacterial polyketide synthases and catalyzes the first step in the reductive modification of the beta-carbonyl centres in the growing polyketide chain. It uses NADPH to reduce the keto group to a hydroxy group.


Pssm-ID: 430138 [Multi-domain]  Cd Length: 180  Bit Score: 47.94  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG-DLVVATARRP------EALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDV 83
Cdd:pfam08659   5 ITGGLGGLGRELARWLAERGaRHLVLLSRSAaprpdaQALIAELEARGVEVVVVACDVSDPDAVAALLAEIKAEGPPIRG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  84 LVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAalpvLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGF 163
Cdd:pfam08659  85 VIHAAGVLRDALLENMTDEDWRRVLAPKVTGTWNLHEA----TPDEPLDFFVLFSSIAG-LLGSPGQANYAAANAFLDAL 159

                  ..
gi 1713980362 164 SR 165
Cdd:pfam08659 160 AE 161
PRK06101 PRK06101
SDR family oxidoreductase;
10-188 1.42e-06

SDR family oxidoreductase;


Pssm-ID: 180399 [Multi-domain]  Cd Length: 240  Bit Score: 48.33  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITGSSRGFGRALVDAVLAAGDLVVATARRPEALaADLAEYGDRVLPLALDVTspDAARAAVEAAVARFgRIDVLVNNAG 89
Cdd:PRK06101    5 LITGATSGIGKQLALDYAKQGWQVIACGRNQSVL-DELHTQSANIFTLAFDVT--DHPGTKAALSQLPF-IPELWIFNAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  90 yanvsPIETTEDADFRAQ-----FETNFWGVYHVTRAALPVLRRqgAGTVVQFSSIGGRVgGSPGIASYQAAKFAVDGFS 164
Cdd:PRK06101   81 -----DCEYMDDGKVDATlmarvFNVNVLGVANCIEGIQPHLSC--GHRVVIVGSIASEL-ALPRAEAYGASKAAVAYFA 152
                         170       180
                  ....*....|....*....|....
gi 1713980362 165 RVLATETAPFGVRVMVVEPSGFAT 188
Cdd:PRK06101  153 RTLQLDLRPKGIEVVTVFPGFVAT 176
DHRS-12_like_SDR_c-like cd09808
human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like ...
7-162 1.92e-06

human dehydrogenase/reductase SDR family member (DHRS)-12/FLJ13639-like, classical (c)-like SDRs; Classical SDR-like subgroup containing human DHRS-12/FLJ13639, the 36K protein of zebrafish CNS myelin, and related proteins. DHRS-12/FLJ13639 is expressed in neurons and oligodendrocytes in the human cerebral cortex. Proteins in this subgroup share the glycine-rich NAD-binding motif of the classical SDRs, have a partial match to the canonical active site tetrad, but lack the typical active site Ser. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187668 [Multi-domain]  Cd Length: 255  Bit Score: 47.97  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARR----PEALAADLAEYGDR-VLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:cd09808     2 RSFLITGANSGIGKAAALAIAKRGGTVHMVCRNqtraEEARKEIETESGNQnIFLHIVDMSDPKQVWEFVEEFKEEGKKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGyANVSPIETTEDAdFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSiGGRVGGSPGIASYQAAKFAVD 161
Cdd:cd09808    82 HVLINNAG-CMVNKRELTEDG-LEKNFATNTLGTYILTTHLIPVLEKEEDPRVITVSS-GGMLVQKLNTNNLQSERTAFD 158

                  .
gi 1713980362 162 G 162
Cdd:cd09808   159 G 159
PRK05717 PRK05717
SDR family oxidoreductase;
7-183 4.49e-06

SDR family oxidoreductase;


Pssm-ID: 168204 [Multi-domain]  Cd Length: 255  Bit Score: 46.81  E-value: 4.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:PRK05717   11 RVALVTGAARGIGLGIAAWLIAEGWQVVLADLDRERGSKVAKALGENAWFIAMDVADEAQVAAGVAEVLGQFGRLDALVC 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYANV--SPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGaGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFS 164
Cdd:PRK05717   91 NAAIADPhnTTLESLSLAHWNRVLAVNLTGPMLLAKHCAPYLRAHN-GAIVNLASTRAR-QSEPDTEAYAASKGGLLALT 168
                         170
                  ....*....|....*....
gi 1713980362 165 RVLATETAPfGVRVMVVEP 183
Cdd:PRK05717  169 HALAISLGP-EIRVNAVSP 186
PRK07023 PRK07023
SDR family oxidoreductase;
11-183 5.44e-06

