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Conserved domains on  [gi|1276242734|gb|PIN03568|]
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Zinc-binding oxidoreductase [Handroanthus impetiginosus]

Protein Classification

MDR/zinc-dependent alcohol dehydrogenase-like family protein( domain architecture ID 94789)

medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family protein may catalyze the reversible NAD(P)(H)-dependent conversion of an alcohol to its corresponding aldehyde

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MDR super family cl16912
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-363 9.09e-87

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.


The actual alignment was detected with superfamily member cd08248:

Pssm-ID: 450120 [Multi-domain]  Cd Length: 350  Bit Score: 266.01  E-value: 9.09e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDDVNVPDL-KPNEVLVRARAVSVNPLDTRMRSGYGRSLF------------EPLLPVILGRDI 99
Cdd:cd08248     2 KAWQIHSYGGIDSLLLLENARIPVIrKPNQVLIKVHAASVNPIDVLMRSGYGRTLLnkkrkpqsckysGIEFPLTLGRDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 100 SGEVAAVGNSVRSLSVGQEVFGALHPtAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQ 179
Cdd:cd08248    82 SGVVVDIGSGVKSFEIGDEVWGAVPP-WSQGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 180 RVLV----VGGGGAVGFSAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDY--ELSIKGYFDAVLDTIGvPET 253
Cdd:cd08248   161 AAGKrvliLGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDVIDYNNEDFeeELTERGKFDVILDTVG-GDT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 254 EKMGVNLLKRGGHYMTLQGEAASFTDRYGLAVGLPMATAVLAKKQIQYrFSHGIDYQWTYMRADAEGLHEIRQLSEAGKL 333
Cdd:cd08248   240 EKWALKLLKKGGTYVTLVSPLLKNTDKLGLVGGMLKSAVDLLKKNVKS-LLKGSHYRWGFFSPSGSALDELAKLVEDGKI 318
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1276242734 334 KIPIERTFPIAQVREAHE---AKDKRiisGKVV 363
Cdd:cd08248   319 KPVIDKVFPFEEVPEAYEkveSGHAR---GKTV 348
 
Name Accession Description Interval E-value
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
33-363 9.09e-87

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The 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: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 266.01  E-value: 9.09e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDDVNVPDL-KPNEVLVRARAVSVNPLDTRMRSGYGRSLF------------EPLLPVILGRDI 99
Cdd:cd08248     2 KAWQIHSYGGIDSLLLLENARIPVIrKPNQVLIKVHAASVNPIDVLMRSGYGRTLLnkkrkpqsckysGIEFPLTLGRDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 100 SGEVAAVGNSVRSLSVGQEVFGALHPtAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQ 179
Cdd:cd08248    82 SGVVVDIGSGVKSFEIGDEVWGAVPP-WSQGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 180 RVLV----VGGGGAVGFSAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDY--ELSIKGYFDAVLDTIGvPET 253
Cdd:cd08248   161 AAGKrvliLGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDVIDYNNEDFeeELTERGKFDVILDTVG-GDT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 254 EKMGVNLLKRGGHYMTLQGEAASFTDRYGLAVGLPMATAVLAKKQIQYrFSHGIDYQWTYMRADAEGLHEIRQLSEAGKL 333
Cdd:cd08248   240 EKWALKLLKKGGTYVTLVSPLLKNTDKLGLVGGMLKSAVDLLKKNVKS-LLKGSHYRWGFFSPSGSALDELAKLVEDGKI 318
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1276242734 334 KIPIERTFPIAQVREAHE---AKDKRiisGKVV 363
Cdd:cd08248   319 KPVIDKVFPFEEVPEAYEkveSGHAR---GKTV 348
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
33-367 8.54e-79

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: 244.67  E-value: 8.54e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRslFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:COG0604     2 KAIVITEFGGPEVLELEE-VPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYP--LPPGLPFIPGSDAAGVVVAVGEGVTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIK---------------Q 177
Cdd:COG0604    79 FKVGDRVAGLGRG----GGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKpgetvlvhgaaggvgS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 178 GqrvlvvggggavgfsAIQLAVAAGCHVSTTCGG-ESIERILAAGAEQAVDYTTEDY-----ELSIKGYFDAVLDTIGVP 251
Cdd:COG0604   155 A---------------AVQLAKALGARVIATASSpEKAELLRALGADHVIDYREEDFaervrALTGGRGVDVVLDTVGGD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 252 ETEKMgVNLLKRGGHYMTlqgeaasftdrYGLAVG--LPMATAVLAKKQIQYrfsHGIDYQWTYMRADAEGLHEIRQLSE 329
Cdd:COG0604   220 TLARS-LRALAPGGRLVS-----------IGAASGapPPLDLAPLLLKGLTL---TGFTLFARDPAERRAALAELARLLA 284
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1276242734 330 AGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVLELD 367
Cdd:COG0604   285 AGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
33-366 3.43e-38

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 139.32  E-value: 3.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrslFEPLLP---VILGRDISGEVAAVGNS 109
Cdd:TIGR02824   2 KAIEITEPGGPEVLVLVE-VPLPVPKAGEVLIRVAAAGVNRPDLLQRAG-----KYPPPPgasDILGLEVAGEVVAVGEG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 110 VRSLSVGQEVFgALHPTavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGA 189
Cdd:TIGR02824  76 VSRWKVGDRVC-ALVAG---GGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKAGETVLIHGGASG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 190 VGFSAIQLAVAAGCHVSTTCGG-ESIERILAAGAEQAVDYTTEDYELSIK-----GYFDAVLDTIGVPETEKmGVNLLKR 263
Cdd:TIGR02824 152 IGTTAIQLAKAFGARVFTTAGSdEKCAACEALGADIAINYREEDFVEVVKaetggKGVDVILDIVGGSYLNR-NIKALAL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 264 GGHYMTL--QGeaasftdryGLAVGLPMAtAVLAKkqiqyRFSHgidyQWTYMRA-DAEGLHEIRQ--------LSEAGK 332
Cdd:TIGR02824 231 DGRIVQIgfQG---------GRKAELDLG-PLLAK-----RLTI----TGSTLRArPVAEKAAIAAelrehvwpLLASGR 291
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1276242734 333 LKIPIERTFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:TIGR02824 292 VRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
33-364 1.39e-27

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 110.89  E-value: 1.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrsLFEPLLPV--ILGRDISGEVAAVGNSV 110
Cdd:PTZ00354    3 RAVTLKGFGGVDVLKIGE-SPKPAPKRNDVLIKVSAAGVNRADTLQRQG----KYPPPPGSseILGLEVAGYVEDVGSDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 111 RSLSVGQEVFGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAV 190
Cdd:PTZ00354   78 KRFKEGDRVMALLPG----GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 191 GFSAIQLAVAAGCH-VSTTCGGESIERILAAGAEQAVDYTTEdyelsiKGYFDAVLDTIGvpeteKMGVNLLKR--GGHY 267
Cdd:PTZ00354  154 GTAAAQLAEKYGAAtIITTSSEEKVDFCKKLAAIILIRYPDE------EGFAPKVKKLTG-----EKGVNLVLDcvGGSY 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 268 MTLQGEAASFTDR---YGLAVGL---PMATAVLAKKQIQYRFS--HGIDYQWtymRAD--AEGLHEIRQLSEAGKLKIPI 337
Cdd:PTZ00354  223 LSETAEVLAVDGKwivYGFMGGAkveKFNLLPLLRKRASIIFStlRSRSDEY---KADlvASFEREVLPYMEEGEIKPIV 299
                         330       340
                  ....*....|....*....|....*..
gi 1276242734 338 ERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:PTZ00354  300 DRTYPLEEVAEAHTFLEQNKNIGKVVL 326
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
95-364 1.12e-17

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 82.05  E-value: 1.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734   95 LGRDISGEVAAVGNSVRSLSVGQEVFGAlhptaVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTAR 174
Cdd:smart00829  26 LGGECAGVVTRVGPGVTGLAVGDRVMGL-----APGAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLAR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  175 IKQGQrvlvvggggavgfS-------------AIQLAVAAGCHVSTTCG-----------GESIERILaagaeqavDYTT 230
Cdd:smart00829 101 LRPGE-------------SvlihaaaggvgqaAIQLARHLGAEVFATAGspekrdflralGIPDDHIF--------SSRD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  231 EDYELSIK----GY-FDAVLDTIGvpeTEKM--GVNLLKRGGHYMTLqgeaaSFTDRYGlAVGLPMATavlAKKQIQYrf 303
Cdd:smart00829 160 LSFADEILratgGRgVDVVLNSLS---GEFLdaSLRCLAPGGRFVEI-----GKRDIRD-NSQLAMAP---FRPNVSY-- 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276242734  304 sHGIDyqwtyMRADAEG-------LHEIRQLSEAGKLK-IPIeRTFPIAQVREA--HEAKDKRIisGKVVL 364
Cdd:smart00829 226 -HAVD-----LDALEEGpdrirelLAEVLELFAEGVLRpLPV-TVFPISDAEDAfrYMQQGKHI--GKVVL 287
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
221-364 8.77e-17

