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Conserved domains on  [gi|495523457|ref|WP_008248102|]
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MULTISPECIES: NADP-dependent oxidoreductase [Zhongshania]

Protein Classification

MDR family NADP-dependent oxidoreductase( domain architecture ID 10143050)

NADP-dependent oxidoreductase belonging to the zinc-dependent medium chain dehydrogenase/reductase (MDR) family

EC:  1.-.-.-
Gene Ontology:  GO:0016628
SCOP:  3000040

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CurA super family cl34409
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
1-340 1.13e-131

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


The actual alignment was detected with superfamily member COG2130:

Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 378.63  E-value: 1.13e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   1 MANINRRYVLKERPRfQVPTAKCFRLEEEAAPEPGEGEFRIRTTWLGMDPNLFSKVKKVSDQARPIPIGAVMYGATVGRV 80
Cdd:COG2130    1 MMTTNRQIVLASRPE-GEPTPEDFRLEEVPVPEPGDGEVLVRNLYLSVDPYMRGRMSDAKSYAPPVELGEVMRGGAVGEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  81 DISNHPDFSVGDLVHGLWGWQDYFISNGAGIFSVDNDISRPSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGAL 160
Cdd:COG2130   80 VESRHPDFAVGDLVLGMLGWQDYAVSDGAGLRKVDPSLAPLSAYLGVLGMPGLTAYFGLLDIGKPKAGETVVVSAAAGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 161 GQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGG 240
Cdd:COG2130  160 GSVVGQIAKLKGCRVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAAACPDGIDVYFDNVGGEILDAVLPLLNTFA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 241 RIAVCGLMALYSMTQLPVTPdrsfMILNEILLKRLTVKGSMVLDMLntDRHVEFKREMKSWIAQGVVRPVEFITEGLENA 320
Cdd:COG2130  240 RIAVCGAISQYNATEPPPGP----RNLGQLLVKRLRMQGFIVFDHA--DRFPEFLAELAGWVAEGKLKYRETVVEGLENA 313
                        330       340
                 ....*....|....*....|
gi 495523457 321 PDALRAVFDGENIGKSVVHV 340
Cdd:COG2130  314 PEAFLGLFEGENFGKLLVKV 333
 
Name Accession Description Interval E-value
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
1-340 1.13e-131

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 378.63  E-value: 1.13e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   1 MANINRRYVLKERPRfQVPTAKCFRLEEEAAPEPGEGEFRIRTTWLGMDPNLFSKVKKVSDQARPIPIGAVMYGATVGRV 80
Cdd:COG2130    1 MMTTNRQIVLASRPE-GEPTPEDFRLEEVPVPEPGDGEVLVRNLYLSVDPYMRGRMSDAKSYAPPVELGEVMRGGAVGEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  81 DISNHPDFSVGDLVHGLWGWQDYFISNGAGIFSVDNDISRPSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGAL 160
Cdd:COG2130   80 VESRHPDFAVGDLVLGMLGWQDYAVSDGAGLRKVDPSLAPLSAYLGVLGMPGLTAYFGLLDIGKPKAGETVVVSAAAGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 161 GQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGG 240
Cdd:COG2130  160 GSVVGQIAKLKGCRVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAAACPDGIDVYFDNVGGEILDAVLPLLNTFA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 241 RIAVCGLMALYSMTQLPVTPdrsfMILNEILLKRLTVKGSMVLDMLntDRHVEFKREMKSWIAQGVVRPVEFITEGLENA 320
Cdd:COG2130  240 RIAVCGAISQYNATEPPPGP----RNLGQLLVKRLRMQGFIVFDHA--DRFPEFLAELAGWVAEGKLKYRETVVEGLENA 313
                        330       340
                 ....*....|....*....|
gi 495523457 321 PDALRAVFDGENIGKSVVHV 340
Cdd:COG2130  314 PEAFLGLFEGENFGKLLVKV 333
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
5-338 1.36e-99

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 297.09  E-value: 1.36e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   5 NRRYVLKERPRfQVPTAKCFRLEEEAAPEPGEGEFRIRTTWLGMDPNLFSKVKKVSDQARPIPIGAVMYGATVGRVDISN 84
Cdd:cd05288    2 NRQVVLAKRPE-GPPPPDDFELVEVPLPELKDGEVLVRTLYLSVDPYMRGWMSDAKSYSPPVQLGEPMRGGGVGEVVESR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  85 HPDFSVGDLVHGLWGWQDYFISNGAGIFS-VDNDI-SRPSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQ 162
Cdd:cd05288   81 SPDFKVGDLVSGFLGWQEYAVVDGASGLRkLDPSLgLPLSAYLGVLGMTGLTAYFGLTEIGKPKPGETVVVSAAAGAVGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 163 MVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRI 242
Cdd:cd05288  161 VVGQIAKLLGARVVGIAGSDEKCRWLVEELGFDAAINYKTPDLAEALKEAAPDGIDVYFDNVGGEILDAALTLLNKGGRI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 243 AVCGLMALYSMtqlpvTPDRSFMILNEILLKRLTVKGSMVLDmlNTDRHVEFKREMKSWIAQGVVRPVEFITEGLENAPD 322
Cdd:cd05288  241 ALCGAISQYNA-----TEPPGPKNLGNIITKRLTMQGFIVSD--YADRFPEALAELAKWLAEGKLKYREDVVEGLENAPE 313
                        330
                 ....*....|....*.
gi 495523457 323 ALRAVFDGENIGKSVV 338
Cdd:cd05288  314 AFLGLFTGKNTGKLVV 329
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
39-341 2.38e-52

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 176.18  E-value: 2.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  39 FRIRTTWLGMDPNLFSKVKKVSDQARP--IPiGAVMYGATVGRVDISNHPDFSVGDLVHGLWGWQDYFI----SNGAGIF 112
Cdd:PLN03154  46 FLVKNLYLSCDPYMRGRMRDFHDSYLPpfVP-GQRIEGFGVSKVVDSDDPNFKPGDLISGITGWEEYSLirssDNQLRKI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 113 SVDNDISRpSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVSKL 192
Cdd:PLN03154 125 QLQDDIPL-SYHLGLLGMAGFTAYAGFYEVCSPKKGDSVFVSAASGAVGQLVGQLAKLHGCYVVGSAGSSQKVDLLKNKL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 193 GYTDCFNYKSE-NFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSMTQlpvtpDRSFMILNEIL 271
Cdd:PLN03154 204 GFDEAFNYKEEpDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSLNSLSA-----SQGIHNLYNLI 278
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 272 LKRLTVKGSMVLDMLNTdrHVEFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVVHVS 341
Cdd:PLN03154 279 SKRIRMQGFLQSDYLHL--FPQFLENVSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIRVA 346
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
45-338 1.13e-45

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 158.24  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   45 WLGMDPNLFSKVKKVSDqarpipiGAVMYGATVGRVDISNHPDFSVGDLVHGLWGWQDYFISNGAGIFSVDN---DISRP 121
Cdd:TIGR02825  40 FLSVDPYMRVAAKRLKE-------GDTMMGQQVARVVESKNVALPKGTIVLASPGWTSHSISDGKDLEKLLTewpDTLPL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  122 SYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLaVSKLGYTDCFNYK 201
Cdd:TIGR02825 113 SLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAY-LKKLGFDVAFNYK 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  202 S-ENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSMT-QLPVTPDRSFMILNEILLKrltvkg 279
Cdd:TIGR02825 192 TvKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTgPLPPGPPPEIVIYQELRME------ 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 495523457  280 SMVLDMLNTDRHVEFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:TIGR02825 266 GFIVNRWQGEVRQKALKELLKWVLEGKIQYKEYVIEGFENMPAAFMGMLKGENLGKTIV 324
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
6-114 1.49e-24

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 96.11  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457    6 RRYVLKERPRfQVPTAKCFRLEEEAAPEPGEGEFRIRTTWLGMDPNLFSKVKKVSDQARPIPIGAVMYGATVGRVDISNH 85
Cdd:pfam16884   1 KQWLLAKRPE-GVPTPSDFELVEAELPELGDGEVLVRTLYLSVDPYMRGRMNDAKSYVPPVELGDVMRGGAVGEVVESNN 79
                          90       100
                  ....*....|....*....|....*....
gi 495523457   86 PDFSVGDLVHGLWGWQDYFISNGAGIFSV 114
Cdd:pfam16884  80 PDFPVGDLVLGMLGWQDYAVSDGKGLTKV 108
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
135-338 1.05e-14