SDR family oxidoreductase;


Pssm-ID: 180796 [Multi-domain]  Cd Length: 243  Bit Score: 46.54  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAAdlAEYGDRVLPLALDVTSPDAARA-AVEAAVARFGR---IDVLVN 86
Cdd:PRK07023    6 VTGHSRGLGAALAEQLLQPGIAVLGVARSRHPSLA--AAAGERLAEVELDLSDAAAAAAwLAGDLLAAFVDgasRVLLIN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  87 NAGYAN-VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRvGGSPGIASYQAAKFAVDGFSR 165
Cdd:PRK07023   84 NAGTVEpIGPLATLDAAAIARAVGLNVAAPLMLTAALAQAASDAAERRILHISSGAAR-NAYAGWSVYCATKAALDHHAR 162
                         170
                  ....*....|....*...
gi 1713980362 166 VLATEtAPFGVRVMVVEP 183
Cdd:PRK07023  163 AVALD-ANRALRIVSLAP 179
PRK12744 PRK12744
SDR family oxidoreductase;
35-183 6.16e-06

SDR family oxidoreductase;


Pssm-ID: 183716 [Multi-domain]  Cd Length: 257  Bit Score: 46.66  E-value: 6.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  35 ATARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWG 114
Cdd:PRK12744   44 ASKADAEETVAAVKAAGAKAVAFQADLTTAAAVEKLFDDAKAAFGRPDIAINTVGKVLKKPIVEISEAEYDEMFAVNSKS 123
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 115 VYHVTRAALPVLRRQGAGTVVQFSSIGGRvggSPGIASYQAAKFAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK12744  124 AFFFIKEAGRHLNDNGKIVTLVTSLLGAF---TPFYSAYAGSKAPVEHFTRAASKEFGARGISVTAVGP 189
PRK07806 PRK07806
SDR family oxidoreductase;
1-88 1.29e-05

SDR family oxidoreductase;


Pssm-ID: 181126 [Multi-domain]  Cd Length: 248  Bit Score: 45.48  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGrALVDAVLAAGDLVVAT-----ARRPEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAV 75
Cdd:PRK07806    1 MGDLPGKTALVTGSSRGIG-ADTAKILAGAGAHVVVnyrqkAPRANKVVAEIEAAGGRASAVGADLTDEESVAALMDTAR 79
                          90
                  ....*....|...
gi 1713980362  76 ARFGRIDVLVNNA 88
Cdd:PRK07806   80 EEFGGLDALVLNA 92
PRK05854 PRK05854
SDR family oxidoreductase;
11-167 1.75e-05

SDR family oxidoreductase;


Pssm-ID: 235627 [Multi-domain]  Cd Length: 313  Bit Score: 45.44  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAEY-----GDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLV 85
Cdd:PRK05854   19 VTGASDGLGLGLARRLAAAGAEVILPVRNRAKGEAAVAAIrtavpDAKLSLRALDLSSLASVAALGEQLRAEGRPIHLLI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  86 NNAGYANVSPIETTEDAdFRAQFETNFWGVYHVTRAALPVLrRQGAGTVVQFSSIGGRVG-----------GSPGIASYQ 154
Cdd:PRK05854   99 NNAGVMTPPERQTTADG-FELQFGTNHLGHFALTAHLLPLL-RAGRARVTSQSSIAARRGainwddlnwerSYAGMRAYS 176
                         170
                  ....*....|...
gi 1713980362 155 AAKFAVDGFSRVL 167
Cdd:PRK05854  177 QSKIAVGLFALEL 189
retinol-DH_like_SDR_c cd09807
retinol dehydrogenases (retinol-DHs), classical (c) SDRs; Classical SDR-like subgroup ...
7-183 3.35e-05