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 75.83  E-value: 8.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 221 GAEQAVDYTTEDYELSIKGY-FDAVLDTIGVPETEKmGVNLLKRGGHYmtlqgeaasftdrygLAVGLPMATAVLAKKQI 299
Cdd:pfam13602   2 GADEVIDYRTTDFVQATGGEgVDVVLDTVGGEAFEA-SLRVLPGGGRL---------------VTIGGPPLSAGLLLPAR 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276242734 300 QyRFSHGIDYQWTYMRAD--AEGLHEIRQLSEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:pfam13602  66 K-RGGRGVKYLFLFVRPNlgADILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
 
Name Accession Description Interval E-value
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
33-363 9.09e-87

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The 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: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 266.01  E-value: 9.09e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDDVNVPDL-KPNEVLVRARAVSVNPLDTRMRSGYGRSLF------------EPLLPVILGRDI 99
Cdd:cd08248     2 KAWQIHSYGGIDSLLLLENARIPVIrKPNQVLIKVHAASVNPIDVLMRSGYGRTLLnkkrkpqsckysGIEFPLTLGRDC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 100 SGEVAAVGNSVRSLSVGQEVFGALHPtAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQ 179
Cdd:cd08248    82 SGVVVDIGSGVKSFEIGDEVWGAVPP-WSQGTHAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPKN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 180 RVLV----VGGGGAVGFSAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDY--ELSIKGYFDAVLDTIGvPET 253
Cdd:cd08248   161 AAGKrvliLGGSGGVGTFAIQLLKAWGAHVTTTCSTDAIPLVKSLGADDVIDYNNEDFeeELTERGKFDVILDTVG-GDT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 254 EKMGVNLLKRGGHYMTLQGEAASFTDRYGLAVGLPMATAVLAKKQIQYrFSHGIDYQWTYMRADAEGLHEIRQLSEAGKL 333
Cdd:cd08248   240 EKWALKLLKKGGTYVTLVSPLLKNTDKLGLVGGMLKSAVDLLKKNVKS-LLKGSHYRWGFFSPSGSALDELAKLVEDGKI 318
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1276242734 334 KIPIERTFPIAQVREAHE---AKDKRiisGKVV 363
Cdd:cd08248   319 KPVIDKVFPFEEVPEAYEkveSGHAR---GKTV 348
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
33-364 6.22e-86

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: 262.50  E-value: 6.22e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELrDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd05289     2 KAVRIHEYGGPEVLEL-ADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTLPLIPGHDVAGVVVAVGPGVTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGALHPTAvRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKqgqrvlvvggggavgf 192
Cdd:cd05289    81 FKVGDEVFGMTPFTR-GGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGLK---------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 193 S----------------AIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDYE-LSIKGYFDAVLDTIGVPETEK 255
Cdd:cd05289   144 AgqtvlihgaaggvgsfAVQLAKARGARVIATASAANADFLRSLGADEVIDYTKGDFErAAAPGGVDAVLDTVGGETLAR 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 256 mGVNLLKRGGHYMTLqgeaasftdryglaVGLPMATAVLAKKQIQYRFshgidyqwTYMRADAEGLHEIRQLSEAGKLKI 335
Cdd:cd05289   224 -SLALVKPGGRLVSI--------------AGPPPAEQAAKRRGVRAGF--------VFVEPDGEQLAELAELVEAGKLRP 280
                         330       340
                  ....*....|....*....|....*....
gi 1276242734 336 PIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd05289   281 VVDRVFPLEDAAEAHERLESGHARGKVVL 309
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
33-367 8.54e-79

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: 244.67  E-value: 8.54e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRslFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:COG0604     2 KAIVITEFGGPEVLELEE-VPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYP--LPPGLPFIPGSDAAGVVVAVGEGVTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIK---------------Q 177
Cdd:COG0604    79 FKVGDRVAGLGRG----GGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALFDRGRLKpgetvlvhgaaggvgS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 178 GqrvlvvggggavgfsAIQLAVAAGCHVSTTCGG-ESIERILAAGAEQAVDYTTEDY-----ELSIKGYFDAVLDTIGVP 251
Cdd:COG0604   155 A---------------AVQLAKALGARVIATASSpEKAELLRALGADHVIDYREEDFaervrALTGGRGVDVVLDTVGGD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 252 ETEKMgVNLLKRGGHYMTlqgeaasftdrYGLAVG--LPMATAVLAKKQIQYrfsHGIDYQWTYMRADAEGLHEIRQLSE 329
Cdd:COG0604   220 TLARS-LRALAPGGRLVS-----------IGAASGapPPLDLAPLLLKGLTL---TGFTLFARDPAERRAALAELARLLA 284
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1276242734 330 AGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVLELD 367
Cdd:COG0604   285 AGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
39-364 7.92e-77

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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 239.42  E-value: 7.92e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  39 RFGGPEVLELRD-DVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEPLLPVILGRDISGEVAAVGNSVRSLSVGQ 117
Cdd:cd08267     5 RYGSPEVLLLLEvEVPIPTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPFPPIPGMDFAGEVVAVGSGVTRFKVGD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 118 EVFGALHPTAvRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVlvvggggavgF----- 192
Cdd:cd08267    85 EVFGRLPPKG-GGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQRV----------Lingas 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 193 -----SAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDYELSIKG--YFDAVLDTIG-VPETEKMGVNLLKRG 264
Cdd:cd08267   154 ggvgtFAVQIAKALGAHVTGVCSTRNAELVRSLGADEVIDYTTEDFVALTAGgeKYDVIFDAVGnSPFSLYRASLALKPG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 265 GHYMTLqgeAASFTDRYGLAVGLPMATAVLAKKqiqyrfshgidYQWTYMRADAEGLHEIRQLSEAGKLKIPIERTFPIA 344
Cdd:cd08267   234 GRYVSV---GGGPSGLLLVLLLLPLTLGGGGRR-----------LKFFLAKPNAEDLEQLAELVEEGKLKPVIDSVYPLE 299
                         330       340
                  ....*....|....*....|
gi 1276242734 345 QVREAHEAKDKRIISGKVVL 364
Cdd:cd08267   300 DAPEAYRRLKSGRARGKVVI 319
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-365 1.12e-63

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: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 205.87  E-value: 1.12e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRslFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08272     2 KALVLESFGGPEVFELRE-VPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAA--ARPPLPAILGCDVAGVVEAVGEGVTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGAlhPTAVR---GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGA 189
Cdd:cd08272    79 FRVGDEVYGC--AGGLGglqGSLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 190 VGFSAIQLAVAAGCHVSTTCGGESIERILAAGAEqAVDYTTEDYELSIKGY-----FDAVLDTIGvPETEKMGVNLLKRG 264
Cdd:cd08272   157 VGHVAVQLAKAAGARVYATASSEKAAFARSLGAD-PIIYYRETVVEYVAEHtggrgFDVVFDTVG-GETLDASFEAVALY 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 265 GHYMTlqgeaasftdrygLAVGLPMATAVLAKKQIQYRFSHGIDYQWTYMRADAEG--LHEIRQLSEAGKLKIPI-ERTF 341
Cdd:cd08272   235 GRVVS-------------ILGGATHDLAPLSFRNATYSGVFTLLPLLTGEGRAHHGeiLREAARLVERGQLRPLLdPRTF 301
                         330       340
                  ....*....|....*....|....
gi 1276242734 342 PIAQVREAHEAKDKRIISGKVVLE 365
Cdd:cd08272   302 PLEEAAAAHARLESGSARGKIVID 325
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
33-364 5.55e-51

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: 172.77  E-value: 5.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YGRslfEPLLPVILGRDISGEVAAVGNSVR 111
Cdd:cd08253     2 RAIRYHEFGAPDVLRLGD-LPVPTPGPGEVLVRVHASGVNPVDTYIRAGaYPG---LPPLPYVPGSDGAGVVEAVGEGVD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQEVFGALHPTAVR-GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAV 190
Cdd:cd08253    78 GLKVGDRVWLTNLGWGRRqGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGETVLVHGGSGAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 191 GFSAIQLAVAAGCHVSTTCG-GESIERILAAGAEQAVDYTTEDYELSIKGY-----FDAVLDTIGVPETEkMGVNLLKRG 264
Cdd:cd08253   158 GHAAVQLARWAGARVIATASsAEGAELVRQAGADAVFNYRAEDLADRILAAtagqgVDVIIEVLANVNLA-KDLDVLAPG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 265 GHYMTLqgeaASFTDRYGLAVGlPMATavlakKQIQYRFshgidyqwTYM-----RADAEGLHEIRQLSEAGKLKIPIER 339
Cdd:cd08253   237 GRIVVY----GSGGLRGTIPIN-PLMA-----KEASIRG--------VLLytatpEERAAAAEAIAAGLADGALRPVIAR 298
                         330       340
                  ....*....|....*....|....*
gi 1276242734 340 TFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08253   299 EYPLEEAAAAHEAVESGGAIGKVVL 323
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
33-364 4.94e-50