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 73.19  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   135 AYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKcRLAVSKLGYTD--CFNYKSENFERMLSDR 212
Cdd:smart00829  91 AYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEK-RDFLRALGIPDdhIFSSRDLSFADEILRA 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   213 IDG-GIDamVV--SAGGQTFDATFPLMAPGGRIAVCGLMALYSMTQL---PVTPDRSFMIlneILLKRLTVKGSMVLDML 286
Cdd:smart00829 170 TGGrGVD--VVlnSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLamaPFRPNVSYHA---VDLDALEEGPDRIRELL 244
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 495523457   287 ntdrhvefkREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:smart00829 245 ---------AEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
 
Name Accession Description Interval E-value
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
1-340 1.13e-131

NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 441733 [Multi-domain]  Cd Length: 333  Bit Score: 378.63  E-value: 1.13e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   1 MANINRRYVLKERPRfQVPTAKCFRLEEEAAPEPGEGEFRIRTTWLGMDPNLFSKVKKVSDQARPIPIGAVMYGATVGRV 80
Cdd:COG2130    1 MMTTNRQIVLASRPE-GEPTPEDFRLEEVPVPEPGDGEVLVRNLYLSVDPYMRGRMSDAKSYAPPVELGEVMRGGAVGEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  81 DISNHPDFSVGDLVHGLWGWQDYFISNGAGIFSVDNDISRPSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGAL 160
Cdd:COG2130   80 VESRHPDFAVGDLVLGMLGWQDYAVSDGAGLRKVDPSLAPLSAYLGVLGMPGLTAYFGLLDIGKPKAGETVVVSAAAGAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 161 GQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGG 240
Cdd:COG2130  160 GSVVGQIAKLKGCRVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAAACPDGIDVYFDNVGGEILDAVLPLLNTFA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 241 RIAVCGLMALYSMTQLPVTPdrsfMILNEILLKRLTVKGSMVLDMLntDRHVEFKREMKSWIAQGVVRPVEFITEGLENA 320
Cdd:COG2130  240 RIAVCGAISQYNATEPPPGP----RNLGQLLVKRLRMQGFIVFDHA--DRFPEFLAELAGWVAEGKLKYRETVVEGLENA 313
                        330       340
                 ....*....|....*....|
gi 495523457 321 PDALRAVFDGENIGKSVVHV 340
Cdd:COG2130  314 PEAFLGLFEGENFGKLLVKV 333
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
5-338 1.36e-99

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 297.09  E-value: 1.36e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   5 NRRYVLKERPRfQVPTAKCFRLEEEAAPEPGEGEFRIRTTWLGMDPNLFSKVKKVSDQARPIPIGAVMYGATVGRVDISN 84
Cdd:cd05288    2 NRQVVLAKRPE-GPPPPDDFELVEVPLPELKDGEVLVRTLYLSVDPYMRGWMSDAKSYSPPVQLGEPMRGGGVGEVVESR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  85 HPDFSVGDLVHGLWGWQDYFISNGAGIFS-VDNDI-SRPSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQ 162
Cdd:cd05288   81 SPDFKVGDLVSGFLGWQEYAVVDGASGLRkLDPSLgLPLSAYLGVLGMTGLTAYFGLTEIGKPKPGETVVVSAAAGAVGS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 163 MVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRI 242
Cdd:cd05288  161 VVGQIAKLLGARVVGIAGSDEKCRWLVEELGFDAAINYKTPDLAEALKEAAPDGIDVYFDNVGGEILDAALTLLNKGGRI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 243 AVCGLMALYSMtqlpvTPDRSFMILNEILLKRLTVKGSMVLDmlNTDRHVEFKREMKSWIAQGVVRPVEFITEGLENAPD 322
Cdd:cd05288  241 ALCGAISQYNA-----TEPPGPKNLGNIITKRLTMQGFIVSD--YADRFPEALAELAKWLAEGKLKYREDVVEGLENAPE 313
                        330
                 ....*....|....*.
gi 495523457 323 ALRAVFDGENIGKSVV 338
Cdd:cd05288  314 AFLGLFTGKNTGKLVV 329
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
39-340 6.13e-74

Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This group includes proteins identified as the Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase. The Arabidopsis enzyme, a member of the medium chain dehydrogenase/reductase family, catalyzes the reduction of 7-8-double bond of phenylpropanal substrates as a plant defense mechanism. Prostaglandins and related eicosanoids (lipid mediators involved in host defense and inflamation) are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. Leukotriene B4 (LTB4) can be metabolized by LTB4 20-hydroxylase in inflamatory cells, and in other cells by bifunctional LTB4 12-HD/PGR. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 231.82  E-value: 6.13e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  39 FRIRTTWLGMDPNLFSKVKKVSDQ--ARPIPIGAVMYGATVGRVDISNHPDFSVGDLVHGLWGWQDY-FISNGAGIFSVD 115
Cdd:cd08295   40 VLVKNLYLSCDPYMRGRMKGHDDSlyLPPFKPGEVITGYGVAKVVDSGNPDFKVGDLVWGFTGWEEYsLIPRGQDLRKID 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 116 NDISRPSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYT 195
Cdd:cd08295  120 HTDVPLSYYLGLLGMPGLTAYAGFYEVCKPKKGETVFVSAASGAVGQLVGQLAKLKGCYVVGSAGSDEKVDLLKNKLGFD 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 196 DCFNYKSE-NFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSMTQLPVTPDrsfmiLNEILLKR 274
Cdd:cd08295  200 DAFNYKEEpDLDAALKRYFPNGIDIYFDNVGGKMLDAVLLNMNLHGRIAACGMISQYNLEWPEGVRN-----LLNIIYKR 274
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495523457 275 LTVKGSMVLDMLntDRHVEFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd08295  275 VKIQGFLVGDYL--HRYPEFLEEMSGYIKEGKLKYVEDIADGLESAPEAFVGLFTGSNIGKQVVKV 338
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
63-340 3.92e-57

13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 hydroxydehydrogenase activity; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto- 13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 188.24  E-value: 3.92e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  63 ARPIPIGAVMYGATVGRVDISNHPDFSVGDLVHGLWGWQDYFISNG---AGIFSVDNDISR---PSYCLGALGATGFGAY 136
Cdd:cd08294   53 SKRLNEGDTMIGTQVAKVIESKNSKFPVGTIVVASFGWRTHTVSDGkdqPDLYKLPADLPDdlpPSLALGVLGMPGLTAY 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 137 LVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVsKLGYTDCFNYKSENFERMLSDRIDGG 216
Cdd:cd08294  133 FGLLEICKPKAGETVVVNGAAGAVGSLVGQIAKIKGCKVIGCAGSDDKVAWLK-ELGFDAVFNYKTVSLEEALKEAAPDG 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 217 IDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSMTQlPVTPDRSFMIlneILLKRLTVKGSMVLDMlnTDRHVEFKR 296
Cdd:cd08294  212 IDCYFDNVGGEFSSTVLSHMNDFGRVAVCGSISTYNDKE-PKKGPYVQET---IIFKQLKMEGFIVYRW--QDRWPEALK 285
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 495523457 297 EMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd08294  286 QLLKWIKEGKLKYREHVTEGFENMPQAFIGMLKGENTGKAIVKV 329
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
4-340 7.81e-54

Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 180.28  E-value: 7.81e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   4 INRRYVLKERP-RFQVPTAKCFRLEEEAA-PEPGEGEFRIRTTWLGMDPNLFSKVKKV--SDQARPIPIGAVMYGATVGR 79
Cdd:cd08293    2 INKRVVLNSRPgKNGNPVAENFRVEECTLpDELNEGQVLVRTLYLSVDPYMRCRMNEDtgTDYLAPWQLSQVLDGGGVGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  80 VDISNHPDFSVGDLVHGL-WGWQDYFISNGAGIFSVDNDI--SRPSYCLGALGATGFGAYLVVNDVLAVKNG--DTVFCS 154
Cdd:cd08293   82 VEESKHQKFAVGDIVTSFnWPWQTYAVLDGSSLEKVDPQLvdGHLSYFLGAVGLPGLTALIGIQEKGHITPGanQTMVVS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 155 AATGALGQMVGQISHLKGGATY-GSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSAGGQTFDATF 233
Cdd:cd08293  162 GAAGACGSLAGQIGRLLGCSRVvGICGSDEKCQLLKSELGFDAAINYKTDNVAERLRELCPEGVDVYFDNVGGEISDTVI 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 234 PLMAPGGRIAVCGLMALYSmTQLPVTPDRSFMIlNEILLKR-LTVKGSMVLDMlnTDRHVEFKREMKSWIAQGVVRPVEF 312
Cdd:cd08293  242 SQMNENSHIILCGQISQYN-KDVPYPPPLPEAT-EAILKERnITRERFLVLNY--KDKFEEAIAQLSQWVKEGKLKVKET 317
                        330       340
                 ....*....|....*....|....*...
gi 495523457 313 ITEGLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd08293  318 VYEGLENAGEAFQSMMNGGNIGKQIVKV 345
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
39-341 2.38e-52