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


Pssm-ID: 212495 [Multi-domain]  Cd Length: 274  Bit Score: 44.38  E-value: 3.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   7 QVWFITGSSRGFGRALVDAVLAAGDLVVATAR---RPEALAADL-AEYGDR-VLPLALDVTSPDAARAAVEAAVARFGRI 81
Cdd:cd09807     2 KTVIITGANTGIGKETARELARRGARVIMACRdmaKCEEAAAEIrRDTLNHeVIVRHLDLASLKSIRAFAAEFLAEEDRL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYANVsPIETTEDAdFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGSP-----------GI 150
Cdd:cd09807    82 DVLINNAGVMRC-PYSKTEDG-FEMQFGVNHLGHFLLTNLLLDLLKKSAPSRIVNVSSLAHKAGKINfddlnseksynTG 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1713980362 151 ASYQAAKFAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:cd09807   160 FAYCQSKLANVLFTRELARRLQGTGVTVNALHP 192
UDP_G4E_4_SDR_e cd05232
UDP-glucose 4 epimerase, subgroup 4, extended (e) SDRs; UDP-glucose 4 epimerase (aka ...
11-152 3.38e-05

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: 44.65  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSrGF-GRALVDAVLAAGDLVVATARRPEALAADLaeygdrVLPLALDVTSPDaaraaveaavARFGRIDVLVNNAG 89
Cdd:cd05232     4 VTGAN-GFiGRALVDKLLSRGEEVRIAVRNAENAEPSV------VLAELPDIDSFT----------DLFLGVDAVVHLAA 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1713980362  90 YANV-SPIETTEDADFRaqfETNFWGVYHVTRAAlpvlRRQGAGTVVQFSSIggRVGGSPGIAS 152
Cdd:cd05232    67 RVHVmNDQGADPLSDYR---KVNTELTRRLARAA----ARQGVKRFVFLSSV--KVNGEGTVGA 121
PRK08415 PRK08415
enoyl-[acyl-carrier-protein] reductase FabI;
35-178 4.38e-05

enoyl-[acyl-carrier-protein] reductase FabI;


Pssm-ID: 181416 [Multi-domain]  Cd Length: 274  Bit Score: 43.96  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  35 ATARRPEALAADLAEygDRVLPLalDVTSPDAARAAVEAAVARFGRIDVLVNNAGYA-----NVSPIETTEDAdFRAQFE 109
Cdd:PRK08415   42 ALKKRVEPIAQELGS--DYVYEL--DVSKPEHFKSLAESLKKDLGKIDFIVHSVAFApkealEGSFLETSKEA-FNIAME 116
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1713980362 110 TNFWGVYHVTRAALPVLRRQGAgtVVQFSSIggrvGGSPGIASYQ---AAKFAVDGFSRVLATETAPFGVRV 178
Cdd:PRK08415  117 ISVYSLIELTRALLPLLNDGAS--VLTLSYL----GGVKYVPHYNvmgVAKAALESSVRYLAVDLGKKGIRV 182
PRK07904 PRK07904
decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;
126-183 6.88e-05

decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase;


Pssm-ID: 181162 [Multi-domain]  Cd Length: 253  Bit Score: 43.54  E-value: 6.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362 126 LRRQGAGTVVQFSSIGG-RVGGSPGIasYQAAKFAVDGFSRVLATETAPFGVRVMVVEP 183
Cdd:PRK07904  133 MRAQGFGQIIAMSSVAGeRVRRSNFV--YGSTKAGLDGFYLGLGEALREYGVRVLVVRP 189
PRK08703 PRK08703
SDR family oxidoreductase;
1-183 8.04e-05

SDR family oxidoreductase;


Pssm-ID: 169556 [Multi-domain]  Cd Length: 239  Bit Score: 43.00  E-value: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATAR---RPEALAADLAEYGD---RVLPLALDVTSPDAARAAVEAA 74
Cdd:PRK08703    1 MATLSDKTILVTGASQGLGEQVAKAYAAAGATVILVARhqkKLEKVYDAIVEAGHpepFAIRFDLMSAEEKEFEQFAATI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  75 VARF-GRIDVLVNNAGY-ANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIAS 152
Cdd:PRK08703   81 AEATqGKLDGIVHCAGYfYALSPLDFQTVAEWVNQYRINTVAPMGLTRALFPLLKQSPDASVIFVGESHG-ETPKAYWGG 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1713980362 153 YQAAKFAVDGFSRVLATETAPFG-VRVMVVEP 183
Cdd:PRK08703  160 FGASKAALNYLCKVAADEWERFGnLRANVLVP 191
PRK09134 PRK09134
SDR family oxidoreductase;
1-88 1.05e-04

SDR family oxidoreductase;