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: 170.90  E-value: 4.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygRSLFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08266     2 KAVVIRGHGGPEVLEYGD-LPEPEPGPDEVLVRVKAAALNHLDLWVRRG--MPGIKLPLPHILGSDGAGVVEAVGPGVTN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVfgALHP-------------------------TAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWR 167
Cdd:cd08266    79 VKPGQRV--VIYPgiscgrceyclagrenlcaqygilgEHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 168 ALRSTARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCHVSTTCGGE-SIERILAAGAEQAVDYTTEDY-----ELSIKGYF 241
Cdd:cd08266   157 MLVTRARLRPGETVLVHGAGSGVGSAAIQIAKLFGATVIATAGSEdKLERAKELGADYVIDYRKEDFvrevrELTGKRGV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 242 DAVLDTIGVpETEKMGVNLLKRGGHYMTLQGeaasftdryglavglpmATAVLAKKQIQYRFSHGIDYQWTYMRADAEgL 321
Cdd:cd08266   237 DVVVEHVGA-ATWEKSLKSLARGGRLVTCGA-----------------TTGYEAPIDLRHVFWRQLSILGSTMGTKAE-L 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1276242734 322 HEIRQLSEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08266   298 DEALRLVFRGKLKPVIDSVFPLEEAAEAHRRLESREQFGKIVL 340
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
33-364 1.16e-48

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: 166.85  E-value: 1.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YgrslfePLLP---VILGRDISGEVAAVGN 108
Cdd:cd05276     2 KAIVIKEPGGPEVLELGE-VPKPAPGPGEVLIRVAAAGVNRADLLQRQGlY------PPPPgasDILGLEVAGVVVAVGP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 109 SVRSLSVGQEVFGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRvlvvgggg 188
Cdd:cd05276    75 GVTGWKVGDRVCALLAG----GGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGLKAGET-------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 189 avgF-----------SAIQLAVAAGCHVSTTCGGES-IERILAAGAEQAVDYTTEDYELSIKGYF-----DAVLDTIGVP 251
Cdd:cd05276   143 ---VlihggasgvgtAAIQLAKALGARVIATAGSEEkLEACRALGADVAINYRTEDFAEEVKEATggrgvDVILDMVGGD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 252 ETEKmGVNLLKRGGHYMT--LQGeaasftdryGLAVGLPMATaVLAKkqiqyRFS-HGidyqwTYMRA-DAEGLHEIRQ- 326
Cdd:cd05276   220 YLAR-NLRALAPDGRLVLigLLG---------GAKAELDLAP-LLRK-----RLTlTG-----STLRSrSLEEKAALAAa 278
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1276242734 327 -------LSEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd05276   279 frehvwpLFASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-366 1.58e-48

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: 166.62  E-value: 1.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELrDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygRSLFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08268     2 RAVRFHQFGGPEVLRI-EELPVPAPGAGEVLIRVEAIGLNRADAMFRRG--AYIEPPPLPARLGYEAAGVVEAVGAGVTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFG-ALHPTAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAVG 191
Cdd:cd08268    79 FAVGDRVSViPAADLGQYGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 192 FSAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVDYTTEDYELSIKGY-----FDAVLDTIGVPETEKMGVNLLKRG- 264
Cdd:cd08268   159 LAAIQIANAAGATViATTRTSEKRDALLALGAAHVIVTDEEDLVAEVLRItggkgVDVVFDPVGGPQFAKLADALAPGGt 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 265 -GHYMTLQGEAASFtdryglavglPMAtAVLAKKQIQYRFSHgidyqwTYMRADAEGLHE----IRQLSEAGKLKIPIER 339
Cdd:cd08268   239 lVVYGALSGEPTPF----------PLK-AALKKSLTFRGYSL------DEITLDPEARRRaiafILDGLASGALKPVVDR 301
                         330       340
                  ....*....|....*....|....*..
gi 1276242734 340 TFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:cd08268   302 VFPFDDIVEAHRYLESGQQIGKIVVTP 328
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
33-338 2.13e-46

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: 161.21  E-value: 2.13e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLelRDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYgrslFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08249     2 KAAVLTGPGGGLLV--VVDVPVPKPGPDEVLVKVKAVALNPVDWKHQDYG----FIPSYPAILGCDFAGTVVEVGSGVTR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGALHPTAVR----GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGG 188
Cdd:cd08249    76 FKVGDRVAGFVHGGNPNdprnGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKLGLPLPPPKPSPASKG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 189 AVGF----------SAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDYELSIKGY----FDAVLDTIGVPETE 254
Cdd:cd08249   156 KPVLiwggsssvgtLAIQLAKLAGYKVITTASPKNFDLVKSLGADAVFDYHDPDVVEDIRAAtggkLRYALDCISTPESA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 255 KMGVNLLKR--GGHYMTLQGEAASFTDRYGLAVGLPMATAVLakKQIQYRFSHGIDYqWTYMradaeglheiRQLSEAGK 332
Cdd:cd08249   236 QLCAEALGRsgGGKLVSLLPVPEETEPRKGVKVKFVLGYTVF--GEIPEDREFGEVF-WKYL----------PELLEEGK 302

                  ....*..
gi 1276242734 333 LK-IPIE 338
Cdd:cd08249   303 LKpHPVR 309
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
61-319 1.17e-43

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: 152.09  E-value: 1.17e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  61 EVLVRARAVSVNPLDTRMRSGYGRslFEPLLPVILGRDISGEVAAVGNSVRSLSVGQEVFGALHP--------------- 125
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYP--PPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLgcgtcelcrelcpgg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 126 ----TAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVvggggavgF-------SA 194
Cdd:cd05188    79 gilgEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLV--------LgaggvglLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 195 IQLAVAAGCHVSTTCGGES-IERILAAGAEQAVDYTTEDYELSIK----GYFDAVLDTIGVPETEKMGVNLLKRGGHYMT 269
Cdd:cd05188   151 AQLAKAAGARVIVTDRSDEkLELAKELGADHVIDYKEEDLEEELRltggGGADVVIDAVGGPETLAQALRLLRPGGRIVV 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1276242734 270 lqgeaasftdrYGLAVGLPMATAVlakkqiQYRFSHGIDYQWTYMRADAE 319
Cdd:cd05188   231 -----------VGGTSGGPPLDDL------RRLLFKELTIIGSTGGTRED 263
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
33-364 1.22e-43

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: 153.36  E-value: 1.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrsLFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd05286     1 KAVRIHKTGGPEVLEYED-VPVPEPGPGEVLVRNTAIGVNFIDTYFRSG----LYPLPLPFVLGVEGAGVVEAVGPGVTG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGAlhptAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLvvggggavgF 192
Cdd:cd05286    76 FKVGDRVAYA----GPPGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYLLRETYPVKPGDTVL---------V 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 193 SA---------IQLAVAAGCHVSTTCGGES-IERILAAGAEQAVDYTTEDYELSIKGY-----FDAVLDTIGvPETEKMG 257
Cdd:cd05286   143 HAaaggvglllTQWAKALGATVIGTVSSEEkAELARAAGADHVINYRDEDFVERVREItggrgVDVVYDGVG-KDTFEGS 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 258 VNLLKRGGHYMTlqgeaasftdrYGLAVGL--PMATAVLAKKQIQY-RFShgidyQWTYMRADAEGLHEIRQLSEA---G 331
Cdd:cd05286   222 LDSLRPRGTLVS-----------FGNASGPvpPFDLLRLSKGSLFLtRPS-----LFHYIATREELLARAAELFDAvasG 285
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1276242734 332 KLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd05286   286 KLKVEIGKRYPLADAAQAHRDLESRKTTGKLLL 318
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
32-366 1.22e-40

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: 145.88  E-value: 1.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  32 CRAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRmRSGYGRSLFEPllPVILGRDISGEVAAVGNSVR 111
Cdd:cd08271     1 MKAWVLPKPGAALQLTLEE-IEIPGPGAGEVLVKVHAAGLNPVDWK-VIAWGPPAWSY--PHVPGVDGAGVVVAVGAKVT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQEVfgALHPTAVR-GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAV 190
Cdd:cd08271    77 GWKVGDRV--AYHASLARgGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKLRIEAGRTILITGGAGGV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 191 GFSAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDYELSIKGY-----FDAVLDTIGVPETEKmGVNLLKRGG 265
Cdd:cd08271   155 GSFAVQLAKRAGLRVITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEItggrgVDAVLDTVGGETAAA-LAPTLAFNG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 266 HYMTLQGeaasftdryglavGLPMATAVLAKKQIQYR-------FSHGIDYQWTYMRADAEGLheiRQLSEAGKLKIPIE 338
Cdd:cd08271   234 HLVCIQG-------------RPDASPDPPFTRALSVHevalgaaHDHGDPAAWQDLRYAGEEL---LELLAAGKLEPLVI 297
                         330       340
                  ....*....|....*....|....*...
gi 1276242734 339 RTFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:cd08271   298 EVLPFEQLPEALRALKDRHTRGKIVVTI 325
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
33-365 6.95e-40