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 176.18  E-value: 2.38e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  39 FRIRTTWLGMDPNLFSKVKKVSDQARP--IPiGAVMYGATVGRVDISNHPDFSVGDLVHGLWGWQDYFI----SNGAGIF 112
Cdd:PLN03154  46 FLVKNLYLSCDPYMRGRMRDFHDSYLPpfVP-GQRIEGFGVSKVVDSDDPNFKPGDLISGITGWEEYSLirssDNQLRKI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 113 SVDNDISRpSYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVSKL 192
Cdd:PLN03154 125 QLQDDIPL-SYHLGLLGMAGFTAYAGFYEVCSPKKGDSVFVSAASGAVGQLVGQLAKLHGCYVVGSAGSSQKVDLLKNKL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 193 GYTDCFNYKSE-NFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSMTQlpvtpDRSFMILNEIL 271
Cdd:PLN03154 204 GFDEAFNYKEEpDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSLNSLSA-----SQGIHNLYNLI 278
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 272 LKRLTVKGSMVLDMLNTdrHVEFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVVHVS 341
Cdd:PLN03154 279 SKRIRMQGFLQSDYLHL--FPQFLENVSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIRVA 346
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
45-338 1.13e-45

leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 12-hydroxydehydrogenase is an NADP-dependent enzyme of arachidonic acid metabolism, responsible for converting leukotriene B4 to the much less active metabolite 12-oxo-leukotriene B4. The BRENDA database lists leukotriene B4 12-hydroxydehydrogenase as one of the synonyms of 2-alkenal reductase (EC 1.3.1.74), while 1.3.1.48 is 15-oxoprostaglandin 13-reductase.


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 158.24  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   45 WLGMDPNLFSKVKKVSDqarpipiGAVMYGATVGRVDISNHPDFSVGDLVHGLWGWQDYFISNGAGIFSVDN---DISRP 121
Cdd:TIGR02825  40 FLSVDPYMRVAAKRLKE-------GDTMMGQQVARVVESKNVALPKGTIVLASPGWTSHSISDGKDLEKLLTewpDTLPL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  122 SYCLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLaVSKLGYTDCFNYK 201
Cdd:TIGR02825 113 SLALGTVGMPGLTAYFGLLEICGVKGGETVMVNAAAGAVGSVVGQIAKLKGCKVVGAAGSDEKVAY-LKKLGFDVAFNYK 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  202 S-ENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSMT-QLPVTPDRSFMILNEILLKrltvkg 279
Cdd:TIGR02825 192 TvKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGRIAICGAISTYNRTgPLPPGPPPEIVIYQELRME------ 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 495523457  280 SMVLDMLNTDRHVEFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:TIGR02825 266 GFIVNRWQGEVRQKALKELLKWVLEGKIQYKEYVIEGFENMPAAFMGMLKGENLGKTIV 324
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
87-340 1.02e-31

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 121.02  E-value: 1.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  87 DFSVGDLV--HGLWG-WQDYFISNGAGIFSVDNDISRPSycLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQM 163
Cdd:COG0604   78 GFKVGDRVagLGRGGgYAEYVVVPADQLVPLPDGLSFEE--AAALPLAGLTAWQALFDRGRLKPGETVLVHGAAGGVGSA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 164 VGQISHLKGGATYGSAGTDEKCRLaVSKLGYTDCFNYKSENFERMLSDRIDG-GIDAMVVSAGGQTFDATFPLMAPGGRI 242
Cdd:COG0604  156 AVQLAKALGARVIATASSPEKAEL-LRALGADHVIDYREEDFAERVRALTGGrGVDVVLDTVGGDTLARSLRALAPGGRL 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 243 AVCGLMalySMTQLPVTpdrsfmiLNEILLKRLTVKGSMVLDMLNTDRHVEFkREMKSWIAQGVVRPVefITE--GLENA 320
Cdd:COG0604  235 VSIGAA---SGAPPPLD-------LAPLLLKGLTLTGFTLFARDPAERRAAL-AELARLLAAGKLRPV--IDRvfPLEEA 301
                        250       260
                 ....*....|....*....|
gi 495523457 321 PDALRAVFDGENIGKSVVHV 340
Cdd:COG0604  302 AEAHRLLESGKHRGKVVLTV 321
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
133-338 1.14e-24

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 102.13  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 133 FGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVsKLGYTDCFNYKSENF-ERMLSD 211
Cdd:cd05276  125 FTAWQNLFQLGGLKAGETVLIHGGASGVGTAAIQLAKALGARVIATAGSEEKLEACR-ALGADVAINYRTEDFaEEVKEA 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 212 RIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMAlYSMTQLPvtpdrsfmiLNEILLKRLTVKGSmVLdmlnTDRH 291
Cdd:cd05276  204 TGGRGVDVILDMVGGDYLARNLRALAPDGRLVLIGLLG-GAKAELD---------LAPLLRKRLTLTGS-TL----RSRS 268
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495523457 292 VEFKREMKS--------WIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd05276  269 LEEKAALAAafrehvwpLFASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
6-114 1.49e-24

N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin reductase and alcohol dehydrogenase.


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 96.11  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457    6 RRYVLKERPRfQVPTAKCFRLEEEAAPEPGEGEFRIRTTWLGMDPNLFSKVKKVSDQARPIPIGAVMYGATVGRVDISNH 85
Cdd:pfam16884   1 KQWLLAKRPE-GVPTPSDFELVEAELPELGDGEVLVRTLYLSVDPYMRGRMNDAKSYVPPVELGDVMRGGAVGEVVESNN 79
                          90       100
                  ....*....|....*....|....*....
gi 495523457   86 PDFSVGDLVHGLWGWQDYFISNGAGIFSV 114
Cdd:pfam16884  80 PDFPVGDLVLGMLGWQDYAVSDGKGLTKV 108
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
135-338 1.66e-23

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 98.27  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 135 AYLVVNDVLA---VKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLaVSKLGYTDCFNYKSENFE----R 207
Cdd:cd08251  105 VFLTVIDAFAragLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATASSDDKLEY-LKQLGVPHVINYVEEDFEeeimR 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 208 MLSDRidgGIDAMVVSAGGQTFDATFPLMAPGGR---IAVCGLMALYSMTQLPVTPDRSFMILNeilLKRLtvkgsmvld 284
Cdd:cd08251  184 LTGGR---GVDVVINTLSGEAIQKGLNCLAPGGRyveIAMTALKSAPSVDLSVLSNNQSFHSVD---LRKL--------- 248
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495523457 285 MLNTDRHV-EFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08251  249 LLLDPEFIaDYQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
127-338 1.21e-22

Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 96.41  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 127 ALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAvSKLGYTDCFNYKSENFE 206
Cdd:cd08241  119 ALPVTYGTAYHALVRRARLQPGETVLVLGAAGGVGLAAVQLAKALGARVIAAASSEEKLALA-RALGADHVIDYRDPDLR 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 207 RMLSDRIDG-GIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLmALYSMTQLPVtpdrsfmilNEILLKRLTVKGsmvLD- 284
Cdd:cd08241  198 ERVKALTGGrGVDVVYDPVGGDVFEASLRSLAWGGRLLVIGF-ASGEIPQIPA---------NLLLLKNISVVG---VYw 264
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495523457 285 ----MLNTDRHVEFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08241  265 gayaRREPELLRANLAELFDLLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVL 322
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
135-338 2.94e-18

enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 83.39  E-value: 2.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 135 AYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDC-FNYKSENFERMLSDRI 213
Cdd:cd05195   96 AYYALVDLARLQKGESVLIHAAAGGVGQAAIQLAQHLGAEVFATVGSEEKREFLRELGGPVDHiFSSRDLSFADGILRAT 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 214 DG-GIDamVV--SAGGQTFDATFPLMAPGGRIAVCGLMALYSMTQLPVTP---DRSFMILNeiLLKRLTVKGSMVLDMLn 287
Cdd:cd05195  176 GGrGVD--VVlnSLSGELLRASWRCLAPFGRFVEIGKRDILSNSKLGMRPflrNVSFSSVD--LDQLARERPELLRELL- 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495523457 288 tdrhvefkREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd05195  251 --------REVLELLEAGVLKPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
56-282 1.06e-17