Pssm-ID: 236389 [Multi-domain]  Cd Length: 258  Bit Score: 42.99  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   1 MSTQDPQVWFITGSSRGFGRALVDAVLAAGDLVVATARR----PEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVA 76
Cdd:PRK09134    4 MSMAAPRAALVTGAARRIGRAIALDLAAHGFDVAVHYNRsrdeAEALAAEIRALGRRAVALQADLADEAEVRALVARASA 83
                          90
                  ....*....|..
gi 1713980362  77 RFGRIDVLVNNA 88
Cdd:PRK09134   84 ALGPITLLVNNA 95
Epimerase pfam01370
NAD dependent epimerase/dehydratase family; This family of proteins utilize NAD as a cofactor. ...
9-184 1.31e-04

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: 42.28  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   9 WFITGSSrGF-GRALVDAVLAAGDLVVATARRPEALAADLAEYGDRVlplALDVTSPDAARAAVEAAvarfgRIDVLVNN 87
Cdd:pfam01370   1 ILVTGAT-GFiGSHLVRRLLEKGYEVIGLDRLTSASNTARLADLRFV---EGDLTDRDALEKLLADV-----RPDAVIHL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  88 AGYANVSpiETTEDADfrAQFETNFWGVYHVTRAAlpvlRRQGAGTVVQFSS--IGGRVGGSPGIAS-----------YQ 154
Cdd:pfam01370  72 AAVGGVG--ASIEDPE--DFIEANVLGTLNLLEAA----RKAGVKRFLFASSseVYGDGAEIPQEETtltgplapnspYA 143
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 155 AAKFAVDgfsRVLATETAPFGVRVMVVEPS 184
Cdd:pfam01370 144 AAKLAGE---WLVLAYAAAYGLRAVILRLF 170
PLN02780 PLN02780
ketoreductase/ oxidoreductase
11-191 2.53e-04

ketoreductase/ oxidoreductase


Pssm-ID: 166421 [Multi-domain]  Cd Length: 320  Bit Score: 41.78  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALA----ADLAEYGD-RVLPLALDVtSPDAARAAVEAAVARFG-RIDVL 84
Cdd:PLN02780   58 VTGPTDGIGKGFAFQLARKGLNLVLVARNPDKLKdvsdSIQSKYSKtQIKTVVVDF-SGDIDEGVKRIKETIEGlDVGVL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAG--YANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAGTVVQFSSIGGRVGGS-PGIASYQAAKFAVD 161
Cdd:PLN02780  137 INNVGvsYPYARFFHEVDEELLKNLIKVNVEGTTKVTQAVLPGMLKRKKGAIINIGSGAAIVIPSdPLYAVYAATKAYID 216
                         170       180       190
                  ....*....|....*....|....*....|
gi 1713980362 162 GFSRVLATETAPFGVRVMVVEPSGFATDWA 191
Cdd:PLN02780  217 QFSRCLYVEYKKSGIDVQCQVPLYVATKMA 246
PRK08340 PRK08340
SDR family oxidoreductase;
11-140 6.50e-04

SDR family oxidoreductase;


Pssm-ID: 169390 [Multi-domain]  Cd Length: 259  Bit Score: 40.56  E-value: 6.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEAL---AADLAEYGDrVLPLALDVTSPDAARAAVEAAVARFGRIDVLVNN 87
Cdd:PRK08340    5 VTASSRGIGFNVARELLKKGARVVISSRNEENLekaLKELKEYGE-VYAVKADLSDKDDLKNLVKEAWELLGGIDALVWN 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1713980362  88 AGYANVSPIeTTEDADFRAQFETNFWGV----YHVTRAALPVLRRQGAGTVVQFSSI 140
Cdd:PRK08340   84 AGNVRCEPC-MLHEAGYSDWLEAALLHLvapgYLTTLLIQAWLEKKMKGVLVYLSSV 139
dTDP_HR_like_SDR_e cd05254
dTDP-6-deoxy-L-lyxo-4-hexulose reductase and related proteins, extended (e) SDRs; ...
11-139 6.55e-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: 40.69  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALaadlaeygdrvlpLALDVTSPDAARAAVEAAvarfgRIDVLVNNAGY 90
Cdd:cd05254     4 ITGATGMLGRALVRLLKERGYEVIGTGRSRASL-------------FKLDLTDPDAVEEAIRDY-----KPDVIINCAAY 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1713980362  91 ANVSPIETTEDADFRAqfetNFWGVYHVTRAAlpvlRRQGAgTVVQFSS 139
Cdd:cd05254    66 TRVDKCESDPELAYRV----NVLAPENLARAA----KEVGA-RLIHIST 105
YbjT COG0702
Uncharacterized conserved protein YbjT, contains NAD(P)-binding and DUF2867 domains [General ...
11-193 9.28e-04