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: 143.79  E-value: 6.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDDVNVPDLkPNEVLVRARAVSVNPLDTRMRSGygRSLFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08241     2 KAVVCKELGGPEDLVLEEVPPEPGA-PGEVRIRVEAAGVNFPDLLMIQG--KYQVKPPLPFVPGSEVAGVVEAVGEGVTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGAlhptAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIK---------------Q 177
Cdd:cd08241    79 FKVGDRVVAL----TGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQpgetvlvlgaaggvgL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 178 gqrvlvvggggavgfSAIQLAVAAGCHVSTTCGG-ESIERILAAGAEQAVDYTTEDYELSIKGYF-----DAVLDTIGVP 251
Cdd:cd08241   155 ---------------AAVQLAKALGARVIAAASSeEKLALARALGADHVIDYRDPDLRERVKALTggrgvDVVYDPVGGD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 252 ETEKMgVNLLKRGGHYMTLqGEAAsftdryGLAVGLPMATAVLakKQIQYrfsHGidYQW-TYMRAD----AEGLHEIRQ 326
Cdd:cd08241   220 VFEAS-LRSLAWGGRLLVI-GFAS------GEIPQIPANLLLL--KNISV---VG--VYWgAYARREpellRANLAELFD 284
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1276242734 327 LSEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVLE 365
Cdd:cd08241   285 LLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
quinone_pig3 TIGR02824
putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative ...
33-366 3.43e-38

putative NAD(P)H quinone oxidoreductase, PIG3 family; Members of this family are putative quinone oxidoreductases that belong to the broader superfamily (modeled by Pfam pfam00107) of zinc-dependent alcohol (of medium chain length) dehydrogenases and quinone oxiooreductases. The alignment shows no motif of conserved Cys residues as are found in zinc-binding members of the superfamily, and members are likely to be quinone oxidoreductases instead. A member of this family in Homo sapiens, PIG3, is induced by p53 but is otherwise uncharacterized. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274316 [Multi-domain]  Cd Length: 325  Bit Score: 139.32  E-value: 3.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrslFEPLLP---VILGRDISGEVAAVGNS 109
Cdd:TIGR02824   2 KAIEITEPGGPEVLVLVE-VPLPVPKAGEVLIRVAAAGVNRPDLLQRAG-----KYPPPPgasDILGLEVAGEVVAVGEG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 110 VRSLSVGQEVFgALHPTavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGA 189
Cdd:TIGR02824  76 VSRWKVGDRVC-ALVAG---GGYAEYVAVPAGQVLPVPEGLSLVEAAALPETFFTVWSNLFQRGGLKAGETVLIHGGASG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 190 VGFSAIQLAVAAGCHVSTTCGG-ESIERILAAGAEQAVDYTTEDYELSIK-----GYFDAVLDTIGVPETEKmGVNLLKR 263
Cdd:TIGR02824 152 IGTTAIQLAKAFGARVFTTAGSdEKCAACEALGADIAINYREEDFVEVVKaetggKGVDVILDIVGGSYLNR-NIKALAL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 264 GGHYMTL--QGeaasftdryGLAVGLPMAtAVLAKkqiqyRFSHgidyQWTYMRA-DAEGLHEIRQ--------LSEAGK 332
Cdd:TIGR02824 231 DGRIVQIgfQG---------GRKAELDLG-PLLAK-----RLTI----TGSTLRArPVAEKAAIAAelrehvwpLLASGR 291
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1276242734 333 LKIPIERTFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:TIGR02824 292 VRPVIDKVFPLEDAAQAHALMESGDHIGKIVLTV 325
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-364 3.86e-38

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: 139.26  E-value: 3.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDDVnVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLfePLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08275     1 RAVVLTGFGGLDKLKVEKEA-LPEPSSGEVRVRVEACGLNFADLMARQGLYDSA--PKPPFVPGFECAGTVEAVGEGVKD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGalhpTAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAVGF 192
Cdd:cd08275    78 FKVGDRVMG----LTRFGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQSVLVHSAAGGVGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 193 SAIQLAVAAGcHVST--TCGGESIERILAAGAEQAVDYTTEDY-----ELSIKGYfDAVLDTIGVPETEKmGVNLLKRGG 265
Cdd:cd08275   154 AAGQLCKTVP-NVTVvgTASASKHEALKENGVTHVIDYRTQDYveevkKISPEGV-DIVLDALGGEDTRK-SYDLLKPMG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 266 HYMT------LQGEAASFtdrYGLAVGLPMATAVLAKKQIQYRFS-HGIDYQWTYMRAD--AEGLHEIRQLSEAGKLKIP 336
Cdd:cd08275   231 RLVVygaanlVTGEKRSW---FKLAKKWWNRPKVDPMKLISENKSvLGFNLGWLFEEREllTEVMDKLLKLYEEGKIKPK 307
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1276242734 337 IERTFPIAQVREAHeakdKRIIS----GKVVL 364
Cdd:cd08275   308 IDSVFPFEEVGEAM----RRLQSrkniGKVVL 335
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
55-365 6.15e-37

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. 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: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 136.63  E-value: 6.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  55 PDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFepLLPVILGRDISGEVAAVGNSVRS-LSVGQEVFGA-LHPTAVRGTY 132
Cdd:cd08247    24 NCYKDNEIVVKVHAAALNPVDLKLYNSYTFHFK--VKEKGLGRDYSGVIVKVGSNVASeWKVGDEVCGIyPHPYGGQGTL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 133 ADYAIL--AED--ELTRKPESISHVEASAIPFAALTAWRALRSTARI-KQGQRVLVVGGGGAVGFSAIQLA--VAAGCHV 205
Cdd:cd08247   102 SQYLLVdpKKDkkSITRKPENISLEEAAAWPLVLGTAYQILEDLGQKlGPDSKVLVLGGSTSVGRFAIQLAknHYNIGTV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 206 STTCGGESIERILAAGAEQAVDYTTEDYELSIK---------GYFDAVLDTIG----VPETEKmgvnLLK---RGGHYMT 269
Cdd:cd08247   182 VGTCSSRSAELNKKLGADHFIDYDAHSGVKLLKpvlenvkgqGKFDLILDCVGgydlFPHINS----ILKpksKNGHYVT 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 270 LQGEA-ASFTDRYGLAVGLPMATAVLAKKQIQYRfshGIDYQWTYMRADAEGLHEIRQLSEAGKLKIPIERTFPIAQVRE 348
Cdd:cd08247   258 IVGDYkANYKKDTFNSWDNPSANARKLFGSLGLW---SYNYQFFLLDPNADWIEKCAELIADGKVKPPIDSVYPFEDYKE 334
                         330
                  ....*....|....*..
gi 1276242734 349 AHEAKDKRIISGKVVLE 365
Cdd:cd08247   335 AFERLKSNRAKGKVVIK 351
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-365 1.43e-36

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: 135.08  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDDvNVPDLKPNEVLVRARAVSVNPLDTRMRSGygRSLFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08273     2 REVVVTRRGGPEVLKVVEA-DLPEPAAGEVVVKVEASGVSFADVQMRRG--LYPDQPPLPFTPGYDLVGRVDALGSGVTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVfGALHPTavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAVGF 192
Cdd:cd08273    79 FEVGDRV-AALTRV---GGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVLIHGASGGVGQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 193 SAIQLAVAAGCHVSTTCGGESIERILAAGAEqAVDYTTEDYELS--IKGYFDAVLDTIGVPETEKmGVNLLKRGGHYMTL 270
Cdd:cd08273   155 ALLELALLAGAEVYGTASERNHAALRELGAT-PIDYRTKDWLPAmlTPGGVDVVFDGVGGESYEE-SYAALAPGGTLVCY 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 271 QGEAASFTDRYGLAVGLPMATAVLAKKQI-QYRFSHGiDYQWTYMRAD----AEGLHEIRQLSEAGKLKIPIERTFPIAQ 345
Cdd:cd08273   233 GGNSSLLQGRRSLAALGSLLARLAKLKLLpTGRRATF-YYVWRDRAEDpklfRQDLTELLDLLAKGKIRPKIAKRLPLSE 311
                         330       340
                  ....*....|....*....|
gi 1276242734 346 VREAHEAKDKRIISGKVVLE 365
Cdd:cd08273   312 VAEAHRLLESGKVVGKIVLL 331
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-366 6.96e-35

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: 130.73  E-value: 6.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YGrslFEPLLPVILGRDISGEVAAVGNSVR 111
Cdd:cd08276     2 KAWRLSGGGGLDNLKLVE-EPVPEPGPGEVLVRVHAVSLNYRDLLILNGrYP---PPVKDPLIPLSDGAGEVVAVGEGVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQEVFGALHPTAVRGTY-----------------ADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTAR 174
Cdd:cd08276    78 RFKVGDRVVPTFFPNWLDGPPtaedeasalggpidgvlAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 175 IKQGQRVLVVGGGGAVGFsAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVDYTT------EDYELSIKGYFDAVLDT 247
Cdd:cd08276   158 LKPGDTVLVQGTGGVSLF-ALQFAKAAGARViATSSSDEKLERAKALGADHVINYRTtpdwgeEVLKLTGGRGVDHVVEV 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 248 IGvPETEKMGVNLLKRGGHYMT---LQGEAASFtdrygLAVGLPMATAVLakkqiqyrfsHGIdyqWTYMRADAEGLheI 324
Cdd:cd08276   237 GG-PGTLAQSIKAVAPGGVISLigfLSGFEAPV-----LLLPLLTKGATL----------RGI---AVGSRAQFEAM--N 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1276242734 325 RQLsEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:cd08276   296 RAI-EAHRIRPVIDRVFPFEEAKEAYRYLESGSHFGKVVIRV 336
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
33-364 3.37e-34