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 81.60  E-value: 1.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  56 VKKVSDQARPIPIG-AVMYGATVGRVDISNHPDFSVGDLVHGLW---GWQDYFISNGAGIFSVDNDISRPSYCLgaLGAT 131
Cdd:cd05188   41 VVEVGPGVTGVKVGdRVVVLPNLGCGTCELCRELCPGGGILGEGldgGFAEYVVVPADNLVPLPDGLSLEEAAL--LPEP 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 132 GFGAYLVVNDVLAVKNGDTVFCSAAtGALGQMVGQISHLKGGATYGSAGTDEKCRLAVsKLGYTDCFNYKSENFERMLSD 211
Cdd:cd05188  119 LATAYHALRRAGVLKPGDTVLVLGA-GGVGLLAAQLAKAAGARVIVTDRSDEKLELAK-ELGADHVIDYKEEDLEEELRL 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495523457 212 RIDGGIDAMVVSAGG-QTFDATFPLMAPGGRIAVCGLMALYSMtqlpvtpdrsFMILNEILLKRLTVKGSMV 282
Cdd:cd05188  197 TGGGGADVVIDAVGGpETLAQALRLLRPGGRIVVVGGTSGGPP----------LDDLRRLLFKELTIIGSTG 258
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
131-338 2.10e-16

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 78.84  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 131 TGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVSkLGYTDCFNYKSENFERMLS 210
Cdd:cd08250  123 SGLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTCSSDEKAEFLKS-LGCDRPINYKTEDLGEVLK 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 211 DRIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSmTQLPVTPDRSFMILNEILLKRLTVKGSMVLDMLNTDR 290
Cdd:cd08250  202 KEYPKGVDVVYESVGGEMFDTCVDNLALKGRLIVIGFISGYQ-SGTGPSPVKGATLPPKLLAKSASVRGFFLPHYAKLIP 280
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495523457 291 HVeFKReMKSWIAQGVVR----PVEFitEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08250  281 QH-LDR-LLQLYQRGKLVcevdPTRF--RGLESVADAVDYLYSGKNIGKVVV 328
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
159-282 8.37e-15

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 70.33  E-value: 8.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  159 ALGQMVGQISHLKGGATYGSAGTDEKCRLAvSKLGYTDCFNYKSENFERMLSDRIDG-GIDAMVVSAG-GQTFDATFPLM 236
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELA-KELGADHVINPKETDLVEEIKELTGGkGVDVVFDCVGsPATLEQALKLL 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 495523457  237 APGGRIAVCGLMalYSMTQLPVTPdrsfmilneILLKRLTVKGSMV 282
Cdd:pfam00107  80 RPGGRVVVVGLP--GGPLPLPLAP---------LLLKELTILGSFL 114
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
136-338 9.90e-15

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 73.63  E-value: 9.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 136 YLVvNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAvSKLGYTDCFNYKSENF-ERMLsdRID 214
Cdd:cd05286  126 YLL-RETYPVKPGDTVLVHAAAGGVGLLLTQWAKALGATVIGTVSSEEKAELA-RAAGADHVINYRDEDFvERVR--EIT 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 215 GGIDAMVV--SAGGQTFDATFPLMAPggriavCGLMALYSMTQLPVTPdrsfmilneILLKRLTvKGSMVL---DMLN-T 288
Cdd:cd05286  202 GGRGVDVVydGVGKDTFEGSLDSLRP------RGTLVSFGNASGPVPP---------FDLLRLS-KGSLFLtrpSLFHyI 265
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495523457 289 DRHVEFKR---EMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd05286  266 ATREELLAraaELFDAVASGKLKVEIGKRYPLADAAQAHRDLESRKTTGKLLL 318
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
135-338 1.05e-14

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 73.19  E-value: 1.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   135 AYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKcRLAVSKLGYTD--CFNYKSENFERMLSDR 212
Cdd:smart00829  91 AYYALVDLARLRPGESVLIHAAAGGVGQAAIQLARHLGAEVFATAGSPEK-RDFLRALGIPDdhIFSSRDLSFADEILRA 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457   213 IDG-GIDamVV--SAGGQTFDATFPLMAPGGRIAVCGLMALYSMTQL---PVTPDRSFMIlneILLKRLTVKGSMVLDML 286
Cdd:smart00829 170 TGGrGVD--VVlnSLSGEFLDASLRCLAPGGRFVEIGKRDIRDNSQLamaPFRPNVSYHA---VDLDALEEGPDRIRELL 244
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 495523457   287 ntdrhvefkREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:smart00829 245 ---------AEVLELFAEGVLRPLPVTVFPISDAEDAFRYMQQGKHIGKVVL 287
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
86-338 2.13e-13

alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 69.90  E-value: 2.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  86 PDFSVGDLVHGL-----WG-WQDYFISNGAGIFSVDNDISRPSycLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGA 159
Cdd:cd05289   79 TGFKVGDEVFGMtpftrGGaYAEYVVVPADELALKPANLSFEE--AAALPLAGLTAWQALFELGGLKAGQTVLIHGAAGG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 160 LGQMVGQISHLKGG---ATYGSAGTDEkcrlaVSKLGYTDCFNYKSENFERmlsDRIDGGIDAMVVSAGGQTFDATFPLM 236
Cdd:cd05289  157 VGSFAVQLAKARGArviATASAANADF-----LRSLGADEVIDYTKGDFER---AAAPGGVDAVLDTVGGETLARSLALV 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 237 APGGRIAvcglmalysmTQLPVTPDRSFMILNEILLKRLTVKGSM-VLDMLNtdrhvefkremkSWIAQGVVRPVEFITE 315
Cdd:cd05289  229 KPGGRLV----------SIAGPPPAEQAAKRRGVRAGFVFVEPDGeQLAELA------------ELVEAGKLRPVVDRVF 286
                        250       260
                 ....*....|....*....|...
gi 495523457 316 GLENAPDALRAVFDGENIGKSVV 338
Cdd:cd05289  287 PLEDAAEAHERLESGHARGKVVL 309
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
122-338 4.71e-13

Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye lens protein with NADP-dependent quinone reductase activity (QOR). It has been cited as a structural component in mammalian eyes, but also has homology to quinone reductases in unrelated species. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 68.76  E-value: 4.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 122 SYCLGA-LGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVsKLGYTDCFNY 200
Cdd:cd08253  118 SFEQGAaLGIPALTAYRALFHRAGAKAGETVLVHGGSGAVGHAAVQLARWAGARVIATASSAEGAELVR-QAGADAVFNY 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 201 KSENF-ERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGlmalySMTQLPVTPdrsfmiLNEILLKRLTVKG 279
Cdd:cd08253  197 RAEDLaDRILAATAGQGVDVIIEVLANVNLAKDLDVLAPGGRIVVYG-----SGGLRGTIP------INPLMAKEASIRG 265
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495523457 280 sMVLDMLNTDRHVEFKREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08253  266 -VLLYTATPEERAAAAEAIAAGLADGALRPVIAREYPLEEAAAAHEAVESGGAIGKVVL 323
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
77-335 6.45e-13

2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 68.46  E-value: 6.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  77 VGRVDI--SNHPDFSVGDLV---HGLWGWQDYFISNGAGIFSVDNDISRpsyclgALGATGF----GAYLVVNDVLAVKN 147
Cdd:cd05282   65 VGVVVEvgSGVSGLLVGQRVlplGGEGTWQEYVVAPADDLIPVPDSISD------EQAAMLYinplTAWLMLTEYLKLPP 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 148 GDTVFCSAATGALGQMVGQISHLKGGAT------------YGSAGTDEKCrlavsklgytdcfNYKSENFERMLSDRIDG 215
Cdd:cd05282  139 GDWVIQNAANSAVGRMLIQLAKLLGFKTinvvrrdeqveeLKALGADEVI-------------DSSPEDLAQRVKEATGG 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 216 -GIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLmalysMTQLPVTPDRSFMILNEILLKRLTVKGSMVlDMLNTDRHVEF 294
Cdd:cd05282  206 aGARLALDAVGGESATRLARSLRPGGTLVNYGL-----LSGEPVPFPRSVFIFKDITVRGFWLRQWLH-SATKEAKQETF 279
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 495523457 295 kREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGK 335
Cdd:cd05282  280 -AEVIKLVEAGVLTTPVGAKFPLEDFEEAVAAAEQPGRGGK 319
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
99-341 7.21e-13