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: 39.83  E-value: 9.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARRPEALAADLAeygDRVLPLALDVTSPDaaraaveAAVARFGRIDVLVnnagy 90
Cdd:COG0702     4 VTGATGFIGRRVVRALLARGHPVRALVRDPEKAAALAA---AGVEVVQGDLDDPE-------SLAAALAGVDAVF----- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  91 aNVSPIETTEDADFRAQFETNFwgvyhvTRAAlpvlRRQGAGTVVQFSSIG-GRVGGSPgiasYQAAKFAVDgfsRVLAT 169
Cdd:COG0702    69 -LLVPSGPGGDFAVDVEGARNL------ADAA----KAAGVKRIVYLSALGaDRDSPSP----YLRAKAAVE---EALRA 130
                         170       180
                  ....*....|....*....|....
gi 1713980362 170 EtapfGVRVMVVEPSGFATDWAGS 193
Cdd:COG0702   131 S----GLPYTILRPGWFMGNLLGF 150
KR_FAS_SDR_x cd05274
ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of ...
11-209 9.94e-04

ketoreductase (KR) and fatty acid synthase (FAS), complex (x) SDRs; Ketoreductase, a module of the multidomain polyketide synthase (PKS), has 2 subdomains, each corresponding to a SDR family monomer. The C-terminal subdomain catalyzes the NADPH-dependent reduction of the beta-carbonyl of a polyketide to a hydroxyl group, a step in the biosynthesis of polyketides, such as erythromycin. The N-terminal subdomain, an interdomain linker, is a truncated Rossmann fold which acts to stabilizes the catalytic subdomain. Unlike typical SDRs, the isolated domain does not oligomerize but is composed of 2 subdomains, each resembling an SDR monomer. The active site resembles that of typical SDRs, except that the usual positions of the catalytic Asn and Tyr are swapped, so that the canonical YXXXK motif changes to YXXXN. Modular PKSs are multifunctional structures in which the makeup recapitulates that found in (and may have evolved from) FAS. In some instances, such as porcine FAS, an enoyl reductase (ER) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consist of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthase uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-KR, forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-ER. Polyketide synthesis also proceeds via the addition of 2-carbon units as in fatty acid synthesis. The complex SDR NADP-binding motif, GGXGXXG, is often present, but is not strictly conserved in each instance of the module. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187582 [Multi-domain]  Cd Length: 375  Bit Score: 40.06  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAG--DLVVATARRPEA----LAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGrIDVL 84
Cdd:cd05274   155 ITGGLGGLGLLVARWLAARGarHLVLLSRRGPAPraaaRAALLRAGGARVSVVRCDVTDPAALAALLAELAAGGP-LAGV 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  85 VNNAGYANVSPIETTEDADFRAQFETNfwgvYHVTRAALPVLRRQGAGTVVQFSSIGGrVGGSPGIASYQAAKFAVDGFS 164
Cdd:cd05274   234 IHAAGVLRDALLAELTPAAFAAVLAAK----VAGALNLHELTPDLPLDFFVLFSSVAA-LLGGAGQAAYAAANAFLDALA 308
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1713980362 165 RVLATEtapfGVRVMVVEPsgfaTDWAGSSMTVHDVPEAYDATVG 209
Cdd:cd05274   309 AQRRRR----GLPATSVQW----GAWAGGGMAAAAALRARLARSG 345
LPOR_like_SDR_c_like cd09810
light-dependent protochlorophyllide reductase (LPOR)-like, classical (c)-like SDRs; Classical ...
11-149 4.24e-03

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


Pssm-ID: 187670 [Multi-domain]  Cd Length: 311  Bit Score: 38.27  E-value: 4.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  11 ITGSSRGFGRALVDAVLAAGDLVVATARR----PEALAADLAEYGDRVLPLALDVTSPDAARAAVEAAVARFGRIDVLVN 86
Cdd:cd09810     6 ITGASSGLGLAAAKALARRGEWHVVMACRdflkAEQAAQEVGMPKDSYSVLHCDLASLDSVRQFVDNFRRTGRPLDALVC 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1713980362  87 NAGYANVSPIETTEDAD-FRAQFETNFWGVYHVTRAALPVLRRQGAGT--VVQFSSIGG---RVGGSPG 149
Cdd:cd09810    86 NAAVYLPTAKEPRFTADgFELTVGVNHLGHFLLTNLLLEDLQRSENASprIVIVGSITHnpnTLAGNVP 154
ENR_SDR cd05372
Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ...
10-178 4.46e-03