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 128.69  E-value: 3.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPevLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YGRslfePLLPVILGRDISGEVAAVGNSVR 111
Cdd:COG1064     2 KAAVLTEPGGP--LELEE-VPRPEPGPGEVLVKVEACGVCHSDLHVAEGeWPV----PKLPLVPGHEIVGRVVAVGPGVT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQEVfgALHP-------------------------TAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAW 166
Cdd:COG1064    75 GFKVGDRV--GVGWvdscgtceycrsgrenlcengrftgYTTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 167 RALRsTARIKqgqrvlvvggggavgfSAIQLAVAAGCHVS-TTCGGESIERILAAGAEQAVDYTTEDYELSIKGY--FDA 243
Cdd:COG1064   153 RALR-RAGVGpgdrvavi-gagglghLAVQIAKALGAEVIaVDRSPEKLELARELGADHVVNSSDEDPVEAVRELtgADV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 244 VLDTIGVPETEKMGVNLLKRGGHYMTlqgeaasftdryglaVGLPMA-----TAVLAKKQIQYRFSHGIDyqwtymRADa 318
Cdd:COG1064   231 VIDTVGAPATVNAALALLRRGGRLVL---------------VGLPGGpiplpPFDLILKERSIRGSLIGT------RAD- 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1276242734 319 egLHEIRQLSEAGKLKiPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:COG1064   289 --LQEMLDLAAEGKIK-PEVETIPLEEANEALERLRAGKVRGRAVL 331
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-364 7.25e-33

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: 125.49  E-value: 7.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YGRSLFEPL----------------LPVIL 95
Cdd:cd08274     2 RAVLLTGHGGLDKLVYRDDVPVPTPAPGEVLIRVGACGVNNTDINTREGwYSTEVDGATdstgageagwwggtlsFPRIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  96 GRDISGEVAAVGNSVRSLSVGQEVfgaLHPTAVR------------------GTYADYAILAEDELTRKPESISHVEASA 157
Cdd:cd08274    82 GADIVGRVVAVGEGVDTARIGERV---LVDPSIRdppeddpadidyigserdGGFAEYTVVPAENAYPVNSPLSDVELAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 158 IPFAALTAWRALRStARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDYELSI 237
Cdd:cd08274   159 FPCSYSTAENMLER-AGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAVAGAAKEEAVRALGADTVILRDAPLLADAK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 238 ---KGYFDAVLDTIGVPETEKMgVNLLKRGGHYMTlQGEAAsftdryGLAVGLPMATAVLakKQIQYrfsHGIDYQwtyM 314
Cdd:cd08274   238 algGEPVDVVADVVGGPLFPDL-LRLLRPGGRYVT-AGAIA------GPVVELDLRTLYL--KDLTL---FGSTLG---T 301
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1276242734 315 RADAEGLheIRQLsEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08274   302 REVFRRL--VRYI-EEGEIRPVVAKTFPLSEIREAQAEFLEKRHVGKLVL 348
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
33-365 5.01e-32

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: 122.86  E-value: 5.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdvnVPDLKP--NEVLVRARAVSVNPLDTRMRSGYGRSLFEPLLPVILGRDISGEVAAVGNSV 110
Cdd:cd08244     2 RAIRLHEFGPPEVLVPED---VPDPVPgpGQVRIAVAAAGVHFVDTQLRSGWGPGPFPPELPYVPGGEVAGVVDAVGPGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 111 RSLSVGQEVFGALHPTAvrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRsTARIKQGQRVLVVGGGGAV 190
Cdd:cd08244    79 DPAWLGRRVVAHTGRAG--GGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTALGLLD-LATLTPGDVVLVTAAAGGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 191 GFSAIQLAVAAGCHVSTTCGGES-IERILAAGAEQAVDYTTEDY-----ELSIKGYFDAVLDTIGVPeTEKMGVNLLKRG 264
Cdd:cd08244   156 GSLLVQLAKAAGATVVGAAGGPAkTALVRALGADVAVDYTRPDWpdqvrEALGGGGVTVVLDGVGGA-IGRAALALLAPG 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 265 GHYMTlqgeaasftdrYGLAVGL--PMATAVLAKKQIQYRFSHGIDYQWTYMRADAEglheiRQLSEA--GKLKIPIERT 340
Cdd:cd08244   235 GRFLT-----------YGWASGEwtALDEDDARRRGVTVVGLLGVQAERGGLRALEA-----RALAEAaaGRLVPVVGQT 298
                         330       340
                  ....*....|....*....|....*
gi 1276242734 341 FPIAQVREAHEAKDKRIISGKVVLE 365
Cdd:cd08244   299 FPLERAAEAHAALEARSTVGKVLLL 323
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
33-364 1.39e-27

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 110.89  E-value: 1.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrsLFEPLLPV--ILGRDISGEVAAVGNSV 110
Cdd:PTZ00354    3 RAVTLKGFGGVDVLKIGE-SPKPAPKRNDVLIKVSAAGVNRADTLQRQG----KYPPPPGSseILGLEVAGYVEDVGSDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 111 RSLSVGQEVFGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAV 190
Cdd:PTZ00354   78 KRFKEGDRVMALLPG----GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQSVLIHAGASGV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 191 GFSAIQLAVAAGCH-VSTTCGGESIERILAAGAEQAVDYTTEdyelsiKGYFDAVLDTIGvpeteKMGVNLLKR--GGHY 267
Cdd:PTZ00354  154 GTAAAQLAEKYGAAtIITTSSEEKVDFCKKLAAIILIRYPDE------EGFAPKVKKLTG-----EKGVNLVLDcvGGSY 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 268 MTLQGEAASFTDR---YGLAVGL---PMATAVLAKKQIQYRFS--HGIDYQWtymRAD--AEGLHEIRQLSEAGKLKIPI 337
Cdd:PTZ00354  223 LSETAEVLAVDGKwivYGFMGGAkveKFNLLPLLRKRASIIFStlRSRSDEY---KADlvASFEREVLPYMEEGEIKPIV 299
                         330       340
                  ....*....|....*....|....*..
gi 1276242734 338 ERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:PTZ00354  300 DRTYPLEEVAEAHTFLEQNKNIGKVVL 326
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
33-363 2.19e-27

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 110.01  E-value: 2.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLfepLLPVILGRDISGEVAAVGNSvrS 112
Cdd:cd08243     2 KAIVIEQPGGPEVLKLRE-IPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSV---KFPRVLGIEAVGEVEEAPGG--T 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVF---GALHPTaVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGA 189
Cdd:cd08243    76 FTPGQRVAtamGGMGRT-FDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWGSLFRSLGLQPGDTLLIRGGTSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 190 VGFSAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVdytTEDYELS-----IKGYFDAVLDTIGVPeTEKMGVNLLKR 263
Cdd:cd08243   155 VGLAALKLAKALGATVtATTRSPERAALLKELGADEVV---IDDGAIAeqlraAPGGFDKVLELVGTA-TLKDSLRHLRP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 264 GGHY-MT-LQGEAASFTDRYglavglPMatAVLAKKQIQYRFSHGIDYqwtymrADAEGLHEIRQLSEAGKLKIPIERTF 341
Cdd:cd08243   231 GGIVcMTgLLGGQWTLEDFN------PM--DDIPSGVNLTLTGSSSGD------VPQTPLQELFDFVAAGHLDIPPSKVF 296
                         330       340
                  ....*....|....*....|..
gi 1276242734 342 PIAQVREAHEAKDKRIISGKVV 363
Cdd:cd08243   297 TFDEIVEAHAYMESNRAFGKVV 318
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
39-364 9.99e-27

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: 108.49  E-value: 9.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  39 RFGGPEVLELR-DDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEPllPVILGRDISGEVAAVGNSVRSLSVGQ 117
Cdd:cd08254     5 RFHKGSKGLLVlEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGGVPTLTKL--PLTLGHEIAGTVVEVGAGVTNFKVGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 118 EV--FGALHPTAVR---------------------GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTAR 174
Cdd:cd08254    83 RVavPAVIPCGACAlcrrgrgnlclnqgmpglgidGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 175 IKQGQRVLVvGGGGAVGFSAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVD----YTTEDYELSIKGYFDAVLDTIG 249
Cdd:cd08254   163 VKPGETVLV-IGLGGLGLNAVQIAKAMGAAViAVDIKEEKLELAKELGADEVLNslddSPKDKKAAGLGGGFDVIFDFVG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 250 VPETEKMGVNLLKRGGHYmtlqgeaasftdrygLAVGLPMA-----TAVLAKKQIQYRFSHGidyqwtymrADAEGLHEI 324
Cdd:cd08254   242 TQPTFEDAQKAVKPGGRI---------------VVVGLGRDkltvdLSDLIARELRIIGSFG---------GTPEDLPEV 297
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1276242734 325 RQLSEAGKLKIPIErTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08254   298 LDLIAKGKLDPQVE-TRPLDEIPEVLERLHKGKVKGRVVL 336
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
51-365 2.39e-26