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 68.63  E-value: 7.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  99 GWQDYFISNGAGIFSVDNDISRPsycLGALG---ATGFGAylvvNDVLAVKNGDTVFCSAAtGALGQMVGQISHLKGGAT 175
Cdd:COG1063  117 GFAEYVRVPAANLVKVPDGLSDE---AAALVeplAVALHA----VERAGVKPGDTVLVIGA-GPIGLLAALAARLAGAAR 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 176 -YGSAGTDEKCRLAvSKLGYTDCFNYKSENFERMLSDRIDG-GIDAMVVSAG-GQTFDATFPLMAPGGRIAVCGLMAlyS 252
Cdd:COG1063  189 vIVVDRNPERLELA-RELGADAVVNPREEDLVEAVRELTGGrGADVVIEAVGaPAALEQALDLVRPGGTVVLVGVPG--G 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 253 MTQLPvtpdrsfmiLNEILLKRLTVKGSMVldmlNTDRHVefkREMKSWIAQGVVRPVEFITE--GLENAPDALRAVFDG 330
Cdd:COG1063  266 PVPID---------LNALVRKELTLRGSRN----YTREDF---PEALELLASGRIDLEPLITHrfPLDDAPEAFEAAADR 329
                        250
                 ....*....|..
gi 495523457 331 E-NIGKSVVHVS 341
Cdd:COG1063  330 AdGAIKVVLDPD 341
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
129-338 7.33e-13

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 68.21  E-value: 7.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 129 GATGFGAYLVVNdvlaVKNGDTVFCSAAtGALGQMVGQISHLKGGATYGSAGTDEKCRLAvSKLGYTDCFNYKSENFERM 208
Cdd:COG1064  148 GITAYRALRRAG----VGPGDRVAVIGA-GGLGHLAVQIAKALGAEVIAVDRSPEKLELA-RELGADHVVNSSDEDPVEA 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 209 LSDriDGGIDAMVVSAG-GQTFDATFPLMAPGGRIAVCGLMalysMTQLPVTPDRsfmilneILLKRLTVKGSMVLDMLN 287
Cdd:COG1064  222 VRE--LTGADVVIDTVGaPATVNAALALLRRGGRLVLVGLP----GGPIPLPPFD-------LILKERSIRGSLIGTRAD 288
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495523457 288 TdrhvefkREMKSWIAQGVVRP-VEFIteGLENAPDALRAVFDGENIGKSVV 338
Cdd:COG1064  289 L-------QEMLDLAAEGKIKPeVETI--PLEEANEALERLRAGKVRGRAVL 331
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
192-338 1.90e-12

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 63.50  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  192 LGYTDCFNYKSENFERMLSDRidgGIDAMVVSAGGQTFDATFPLMAPGGRIaVCGLMALYSMTQLPVTPDRSFMILNEIL 271
Cdd:pfam13602   1 LGADEVIDYRTTDFVQATGGE---GVDVVLDTVGGEAFEASLRVLPGGGRL-VTIGGPPLSAGLLLPARKRGGRGVKYLF 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495523457  272 LKRLTVKGSMVLdmlntdrhvefkREMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:pfam13602  77 LFVRPNLGADIL------------QELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
87-338 4.28e-11

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 62.99  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  87 DFSVGDLVHGL---WGWQDYFISNGAGIFSVDNDISRPSycLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQM 163
Cdd:cd08275   77 DFKVGDRVMGLtrfGGYAEVVNVPADQVFPLPDGMSFEE--AAAFPVNYLTAYYALFELGNLRPGQSVLVHSAAGGVGLA 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 164 VGQI-SHLKGGATYGSAGTdEKCRlAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSAGGQTFDATFPLMAPGGRi 242
Cdd:cd08275  155 AGQLcKTVPNVTVVGTASA-SKHE-ALKENGVTHVIDYRTQDYVEEVKKISPEGVDIVLDALGGEDTRKSYDLLKPMGR- 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 243 avcglMALYSMTQLPVTPDRSFMILNEILLKRLTV---------KGSMVLDMLNTDRHVEFKREMKS----WIAQGVVRP 309
Cdd:cd08275  232 -----LVVYGAANLVTGEKRSWFKLAKKWWNRPKVdpmklisenKSVLGFNLGWLFEERELLTEVMDkllkLYEEGKIKP 306
                        250       260
                 ....*....|....*....|....*....
gi 495523457 310 VEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08275  307 KIDSVFPFEEVGEAMRRLQSRKNIGKVVL 335
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
83-342 5.85e-11

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 62.74  E-value: 5.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  83 SNHPDFSVGDLVHGLW---GWQDYFISNGAGIFSVDNDISRPSycLGALGATGFGAYLVVNDVLAVKNGDTVFCSAATGA 159
Cdd:PTZ00354  75 SDVKRFKEGDRVMALLpggGYAEYAVAHKGHVMHIPQGYTFEE--AAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASG 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 160 LGQMVGQISHLKGGATYGSAGTDEKCRlAVSKLGYTDCFNYKSE-NF-ERMLSDRIDGGIDAMVVSAGGQTFDATFPLMA 237
Cdd:PTZ00354 153 VGTAAAQLAEKYGAATIITTSSEEKVD-FCKKLAAIILIRYPDEeGFaPKVKKLTGEKGVNLVLDCVGGSYLSETAEVLA 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 238 PGGRIAVCGLMALYSMTQLPVTPdrsfmilneILLKRLTVKGSMVL---DMLNTDRHVEFKREMKSWIAQGVVRPVEFIT 314
Cdd:PTZ00354 232 VDGKWIVYGFMGGAKVEKFNLLP---------LLRKRASIIFSTLRsrsDEYKADLVASFEREVLPYMEEGEIKPIVDRT 302
                        250       260
                 ....*....|....*....|....*...
gi 495523457 315 EGLENAPDALRAVFDGENIGKSVVHVSD 342
Cdd:PTZ00354 303 YPLEEVAEAHTFLEQNKNIGKVVLTVNE 330
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
145-340 6.32e-11

Alcohol dehydrogenases of the MDR family; This group contains proteins related to the zinc-dependent alcohol dehydrogenases. However, while the group has structural zinc site characteristic of these enzymes, it lacks the consensus site for a catalytic zinc. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 62.66  E-value: 6.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 145 VKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAvSKLGYTDCFNYKSENFERMLSDRIDG-GIDAMVVS 223
Cdd:cd08266  164 LRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEDKLERA-KELGADYVIDYRKEDFVREVRELTGKrGVDVVVEH 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 224 AGGQTFDATFPLMAPGGRIAVCGlmalySMTQLPVTPDrsfmiLNEILLKRLTVKGSMvldMLNTDrhvEFkREMKSWIA 303
Cdd:cd08266  243 VGAATWEKSLKSLARGGRLVTCG-----ATTGYEAPID-----LRHVFWRQLSILGST---MGTKA---EL-DEALRLVF 305
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 495523457 304 QGVVRPVEFITEGLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd08266  306 RGKLKPVIDSVFPLEEAAEAHRRLESREQFGKIVLTP 342
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
87-339 3.68e-10

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 60.23  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  87 DFSVGDLVhglwgwqdyfisngagifSVDNDIS----------RPSYC--LGALGAT---GFGAYLVVN----------- 140
Cdd:cd08234   73 GFKVGDRV------------------AVDPNIYcgecfycrrgRPNLCenLTAVGVTrngGFAEYVVVPakqvykipdnl 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 141 ------------------DVLAVKNGDTVFCSAAtGALGQMVGQISHLKGGAT-YGSAGTDEKCRLAvSKLGYTDCFNYK 201
Cdd:cd08234  135 sfeeaalaeplscavhglDLLGIKPGDSVLVFGA-GPIGLLLAQLLKLNGASRvTVAEPNEEKLELA-KKLGATETVDPS 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 202 SENFERMLSDRIdGGIDAmVVSAGG--QTFDATFPLMAPGGRIAVCGLMAlysmtqlpvtPDRSFMI-LNEILLKRLTVK 278
Cdd:cd08234  213 REDPEAQKEDNP-YGFDV-VIEATGvpKTLEQAIEYARRGGTVLVFGVYA----------PDARVSIsPFEIFQKELTII 280
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495523457 279 GSMVLdMLNTDRHVEfkremksWIAQGVVRPVEFITE--GLENAPDALRAVFDGENIgKSVVH 339
Cdd:cd08234  281 GSFIN-PYTFPRAIA-------LLESGKIDVKGLVSHrlPLEEVPEALEGMRSGGAL-KVVVV 334
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
144-338 1.01e-09