Enoyl acyl carrier protein (ACP) reductase (ENR), divergent SDR; This bacterial subgroup of ENRs includes Escherichia coli ENR. ENR catalyzes the NAD(P)H-dependent reduction of enoyl-ACP in the last step of fatty acid biosynthesis. De novo fatty acid biosynthesis is catalyzed by the fatty acid synthetase complex, through the serial addition of 2-carbon subunits. In bacteria and plants,ENR catalyzes one of six synthetic steps in this process. Oilseed rape ENR, and also apparently the NADH-specific form of Escherichia coli ENR, is tetrameric. Although similar to the classical SDRs, this group does not have the canonical catalytic tetrad, nor does it have the typical Gly-rich NAD-binding pattern. Such so-called divergent SDRs have a GXXXXXSXA NAD-binding motif and a YXXMXXXK (or YXXXMXXXK) active site motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187630 [Multi-domain]  Cd Length: 250  Bit Score: 37.95  E-value: 4.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  10 FITG----SSRGFGRALV----DAVLAAGDLVVATARRPEALAADLAEYgDRVLPLalDVTSPDAARAAVEAAVARFGRI 81
Cdd:cd05372     5 LITGiandRSIAWGIAKAlheaGAELAFTYQPEALRKRVEKLAERLGES-ALVLPC--DVSNDEEIKELFAEVKKDWGKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  82 DVLVNNAGYAN----VSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgtVVQFSSIGG-RVggSPGIASYQAA 156
Cdd:cd05372    82 DGLVHSIAFAPkvqlKGPFLDTSRKGFLKALDISAYSLVSLAKAALPIMNPGGS--IVTLSYLGSeRV--VPGYNVMGVA 157
                         170       180
                  ....*....|....*....|..
gi 1713980362 157 KFAVDGFSRVLATETAPFGVRV 178
Cdd:cd05372   158 KAALESSVRYLAYELGRKGIRV 179
PRK07578 PRK07578
short chain dehydrogenase; Provisional
79-212 8.66e-03

short chain dehydrogenase; Provisional


Pssm-ID: 236057 [Multi-domain]  Cd Length: 199  Bit Score: 36.71  E-value: 8.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  79 GRIDVLVNNAGYANVSPIETTEDADFRAQFETNFWGVYHVTRAALPVLRRQGAgtvvqFSSIGGRVGGSP--GIASYQAA 156
Cdd:PRK07578   54 GKVDAVVSAAGKVHFAPLAEMTDEDFNVGLQSKLMGQVNLVLIGQHYLNDGGS-----FTLTSGILSDEPipGGASAATV 128
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1713980362 157 KFAVDGFSRVLATEtAPFGVRVMVVEPSGFATDWAG--------SSMTVHDVPEAYDATV-GAMN 212
Cdd:PRK07578  129 NGALEGFVKAAALE-LPRGIRINVVSPTVLTESLEKygpffpgfEPVPAARVALAYVRSVeGAQT 192
SDR_a5 cd05243
atypical (a) SDRs, subgroup 5; This subgroup contains atypical SDRs, some of which are ...
9-193 9.16e-03

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: 36.44  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362   9 WFITGSSRGFGRALVDAVLAAGDLVVATARRPEAlAADLAEYGDRVlpLALDVTSPDAARAAVEAavarfgrIDVLVNNA 88
Cdd:cd05243     2 VLVVGATGKVGRHVVRELLDRGYQVRALVRDPSQ-AEKLEAAGAEV--VVGDLTDAESLAAALEG-------IDAVISAA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1713980362  89 GyANVSPIETTEDADfraqfetnFWGVYHVTRAAlpvlRRQGAGTVVQFSSIGG--RVGGSPGIASYQAAKFAVDgfsRV 166
Cdd:cd05243    72 G-SGGKGGPRTEAVD--------YDGNINLIDAA----KKAGVKRFVLVSSIGAdkPSHPLEALGPYLDAKRKAE---DY 135
                         170       180
                  ....*....|....*....|....*..
gi 1713980362 167 LATETAPFgvrvMVVEPSGFATDWAGS 193
Cdd:cd05243   136 LRASGLDY----TIVRPGGLTDDPAGT 158
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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