Arginate lyase and other MDR family members; This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. 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: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 107.23  E-value: 2.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  51 DVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEpllPVILGRDISGEVAAVGNSVRSLSVGQEVFGALHPTavR- 129
Cdd:cd08252    22 ELPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQ---PKILGWDASGVVEAVGSEVTLFKVGDEVYYAGDIT--Rp 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 130 GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVggggavgfS-------------AIQ 196
Cdd:cd08252    97 GSNAEYQLVDERIVGHKPKSLSFAEAAALPLTSLTAWEALFDRLGISEDAENEGK--------TlliiggaggvgsiAIQ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 197 LAVAAGC-HVSTTCG-GESIERILAAGAEQAVDY-------------TTEDYELS---IKGYFDAVLD------TIGVPE 252
Cdd:cd08252   169 LAKQLTGlTVIATASrPESIAWVKELGADHVINHhqdlaeqlealgiEPVDYIFCltdTDQHWDAMAEliapqgHICLIV 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 253 TEKMGVNLlkrgghyMTLQGEAASFTDRYglavglpMATAVLakkqiqyrfshgidYQWTYMRADAEGLHEIRQLSEAGK 332
Cdd:cd08252   249 DPQEPLDL-------GPLKSKSASFHWEF-------MFTRSM--------------FQTPDMIEQHEILNEVADLLDAGK 300
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1276242734 333 LKIPIERTF-PI--AQVREAHEA-KDKRIIsGKVVLE 365
Cdd:cd08252   301 LKTTLTETLgPInaENLREAHALlESGKTI-GKIVLE 336
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
54-364 2.88e-26

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: 106.36  E-value: 2.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  54 VPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLfePLLPVILGRDISGEVAAVGNSVRSLSVGQEVFGALHPTAvrGTYA 133
Cdd:cd08251     2 VAPPGPGEVRIQVRAFSLNFGDLLCVRGLYPTM--PPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGTGESM--GGHA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 134 DYAILAEDELTRKPESISHVEASAIPFAALTAWRALRStARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCHVSTTCGG-E 212
Cdd:cd08251    78 TLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFAR-AGLAKGEHILIQTATGGTGLMAVQLARLKGAEIYATASSdD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 213 SIERILAAGAEQAVDYTTEDYELSIKGY-----FDAVLDTIGVPETEKmGVNLLKRGGHYMTLQgeaasftdRYGLAVGL 287
Cdd:cd08251   157 KLEYLKQLGVPHVINYVEEDFEEEIMRLtggrgVDVVINTLSGEAIQK-GLNCLAPGGRYVEIA--------MTALKSAP 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 288 PMATAVLAKKQiqyRFsHGIDYQWTYMRAD---AEGLHEIRQLSEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08251   228 SVDLSVLSNNQ---SF-HSVDLRKLLLLDPefiADYQAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
39-365 1.00e-24

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: 102.74  E-value: 1.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  39 RFGGPE--VLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YGRSlfePLLPVILGRDISGEVAAVGNSVRSLSV 115
Cdd:cd05282     5 QFGEPLplVLELVS-LPIPPPGPGEVLVRMLAAPINPSDLITISGaYGSR---PPLPAVPGNEGVGVVVEVGSGVSGLLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 116 GQEVFgalhPTAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAVGFSAI 195
Cdd:cd05282    81 GQRVL----PLGGEGTWQEYVVAPADDLIPVPDSISDEQAAMLYINPLTAWLMLTEYLKLPPGDWVIQNAANSAVGRMLI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 196 QLAVAAGCH-VSTTCGGESIERILAAGAEQAVDYTTEDYELSIK-----GYFDAVLDTIGVPETEKMgVNLLKRGGHYMT 269
Cdd:cd05282   157 QLAKLLGFKtINVVRRDEQVEELKALGADEVIDSSPEDLAQRVKeatggAGARLALDAVGGESATRL-ARSLRPGGTLVN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 270 lqgeaasftdrYGLAVGLPMATAVLAKKQIQYRFSHGIDYQWTYMRADAEGLH---EIRQLSEAGKLKIPIERTFPIAQV 346
Cdd:cd05282   236 -----------YGLLSGEPVPFPRSVFIFKDITVRGFWLRQWLHSATKEAKQEtfaEVIKLVEAGVLTTPVGAKFPLEDF 304
                         330
                  ....*....|....*....
gi 1276242734 347 REAHEAKDKRIISGKVVLE 365
Cdd:cd05282   305 EEAVAAAEQPGRGGKVLLT 323
PRK10754 PRK10754
NADPH:quinone reductase;
41-364 1.01e-24

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 102.89  E-value: 1.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  41 GGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrsLFEP-LLPVILGRDISGEVAAVGNSVRSLSVGQEV 119
Cdd:PRK10754   11 GGPEVLQAVE-FTPADPAENEVQVENKAIGINYIDTYIRSG----LYPPpSLPSGLGTEAAGVVSKVGSGVKHIKVGDRV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 120 FGALHPTavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAVGFSAIQLAV 199
Cdd:PRK10754   86 VYAQSAL---GAYSSVHNVPADKAAILPDAISFEQAAASFLKGLTVYYLLRKTYEIKPDEQFLFHAAAGGVGLIACQWAK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 200 AAGCHVSTTCGG-ESIERILAAGAEQAVDYTTED-----YELSIKGYFDAVLDTIGvPETEKMGVNLLKRgghymtlQGE 273
Cdd:PRK10754  163 ALGAKLIGTVGSaQKAQRAKKAGAWQVINYREENivervKEITGGKKVRVVYDSVG-KDTWEASLDCLQR-------RGL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 274 AASFTDRYGLAVGLPMatAVLAKKQIQYRFSHGIDYQWTYMRADAEGLHEIRQLSEAGKLK--IPIERTFPIAQVREAHE 351
Cdd:PRK10754  235 MVSFGNASGPVTGVNL--GILNQKGSLYVTRPSLQGYITTREELTEASNELFSLIASGVIKvdVAEQQKFPLKDAQRAHE 312
                         330
                  ....*....|...
gi 1276242734 352 AKDKRIISGKVVL 364
Cdd:PRK10754  313 ILESRATQGSSLL 325
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
33-358 2.03e-24

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. 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: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 102.04  E-value: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGgPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGrslFEPLlPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08264     2 KALVFEKSG-IENLKVED-VKDPKPGPGEVLIRVKMAGVNPVDYNVINAVK---VKPM-PHIPGAEFAGVVEEVGDHVKG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVF-----------------------GALHPTAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRAL 169
Cdd:cd08264    76 VKKGDRVVvynrvfdgtcdmclsgnemlcrnGGIIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 170 RsTARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCHVSTTCGGESIERilaAGAEQAVDY-TTEDYELSIKGYFDAVLDTI 248
Cdd:cd08264   156 K-TAGLGPGETVVVFGASGNTGIFAVQLAKMMGAEVIAVSRKDWLKE---FGADEVVDYdEVEEKVKEITKMADVVINSL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 249 GVPETEKmGVNLLKRGGHYMTlqgeaasftdrYGLAVG--LPMATAVLAKKQIQYRFSHGIDyqwtymRADAEGLHEIrq 326
Cdd:cd08264   232 GSSFWDL-SLSVLGRGGRLVT-----------FGTLTGgeVKLDLSDLYSKQISIIGSTGGT------RKELLELVKI-- 291
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1276242734 327 lseAGKLKIPIERTFPIAQVREA-----HEAKDKRII 358
Cdd:cd08264   292 ---AKDLKVKVWKTFKLEEAKEAlkelfSKERDGRIL 325
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
33-364 1.69e-23

D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related alcohol dehydrogenases. AraDH is a member of the medium chain dehydrogenase/reductase family and catalyzes the NAD(P)-dependent oxidation of D-arabinose and other pentoses, the initial step in the metabolism of d-arabinose into 2-oxoglutarate. Like the alcohol dehydrogenases, AraDH binds a zinc in the catalytic cleft as well as a distal structural zinc. AraDH forms homotetramers as a dimer of dimers. AraDH replaces a conserved catalytic His with replace with Arg, compared to the canonical ADH site. 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: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 99.56  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd05284     2 KAARLYEYGKPLRLE---DVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGILPYKLPFTLGHENAGWVEEVGSGVDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVfgALHPT-------AVR------------------GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWR 167
Cdd:cd05284    79 LKEGDPV--VVHPPwgcgtcrYCRrgeenycenarfpgigtdGGFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 168 ALRSTARIKQGQRVLVVGGGGAVGFSAIQL--AVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDYEL-----SIKGy 240
Cdd:cd05284   157 AVKKALPYLDPGSTVVVIGVGGLGHIAVQIlrALTPATVIAVDRSEEALKLAERLGADHVLNASDDVVEEvreltGGRG- 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 241 FDAVLDTIGVPETEKMGVNLLKRGGHYmTLQGeaasftdrYGLAVGLPmatavlakkqiqyrFSHGIDYQWTYM------ 314
Cdd:cd05284   236 ADAVIDFVGSDETLALAAKLLAKGGRY-VIVG--------YGGHGRLP--------------TSDLVPTEISVIgslwgt 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1276242734 315 RADaegLHEIRQLSEAGKLKIPIERtFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd05284   293 RAE---LVEVVALAESGKVKVEITK-FPLEDANEALDRLREGRVTGRAVL 338
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
33-364 1.52e-20