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 59.23  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 144 AVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCrlAVSKLGyTDCFNYKSENFERMLSDRIDGGIDAMVVS 223
Cdd:cd08274  174 GVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAVAGAAKEE--AVRALG-ADTVILRDAPLLADAKALGGEPVDVVADV 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 224 AGGQTFDATFPLMAPGGRIAVCGLMAlYSMTQLPvtpdrsfmiLNEILLKRLTVKGSMVLdmlnTDRhvEFkREMKSWIA 303
Cdd:cd08274  251 VGGPLFPDLLRLLRPGGRYVTAGAIA-GPVVELD---------LRTLYLKDLTLFGSTLG----TRE--VF-RRLVRYIE 313
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495523457 304 QGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08274  314 EGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVL 348
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
71-330 3.78e-09

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 56.90  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  71 VMYG-ATVGRV-DI-SNHPDFSVGDLVHGLWGWQDYFISNGAGIFSVDNDISRPSYCLGALGATGfgaylvVNDVL--AV 145
Cdd:cd08255   22 LPPGySSVGRVvEVgSGVTGFKPGDRVFCFGPHAERVVVPANLLVPLPDGLPPERAALTALAATA------LNGVRdaEP 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 146 KNGDTVFCSAAtGALGQMVGQISHLKGGATYgsAGTD---EKCRLAVsKLGYTDCFnyKSENFERMLSDRIDGGIDAmvv 222
Cdd:cd08255   96 RLGERVAVVGL-GLVGLLAAQLAKAAGAREV--VGVDpdaARRELAE-ALGPADPV--AADTADEIGGRGADVVIEA--- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 223 SAGGQTFDATFPLMAPGGRIavcGLMALYSMTQLPvtPDRSFMIlneillKRLTVKGSMV--LDMLNTDRHVEFKREMK- 299
Cdd:cd08255  167 SGSPSALETALRLLRDRGRV---VLVGWYGLKPLL--LGEEFHF------KRLPIRSSQVygIGRYDRPRRWTEARNLEe 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 495523457 300 --SWIAQGVVRPveFITE--GLENAPDALRAVFDG 330
Cdd:cd08255  236 alDLLAEGRLEA--LITHrvPFEDAPEAYRLLFED 268
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
129-337 7.32e-09

Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 56.22  E-value: 7.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 129 GATGFGAYlvvnDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVsKLGYTDCFNYKSENFERM 208
Cdd:cd08244  128 GRTALGLL----DLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAKTALVR-ALGADVAVDYTRPDWPDQ 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 209 LSDRIDGGiDAMVV--SAGGQTFDATFPLMAPGGRIAVCGLMalySMTQLPVTPDrsfmilnEILLKRLTVKGSMVLDML 286
Cdd:cd08244  203 VREALGGG-GVTVVldGVGGAIGRAALALLAPGGRFLTYGWA---SGEWTALDED-------DARRRGVTVVGLLGVQAE 271
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495523457 287 NTDRHVEFKREMKSwIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSV 337
Cdd:cd08244  272 RGGLRALEARALAE-AAAGRLVPVVGQTFPLERAAEAHAALEARSTVGKVL 321
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
145-339 1.39e-08

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 55.33  E-value: 1.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 145 VKNGDTVFCsAATGALGQMVGQISHLKGGATYGSAGTDEKcRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVSA 224
Cdd:cd08254  163 VKPGETVLV-IGLGGLGLNAVQIAKAMGAAVIAVDIKEEK-LELAKELGADEVLNSLDDSPKDKKAAGLGGGFDVIFDFV 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 225 G-GQTFDATFPLMAPGGRIAVCGLmalySMTQLPVTpdrsfmiLNEILLKRLTVKGSmvldmlNTDRHVEFkREMKSWIA 303
Cdd:cd08254  241 GtQPTFEDAQKAVKPGGRIVVVGL----GRDKLTVD-------LSDLIARELRIIGS------FGGTPEDL-PEVLDLIA 302
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 495523457 304 QGVVRP-VEfiTEGLENAPDALRAVFDGENIGKSVVH 339
Cdd:cd08254  303 KGKLDPqVE--TRPLDEIPEVLERLHKGKVKGRVVLV 337
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
127-340 1.61e-08

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 55.30  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 127 ALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRlAVSKLGYTDCFNYKSENFe 206
Cdd:cd08268  124 ALWMQYLTAYGALVELAGLRPGDSVLITAASSSVGLAAIQIANAAGATVIATTRTSEKRD-ALLALGAAHVIVTDEEDL- 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 207 RMLSDRIDGGIDAMVV--SAGGQTFDATFPLMAPGGRIAVCGLMAlysmtqLPVTPDrsfmILNEILLKRLTVKGsmvLD 284
Cdd:cd08268  202 VAEVLRITGGKGVDVVfdPVGGPQFAKLADALAPGGTLVVYGALS------GEPTPF----PLKAALKKSLTFRG---YS 268
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 285 MLNTDRHVEFKREMKSWI----AQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd08268  269 LDEITLDPEARRRAIAFIldglASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP 328
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
144-338 4.09e-08

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 54.24  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 144 AVKNGDTVFCSAATGALGqmVGQISHLKG-GATYGSAGTDEKCRLAVSKLGYTDCFNYK--SENFERMlsdridGGIDAM 220
Cdd:cd08259  159 GVKKGDTVLVTGAGGGVG--IHAIQLAKAlGARVIAVTRSPEKLKILKELGADYVIDGSkfSEDVKKL------GGADVV 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 221 VVSAGGQTFDATFPLMAPGGRIAVCGlmalysmtqlPVTPDRSFMILNEILLKRLTVKGSMVldmlNTDRHVEFKREMks 300
Cdd:cd08259  231 IELVGSPTIEESLRSLNKGGRLVLIG----------NVTPDPAPLRPGLLILKEIRIIGSIS----ATKADVEEALKL-- 294
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495523457 301 wIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08259  295 -VKEGKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVL 331
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
127-338 1.77e-07

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 51.89  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 127 ALGATGFGAYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRlaVSKLGYTDCFNYKSENFE 206
Cdd:cd08271  121 ALPCAGLTAYQALFKKLRIEAGRTILITGGAGGVGSFAVQLAKRAGLRVITTCSKRNFEY--VKSLGADHVIDYNDEDVC 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 207 RMLSDRIDG-GIDAMVVSAGGQTFDATFPLMAPGGRIAVcgLMALysmtqLPVTPDRSFMI---LNEILLKRLTVKGSMV 282
Cdd:cd08271  199 ERIKEITGGrGVDAVLDTVGGETAAALAPTLAFNGHLVC--IQGR-----PDASPDPPFTRalsVHEVALGAAHDHGDPA 271
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495523457 283 lDMLNTDRHVEfkrEMKSWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08271  272 -AWQDLRYAGE---ELLELLAAGKLEPLVIEVLPFEQLPEALRALKDRHTRGKIVV 323
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
135-338 3.41e-07

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 51.11  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 135 AYLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAgtDEKCRLAVSKLGYTdCFNYKSENF-ERMLsdrI 213
Cdd:cd08273  127 AYQMLHRAAKVLTGQRVLIHGASGGVGQALLELALLAGAEVYGTA--SERNHAALRELGAT-PIDYRTKDWlPAML---T 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 214 DGGIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMALYSmtQLPVTPDRSFMILNEILLKRLTVKGSMV----LDMLNTD 289
Cdd:cd08273  201 PGGVDVVFDGVGGESYEESYAALAPGGTLVCYGGNSSLL--QGRRSLAALGSLLARLAKLKLLPTGRRAtfyyVWRDRAE 278
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495523457 290 RHVEFKREMK---SWIAQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08273  279 DPKLFRQDLTellDLLAKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVL 330
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
99-338 7.02e-07

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 50.45  E-value: 7.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  99 GWQDYFISNGAGIFSVDNDISRPSYCLgaLGATGFGAYLVVNDVLAVKNGDTVfCSAATGALGQMVGQISHLKGGATYGS 178
Cdd:cd08263  141 GLAEYAVVPATALAPLPESLDYTESAV--LGCAGFTAYGALKHAADVRPGETV-AVIGVGGVGSSAIQLAKAFGASPIIA 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 179 AGT-DEKCRLAvSKLGYTDCFNYKSENFERMLSDRIDG-GIDaMVVSAGG--QTFDATFPLMAPGGRIAVCGLMALYSMT 254
Cdd:cd08263  218 VDVrDEKLAKA-KELGATHTVNAAKEDAVAAIREITGGrGVD-VVVEALGkpETFKLALDVVRDGGRAVVVGLAPGGATA 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 255 QLPVTPdrsfmilneILLKRLTVKGSM----------VLDMlntdrhvefkremkswIAQGVVRPVEFITE--GLENAPD 322
Cdd:cd08263  296 EIPITR---------LVRRGIKIIGSYgarprqdlpeLVGL----------------AASGKLDPEALVTHkyKLEEINE 350
                        250
                 ....*....|....*.
gi 495523457 323 ALRAVFDGENIGKSVV 338
Cdd:cd08263  351 AYENLRKGLIHGRAIV 366
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
145-341 1.46e-06