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: 91.22  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLfepLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08259     2 KAAILHKPNKPLQIE---EVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRG---KYPLILGHEIVGTVEEVGEGVER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFG-----------------------ALHPTAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRAL 169
Cdd:cd08259    76 FKPGDRVILyyyipcgkceyclsgeenlcrnrAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAVHAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 170 RsTARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVDYTTEDYELSIKGYFDAVLDTI 248
Cdd:cd08259   156 K-RAGVKKGDTVLVTGAGGGVGIHAIQLAKALGARViAVTRSPEKLKILKELGADYVIDGSKFSEDVKKLGGADVVIELV 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 249 GVPETEKmGVNLLKRGGHyMTLQGEAAsftdryGLAVGLPMATAVLakKQIQYRFSHGidyqwtYMRADAEglhEIRQLS 328
Cdd:cd08259   235 GSPTIEE-SLRSLNKGGR-LVLIGNVT------PDPAPLRPGLLIL--KEIRIIGSIS------ATKADVE---EALKLV 295
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1276242734 329 EAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08259   296 KEGKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVL 331
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
60-212 2.63e-20

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: 89.55  E-value: 2.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  60 NEVLVRARAVSVNPLDTRMRSGygrslFEPLLPVILGRDISGEVAAVGNSVRSLSVGQEVFGALHptavrGTYADYAILA 139
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVALG-----LLPGDETPLGLECSGIVTRVGSGVTGLKVGDRVMGLAP-----GAFATHVRVD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 140 EDELTRKPESISHVEASAIPFAALTAWRALRSTARIK---------------QgqrvlvvggggavgfSAIQLAVAAGCH 204
Cdd:cd05195    71 ARLVVKIPDSLSFEEAATLPVAYLTAYYALVDLARLQkgesvlihaaaggvgQ---------------AAIQLAQHLGAE 135

                  ....*...
gi 1276242734 205 VSTTCGGE 212
Cdd:cd05195   136 VFATVGSE 143
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
33-363 9.26e-20

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: 88.92  E-value: 9.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPevLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGrslFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08245     1 KAAVVHAAGGP--LEPEE-VPVPEPGPGEVLIKIEACGVCHTDLHAAEGDW---GGSKYPLVPGHEIVGEVVEVGAGVEG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQ---------------------EVFGA---LHPTAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRA 168
Cdd:cd08245    75 RKVGDrvgvgwlvgscgrceycrrglENLCQkavNTGYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 169 LRSTAriKQGQRVLVVGGGGAVGFSAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVDYTTEDYELSIKGYFDAVLDT 247
Cdd:cd08245   155 LRDAG--PRPGERVAVLGIGGLGHLAVQYARAMGFETvAITRSPDKRELARKLGADEVVDSGAELDEQAAAGGADVILVT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 248 IGVPETEKMGVNLLKRGGHyMTLQGEAASftdryglAVGLPMATAVLAK-KQIQYRFSHGIDYqwtymradaegLHEIRQ 326
Cdd:cd08245   233 VVSGAAAEAALGGLRRGGR-IVLVGLPES-------PPFSPDIFPLIMKrQSIAGSTHGGRAD-----------LQEALD 293
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1276242734 327 LSEAGKLKIPIErTFPIAQVREAHEakdkRIISGKVV 363
Cdd:cd08245   294 FAAEGKVKPMIE-TFPLDQANEAYE----RMEKGDVR 325
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
95-364 1.12e-17

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 82.05  E-value: 1.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734   95 LGRDISGEVAAVGNSVRSLSVGQEVFGAlhptaVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTAR 174
Cdd:smart00829  26 LGGECAGVVTRVGPGVTGLAVGDRVMGL-----APGAFATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLAR 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  175 IKQGQrvlvvggggavgfS-------------AIQLAVAAGCHVSTTCG-----------GESIERILaagaeqavDYTT 230
Cdd:smart00829 101 LRPGE-------------SvlihaaaggvgqaAIQLARHLGAEVFATAGspekrdflralGIPDDHIF--------SSRD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  231 EDYELSIK----GY-FDAVLDTIGvpeTEKM--GVNLLKRGGHYMTLqgeaaSFTDRYGlAVGLPMATavlAKKQIQYrf 303
Cdd:smart00829 160 LSFADEILratgGRgVDVVLNSLS---GEFLdaSLRCLAPGGRFVEI-----GKRDIRD-NSQLAMAP---FRPNVSY-- 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1276242734  304 sHGIDyqwtyMRADAEG-------LHEIRQLSEAGKLK-IPIeRTFPIAQVREA--HEAKDKRIisGKVVL 364
Cdd:smart00829 226 -HAVD-----LDALEEGpdrirelLAEVLELFAEGVLRpLPV-TVFPISDAEDAfrYMQQGKHI--GKVVL 287
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
32-364 2.91e-17

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: 81.88  E-value: 2.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  32 CRAVLLPRFGGP-EVLELRDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSL--FEPLLPVILGRDISGEVAAVGN 108
Cdd:cd08290     1 AKALVYTEHGEPkEVLQLESYEIPPPGPPNEVLVKMLAAPINPADINQIQGVYPIKppTTPEPPAVGGNEGVGEVVKVGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 109 SVRSLSVGQEVFGALHPtavRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIK------------ 176
Cdd:cd08290    81 GVKSLKPGDWVIPLRPG---LGTWRTHAVVPADDLIKVPNDVDPEQAATLSVNPCTAYRLLEDFVKLQpgdwviqngans 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 177 ---QgqrvlvvggggavgfSAIQLAVAAGCHVSTTC-----GGESIERILAAGAEQAVdytTEDyELSIKGYFDAV---- 244
Cdd:cd08290   158 avgQ---------------AVIQLAKLLGIKTINVVrdrpdLEELKERLKALGADHVL---TEE-ELRSLLATELLksap 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 245 -------LDTIGVPETEKMgVNLLKRGGHYMTlqgeaasftdrYGL----AVGLPmaTAVLAKKQIQYR-FSHGidyQWT 312
Cdd:cd08290   219 ggrpklaLNCVGGKSATEL-ARLLSPGGTMVT-----------YGGmsgqPVTVP--TSLLIFKDITLRgFWLT---RWL 281
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1276242734 313 YMR---ADAEGLHEIRQLSEAGKLKIP---IERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08290   282 KRAnpeEKEDMLEELAELIREGKLKAPpveKVTDDPLEEFKDALANALKGGGGGKQVL 339
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
33-367 4.01e-17

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: 81.34  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPrfgGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGyGRSLFEPllPVILGRDISGEVAAVGNSVRS 112
Cdd:COG1063     2 KALVLH---GPGDLRLEE-VPDPEPGPGEVLVRVTAVGICGSDLHIYRG-GYPFVRP--PLVLGHEFVGEVVEVGEGVTG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEV---------------------------FGALHptaVRGTYADYAILAEDELTRKPESISHVEASAI-PFAalT 164
Cdd:COG1063    75 LKVGDRVvvepnipcgecrycrrgrynlcenlqfLGIAG---RDGGFAEYVRVPAANLVKVPDGLSDEAAALVePLA--V 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 165 AWRALRStARIK--------------QgqrvlvvggggavgfSAIQLAVAAGCHVSTTCGG--ESIERILAAGAEQAVDY 228
Cdd:COG1063   150 ALHAVER-AGVKpgdtvlvigagpigL---------------LAALAARLAGAARVIVVDRnpERLELARELGADAVVNP 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 229 TTEDYELSIK----GY-FDAVLDTIGVPETEKMGVNLLKRGGHYmtlqgeaaSFTDRYGLAVGLPMATAVLakKQIQYRF 303
Cdd:COG1063   214 REEDLVEAVReltgGRgADVVIEAVGAPAALEQALDLVRPGGTV--------VLVGVPGGPVPIDLNALVR--KELTLRG 283
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276242734 304 SHGidYQWTYMRadaeglhEIRQLSEAGKLKIP--IERTFPIAQVREA-HEAKDKRIISGKVVLELD 367
Cdd:COG1063   284 SRN--YTREDFP-------EALELLASGRIDLEplITHRFPLDDAPEAfEAAADRADGAIKVVLDPD 341
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
221-364 8.77e-17

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 75.83  E-value: 8.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 221 GAEQAVDYTTEDYELSIKGY-FDAVLDTIGVPETEKmGVNLLKRGGHYmtlqgeaasftdrygLAVGLPMATAVLAKKQI 299
Cdd:pfam13602   2 GADEVIDYRTTDFVQATGGEgVDVVLDTVGGEAFEA-SLRVLPGGGRL---------------VTIGGPPLSAGLLLPAR 65
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276242734 300 QyRFSHGIDYQWTYMRAD--AEGLHEIRQLSEAGKLKIPIERTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:pfam13602  66 K-RGGRGVKYLFLFVRPNlgADILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
33-364 9.14e-17