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 49.27  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 145 VKNGDTVFCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRlAVSKLG-YTDCFNYKSENFERMlsdridGGIDAMVVS 223
Cdd:PRK13771 160 VKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAK-IVSKYAdYVIVGSKFSEEVKKI------GGADIVIET 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 224 AGGQTFDATFPLMAPGGRIAVCGlmalysmtqlPVTPDRSF-MILNEILLKRLTVKGSMVldmlNTDRHVEFKREMkswI 302
Cdd:PRK13771 233 VGTPTLEESLRSLNMGGKIIQIG----------NVDPSPTYsLRLGYIILKDIEIIGHIS----ATKRDVEEALKL---V 295
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495523457 303 AQGVVRPVEFITEGLENAPDALRAVFDGENIGKSVVHVS 341
Cdd:PRK13771 296 AEGKIKPVIGAEVSLSEIDKALEELKDKSRIGKILVKPS 334
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
96-329 1.61e-06

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 49.20  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  96 GLWGWQD----------YFISNGA--GIFSVDNDISRPS-YCLGALGATGF-GAylvvndVLA-VKNGDTVfCSAATGAL 160
Cdd:cd05278  107 GLWGWKLgnridggqaeYVRVPYAdmNLAKIPDGLPDEDaLMLSDILPTGFhGA------ELAgIKPGSTV-AVIGAGPV 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 161 GQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDG-GIDAMVVSAGGQ-TFDATFPLMAP 238
Cdd:cd05278  180 GLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKNGDIVEQILELTGGrGVDCVIEAVGFEeTFEQAVKVVRP 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 239 GGRIAVCGlmalysmtqLPVTPDRSFMiLNEILLKRLTVKGSMVLDMLNTdrhvefkREMKSWIAQGVVRPVEFITE--G 316
Cdd:cd05278  260 GGTIANVG---------VYGKPDPLPL-LGEWFGKNLTFKTGLVPVRARM-------PELLDLIEEGKIDPSKLITHrfP 322
                        250
                 ....*....|...
gi 495523457 317 LENAPDALRaVFD 329
Cdd:cd05278  323 LDDILKAYR-LFD 334
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
145-340 1.65e-06

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 49.07  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 145 VKNGDTVfcsaatgaLGQMVG-------QISHLKGGATYGSAGTDEKcrLA-VSKLGYTDCFNYKSE-NFERMLSDRIDG 215
Cdd:cd08276  158 LKPGDTV--------LVQGTGgvslfalQFAKAAGARVIATSSSDEK--LErAKALGADHVINYRTTpDWGEEVLKLTGG 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 216 -GIDAMVVSAGGQTFDATFPLMAPGGRIAVCGLMAlYSMTQLPVTPdrsfmilneILLKRLTVKGSMV--LDMLntdrhv 292
Cdd:cd08276  228 rGVDHVVEVGGPGTLAQSIKAVAPGGVISLIGFLS-GFEAPVLLLP---------LLTKGATLRGIAVgsRAQF------ 291
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495523457 293 efkREMKSWIAQGVVRPVefITE--GLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd08276  292 ---EAMNRAIEAHRIRPV--IDRvfPFEEAKEAYRYLESGSHFGKVVIRV 336
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
77-340 1.72e-06

2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 49.14  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  77 VGRV-DI-SNHPDFSVGDLV----HGLWGWQDYFISNGAGIFSVDNDIsrPSYCLGALG---ATgfgAYLVVNDVLAVKN 147
Cdd:cd08290   72 VGEVvKVgSGVKSLKPGDWViplrPGLGTWRTHAVVPADDLIKVPNDV--DPEQAATLSvnpCT---AYRLLEDFVKLQP 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 148 GDTVFCSAATGALGQMVGQISHLKGGATY----GSAGTDE-KCRLAvsKLGYTDCFNYkSENFERMLSDRIDGGIDAMVV 222
Cdd:cd08290  147 GDWVIQNGANSAVGQAVIQLAKLLGIKTInvvrDRPDLEElKERLK--ALGADHVLTE-EELRSLLATELLKSAPGGRPK 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 223 SA----GGQTFDATFPLMAPGGRIAVCGLMalySMTQLPVtPDRSFmilneiLLKRLTVKG---SMVLDMLNTDRHVEFK 295
Cdd:cd08290  224 LAlncvGGKSATELARLLSPGGTMVTYGGM---SGQPVTV-PTSLL------IFKDITLRGfwlTRWLKRANPEEKEDML 293
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 495523457 296 REMKSWIAQGVVR--PVEFITE-GLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd08290  294 EELAELIREGKLKapPVEKVTDdPLEEFKDALANALKGGGGGKQVLVM 341
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
144-340 1.99e-06

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 48.72  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 144 AVKNGDTVFCSAAtGALGQMVGQISHLKGGATYGSAGTDEKCRLAVsKLGYTDCFNYKSENFERMLSDRIDGGIDAMVVS 223
Cdd:cd08261  156 GVTAGDTVLVVGA-GPIGLGVIQVAKARGARVIVVDIDDERLEFAR-ELGADDTINVGDEDVAARLRELTDGEGADVVID 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 224 AGG--QTFDATFPLMAPGGRIAVCGLmalysmTQLPVT-PDRsfmilnEILLKRLTVKGSMvldmlNTDRHvEFKREMKs 300
Cdd:cd08261  234 ATGnpASMEEAVELVAHGGRVVLVGL------SKGPVTfPDP------EFHKKELTILGSR-----NATRE-DFPDVID- 294
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495523457 301 WIAQGVVRPVEFITE--GLENAPDAL-RAVFDGENIGKSVVHV 340
Cdd:cd08261  295 LLESGKVDPEALITHrfPFEDVPEAFdLWEAPPGGVIKVLIEF 337
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
145-331 2.40e-06

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 48.76  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 145 VKNGDTVFCSAAtGALGQMVGQISHLKGGATYGSAGTDEKcRLAVSK-LGYTDCFNYKSENFERMLSDRIDGGIDAMVVS 223
Cdd:cd08236  157 ITLGDTVVVIGA-GTIGLLAIQWLKILGAKRVIAVDIDDE-KLAVAReLGADDTINPKEEDVEKVRELTEGRGADLVIEA 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 224 AG-GQTFDATFPLMAPGGRIAVCGLmalysmtqlpVTPDRSFM--ILNEILLKRLTVKGSMvldMLNT--DRHVEFKREM 298
Cdd:cd08236  235 AGsPATIEQALALARPGGKVVLVGI----------PYGDVTLSeeAFEKILRKELTIQGSW---NSYSapFPGDEWRTAL 301
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495523457 299 kSWIAQGVVRPVEFITE--GLENAPDALRAVFDGE 331
Cdd:cd08236  302 -DLLASGKIKVEPLITHrlPLEDGPAAFERLADRE 335
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
158-338 2.54e-06

Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes, or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 48.47  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 158 GALGQMVGQISHLKGGATYGSAGTDEKCRLAvSKLGYTDCFNYKSENfeRMLSDriDGGID-AMVVSAGGQTFDATFPLM 236
Cdd:cd08245  172 GGLGHLAVQYARAMGFETVAITRSPDKRELA-RKLGADEVVDSGAEL--DEQAA--AGGADvILVTVVSGAAAEAALGGL 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 237 APGGRIAVCGlmalysmtqLPVTPDRSFMILNeILLKRLTVKGSMVLDMLNTdrhvefkREMKSWIAQGVVRP-VEfiTE 315
Cdd:cd08245  247 RRGGRIVLVG---------LPESPPFSPDIFP-LIMKRQSIAGSTHGGRADL-------QEALDFAAEGKVKPmIE--TF 307
                        170       180
                 ....*....|....*....|...
gi 495523457 316 GLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08245  308 PLDQANEAYERMEKGDVRFRFVL 330
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
73-340 1.79e-05

enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 46.04  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  73 YGATVGRvDI--------SNHPDFSVGD----LVHGLW-------GWQDYFISNGAGIFSVDNDISRP---SYCLGALGA 130
Cdd:cd08249   54 YPAILGC-DFagtvvevgSGVTRFKVGDrvagFVHGGNpndprngAFQEYVVADADLTAKIPDNISFEeaaTLPVGLVTA 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 131 -TGFGAYLVVNDVL----AVKNGDTVFCSAATGALGQMVGQISHLKGG---ATYGSAGTDEkcrlaVSKLGYTDCFNYKS 202
Cdd:cd08249  133 aLALFQKLGLPLPPpkpsPASKGKPVLIWGGSSSVGTLAIQLAKLAGYkviTTASPKNFDL-----VKSLGADAVFDYHD 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 203 EN----FERMLSDRIDGGIDAmvVSAGGqTFDATFPLMAPGGRIAVCGLmalysmtqLPVTPDRSFMilneillKRLTVK 278
Cdd:cd08249  208 PDvvedIRAATGGKLRYALDC--ISTPE-SAQLCAEALGRSGGGKLVSL--------LPVPEETEPR-------KGVKVK 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 279 GSMVLDMLNTDRH-----VEFKREMKSWIAQGVVR--PVEFITEGLENAPDALRAVFDGENIG-KSVVHV 340
Cdd:cd08249  270 FVLGYTVFGEIPEdrefgEVFWKYLPELLEEGKLKphPVRVVEGGLEGVQEGLDLLRKGKVSGeKLVVRL 339
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
158-338 7.89e-05

6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the zinc-dependent alcohol dehydrogenase-like family of medium chain dehydrogenases/reductases catalyzes the conversion of 6-hydroxyhexanoate and NAD(+) to 6-oxohexanoate + NADH and H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 44.14  E-value: 7.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 158 GALGQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDAMV--VSAGgQTFDATFPL 235
Cdd:cd08240  185 GGLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADVVVNGSDPDAAKRIIKAAGGGVDAVIdfVNNS-ATASLAFDI 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 236 MAPGGRIAVCGLMALYSMTQLPVTPdrsfmilneilLKRLTVKGSMV--LDMLntdrhvefkREMKSWIAQGVVRPVEFI 313
Cdd:cd08240  264 LAKGGKLVLVGLFGGEATLPLPLLP-----------LRALTIQGSYVgsLEEL---------RELVALAKAGKLKPIPLT 323
                        170       180
                 ....*....|....*....|....*
gi 495523457 314 TEGLENAPDALRAVFDGENIGKSVV 338
Cdd:cd08240  324 ERPLSDVNDALDDLKAGKVVGRAVL 348
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
38-330 2.34e-04

Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 42.34  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  38 EFRIR---TTWLGMDPNLFSKVKKV-SDQARPIPIGavmyGATVGRVDI--SNHPDFSVGDLVHGL--WGWQDYFISNGA 109
Cdd:cd08269   21 QVLVRvegCGVCGSDLPAFNQGRPWfVYPAEPGGPG----HEGWGRVVAlgPGVRGLAVGDRVAGLsgGAFAEYDLADAD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 110 GIFSVdndisrPSYCLG-ALGATGFGAYLVVNDVLAVKNGDTVFCSAAtGALGQMVGQISHLKGGATYgSAGTDEKCRLA 188
Cdd:cd08269   97 HAVPL------PSLLDGqAFPGEPLGCALNVFRRGWIRAGKTVAVIGA-GFIGLLFLQLAAAAGARRV-IAIDRRPARLA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 189 VSK-LGYTDCFNYKSENFERMLSDRIDG-GIDAMVVSAGGQ-TFDATFPLMAPGGRIAVCGLmALYSMTQLPvtpdrsfm 265
Cdd:cd08269  169 LAReLGATEVVTDDSEAIVERVRELTGGaGADVVIEAVGHQwPLDLAGELVAERGRLVIFGY-HQDGPRPVP-------- 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495523457 266 iLNEILLKRLTVKGSMVLdmlntDRHVEFK--REMKSWIAQGVVRPVEFIT--EGLENAPDALRAVFDG 330
Cdd:cd08269  240 -FQTWNWKGIDLINAVER-----DPRIGLEgmREAVKLIADGRLDLGSLLTheFPLEELGDAFEAARRR 302
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
130-243 7.80e-04

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 41.07  E-value: 7.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 130 ATGFGAylvvNDVLAVKNGDTVfCSAATGALGQMVGQISHLKGGATYGSAGTDEKCRLAVSKLGYTDCFNYKSENFERML 209
Cdd:cd08285  153 STGFHG----AELANIKLGDTV-AVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDIVDYKNGDVVEQI 227
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 495523457 210 SDRIDG-GIDAMVVSAGGQ-TFDATFPLMAPGGRIA 243
Cdd:cd08285  228 LKLTGGkGVDAVIIAGGGQdTFEQALKVLKPGGTIS 263
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
77-340 9.45e-04

Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 40.60  E-value: 9.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  77 VGRVDISNHPDFSVGD--LVHGlWGwqdyFISNGAGIFS------VDNDISRP----SYCLGALGATGFGAYLVVNDVLa 144
Cdd:cd05280   66 AGTVVSSDDPRFREGDevLVTG-YD----LGMNTDGGFAeyvrvpADWVVPLPeglsLREAMILGTAGFTAALSVHRLE- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 145 vKNGDT-----VFCSAATGALGQMVGQISHLKGGATYGSAGTDEKC----RLAVSKLGYTDCFNYKSEnfERMLSDRIDG 215
Cdd:cd05280  140 -DNGQTpedgpVLVTGATGGVGSIAVAILAKLGYTVVALTGKEEQAdylkSLGASEVLDREDLLDESK--KPLLKARWAG 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 216 GIDAmvvsAGGQTFDATFPLMAPGGRIAVCGLMALYSMTqLPVTPdrsFMILNEILLKRLTVKGSMvldmlNTDRHVEFK 295
Cdd:cd05280  217 AIDT----VGGDVLANLLKQTKYGGVVASCGNAAGPELT-TTVLP---FILRGVSLLGIDSVNCPM-----ELRKQVWQK 283
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 495523457 296 --REMKSWIAQGVVRPVefiteGLENAPDALRAVFDGENIGKSVVHV 340
Cdd:cd05280  284 laTEWKPDLLEIVVREI-----SLEELPEAIDRLLAGKHRGRTVVKI 325
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
38-341 2.47e-03

2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 39.24  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457  38 EFRIRTTwlgMDPNLFSKVKKVSDQARPIP-IGAVMYGATVGRVDisnhpdfSVGDLVHGLW------------GWQDYF 104
Cdd:cd08292   30 EVLVRTT---LSPIHNHDLWTIRGTYGYKPeLPAIGGSEAVGVVD-------AVGEGVKGLQvgqrvavapvhgTWAEYF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 105 ISNGAGIFSVDNDISRPSYClgALGATGFGAyLVVNDVLAVKNGDTVFCSAATGALGQMVGQISHLKGGATYG----SAG 180
Cdd:cd08292  100 VAPADGLVPLPDGISDEVAA--QLIAMPLSA-LMLLDFLGVKPGQWLIQNAAGGAVGKLVAMLAAARGINVINlvrrDAG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 181 TDEKCRLAVSKLGYTDCFNYKSENFERMLSDRIDGGIDamvvSAGGQTFDATFPLMAPGGRIAVCGLMALYSMtQLPVTP 260
Cdd:cd08292  177 VAELRALGIGPVVSTEQPGWQDKVREAAGGAPISVALD----SVGGKLAGELLSLLGEGGTLVSFGSMSGEPM-QISSGD 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 261 drsfmilneILLKRLTVKGSMVLdMLNTDRHVEFKREMkswiaqgVVRPVEFITEGLENAPDAlrAVFDGENIGKSVVHV 340
Cdd:cd08292  252 ---------LIFKQATVRGFWGG-RWSQEMSVEYRKRM-------IAELLTLALKGQLLLPVE--AVFDLGDAAKAAAAS 312

                 .
gi 495523457 341 S 341
Cdd:cd08292  313 M 313
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
145-246 4.44e-03

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 38.39  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495523457 145 VKNGDTVFCSAAtGALGQMVGQISHLKGGATYGSAGTDEKcRLAVSK-LGYTDCFNYKSENFERMLSDRIDG-GIDAmVV 222
Cdd:cd08286  164 VKPGDTVAIVGA-GPVGLAALLTAQLYSPSKIIMVDLDDN-RLEVAKkLGATHTVNSAKGDAIEQVLELTDGrGVDV-VI 240
                         90       100
                 ....*....|....*....|....*.
gi 495523457 223 SAGG--QTFDATFPLMAPGGRIAVCG 246
Cdd:cd08286  241 EAVGipATFELCQELVAPGGHIANVG 266
 
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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