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: 80.07  E-value: 9.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPE-VLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YGrslFEPLLPVILGRDISGEVAAVGNSV 110
Cdd:cd08292     2 RAAVHTQFGDPAdVLEIGE-VPKPTPGAGEVLVRTTLSPIHNHDLWTIRGtYG---YKPELPAIGGSEAVGVVDAVGEGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 111 RSLSVGQEVFGAlhptAVRGTYADYAILAEDELTRKPESISHVEAS---AIPFAALTAWRALrstaRIKQGQRVLVVGGG 187
Cdd:cd08292    78 KGLQVGQRVAVA----PVHGTWAEYFVAPADGLVPLPDGISDEVAAqliAMPLSALMLLDFL----GVKPGQWLIQNAAG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 188 GAVGFSAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVDYTTEDYELSIKGYFD-----AVLDTIGVPETEKMgVNLL 261
Cdd:cd08292   150 GAVGKLVAMLAAARGINViNLVRRDAGVAELRALGIGPVVSTEQPGWQDKVREAAGgapisVALDSVGGKLAGEL-LSLL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 262 KRGGHYMTlqgeaasftdrYGLAVGLPMATAV--LAKKQIQYR-FSHGIDYQWTYMRADAEGLHEIRQLSEAGKLKIPIE 338
Cdd:cd08292   229 GEGGTLVS-----------FGSMSGEPMQISSgdLIFKQATVRgFWGGRWSQEMSVEYRKRMIAELLTLALKGQLLLPVE 297
                         330       340
                  ....*....|....*....|....*.
gi 1276242734 339 RTFPIAQVREAHEAKDKRIISGKVVL 364
Cdd:cd08292   298 AVFDLGDAAKAAAASMRPGRAGKVLL 323
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
42-364 1.03e-16

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: 80.35  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  42 GPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFepllPVILGRDISGEVAAVGNSVRSLSVGQEV-- 119
Cdd:cd08236     8 GPGDLRYED-IPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAYHP----PLVLGHEFSGTVEEVGSGVDDLAVGDRVav 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 120 -------------------------FGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAAlTAWRALRStAR 174
Cdd:cd08236    83 npllpcgkceyckkgeyslcsnydyIGSRRD----GAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAA-VALHAVRL-AG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 175 IKQGQRVLVVGGGGAVGFsAIQLAVAAGC-HVSTTC-GGESIERILAAGAEQAVDYTTEDYELSIK----GYFDAVLDTI 248
Cdd:cd08236   157 ITLGDTVVVIGAGTIGLL-AIQWLKILGAkRVIAVDiDDEKLAVARELGADDTINPKEEDVEKVREltegRGADLVIEAA 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 249 GVPETEKMGVNLLKRGGHYMtlqgeaasftdryglAVGLPMATAVLAKKQIQYRFSHGIDYQ--WTYMRADAEG--LHEI 324
Cdd:cd08236   236 GSPATIEQALALARPGGKVV---------------LVGIPYGDVTLSEEAFEKILRKELTIQgsWNSYSAPFPGdeWRTA 300
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1276242734 325 RQLSEAGKLKIP--IERTFPIAQVREAHEA-KDKRIISGKVVL 364
Cdd:cd08236   301 LDLLASGKIKVEplITHRLPLEDGPAAFERlADREEFSGKVLL 343
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
33-364 6.63e-16

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: 78.04  E-value: 6.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPevLELrDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGY------GRSLFE---PLLPVILGRDISGEV 103
Cdd:cd08240     2 KAAAVVEPGKP--LEE-VEIDTPKPPGTEVLVKVTACGVCHSDLHIWDGGydlgggKTMSLDdrgVKLPLVLGHEIVGEV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 104 AAVGNSVRSLSVGQEVfgALHP-------------------------TAVRGTYADYAILAEDELTRKPESISHVEASAI 158
Cdd:cd08240    79 VAVGPDAADVKVGDKV--LVYPwigcgecpvclagdenlcakgralgIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 159 PFAALTAWRALRStarikqgqRVLVVGGGGAVGFSA-------IQLAVAAGcHVSTTC---GGESIERILAAGAEQAVDY 228
Cdd:cd08240   157 ACSGLTAYSAVKK--------LMPLVADEPVVIIGAgglglmaLALLKALG-PANIIVvdiDEAKLEAAKAAGADVVVNG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 229 TTEDYELSIK----GYFDAVLDTIGVPETEKMGVNLLKRGGHYMT--LQGEAASFtdryglavglPMATAVLAKKQIQyr 302
Cdd:cd08240   228 SDPDAAKRIIkaagGGVDAVIDFVNNSATASLAFDILAKGGKLVLvgLFGGEATL----------PLPLLPLRALTIQ-- 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276242734 303 fshGidyqwTYMRADAEgLHEIRQLSEAGKLK-IPIErTFPIAQVREA-HEAKDKRIIsGKVVL 364
Cdd:cd08240   296 ---G-----SYVGSLEE-LRELVALAKAGKLKpIPLT-ERPLSDVNDAlDDLKAGKVV-GRAVL 348
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
32-366 7.44e-16

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) 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: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 77.57  E-value: 7.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  32 CRAVLLPRFGGPEVLelRDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLfePLLPVILGRDISGEVAAVGNSVR 111
Cdd:cd08297     1 MKAAVVEEFGEKPYE--VKDVPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPVK--PKLPLIGGHEGAGVVVAVGPGVS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQEV-----FGA---------LHPT----------AVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWR 167
Cdd:cd08297    77 GLKVGDRVgvkwlYDAcgkceycrtGDETlcpnqknsgyTVDGTFAEYAIADARYVTPIPDGLSFEQAAPLLCAGVTVYK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 168 ALRST-ARIKQgqrvlvvggggAVGFS---------AIQLAVAAGCHVSTTCGGESIERI-LAAGAEQAVDYTTEDYELS 236
Cdd:cd08297   157 ALKKAgLKPGD-----------WVVISgaggglghlGVQYAKAMGLRVIAIDVGDEKLELaKELGADAFVDFKKSDDVEA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 237 IKGYF-----DAVLDTIGVPETEKMGVNLLKRGGhymTLqgeaasftdrygLAVGLPmatavlAKKQIQyrfshgIDYQW 311
Cdd:cd08297   226 VKELTggggaHAVVVTAVSAAAYEQALDYLRPGG---TL------------VCVGLP------PGGFIP------LDPFD 278
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276242734 312 TYMRadaeGLHEI-------RQLSEA------GKLKIPIErTFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:cd08297   279 LVLR----GITIVgslvgtrQDLQEAlefaarGKVKPHIQ-VVPLEDLNEVFEKMEEGKIAGRVVVDF 341
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
33-354 7.98e-16

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 has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. 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: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 77.64  E-value: 7.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPevLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSlfePLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08260     2 RAAVYEEFGEP--LEIRE-VPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPD---VTLPHVPGHEFAGVVVEVGEDVSR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVG---------------------------QEVFGALHPtavrGTYADYAIL--AEDELTRKPESISHVEASAIPFAAL 163
Cdd:cd08260    76 WRVGdrvtvpfvlgcgtcpycragdsnvcehQVQPGFTHP----GSFAEYVAVprADVNLVRLPDDVDFVTAAGLGCRFA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 164 TAWRALRSTARIKQGQRVLVvGGGGAVGFSAIQLAVAAGCHV-STTCGGESIERILAAGAEQAVDYTTED------YELS 236
Cdd:cd08260   152 TAFRALVHQARVKPGEWVAV-HGCGGVGLSAVMIASALGARViAVDIDDDKLELARELGAVATVNASEVEdvaaavRDLT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 237 iKGYFDAVLDTIGVPETEKMGVNLLKRGGHY----MTLQGEAasftdryglAVGLPMATAVLakKQIQYRFSHGI---DY 309
Cdd:cd08260   231 -GGGAHVSVDALGIPETCRNSVASLRKRGRHvqvgLTLGEEA---------GVALPMDRVVA--RELEIVGSHGMpahRY 298
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1276242734 310 QwtymradaeglhEIRQLSEAGKLKIP--IERTFPIAQVREAHEAKD 354
Cdd:cd08260   299 D------------AMLALIASGKLDPEplVGRTISLDEAPDALAAMD 333
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
51-250 5.84e-15

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: 74.99  E-value: 5.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  51 DVNVPDLKPNEVLVRARAVSVNPLDTRMRSG-YGRSlfePLLPVILGRDISGEVAAVGNSVRSLSVGQEVfgalhPTAVR 129
Cdd:cd08250    22 DVPVPLPGPGEVLVKNRFVGINASDINFTAGrYDPG---VKPPFDCGFEGVGEVVAVGEGVTDFKVGDAV-----ATMSF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 130 GTYADYAILAEDELTRKPESIShvEASAIPFAALTAWRALRSTARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCHVSTTC 209
Cdd:cd08250    94 GAFAEYQVVPARHAVPVPELKP--EVLPLLVSGLTASIALEEVGEMKSGETVLVTAAAGGTGQFAVQLAKLAGCHVIGTC 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1276242734 210 GGESIERILAA-GAEQAVDYTTED----------------YElSIKG-YFDAVLDTIGV 250
Cdd:cd08250   172 SSDEKAEFLKSlGCDRPINYKTEDlgevlkkeypkgvdvvYE-SVGGeMFDTCVDNLAL 229
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
39-363 4.84e-14

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: 72.17  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  39 RFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrsLFEPLLPVILGRDISGEVAAVGNSVRSLSVGQE 118
Cdd:cd08234     5 VYEGPGELEVEE-VPVPEPGPDEVLIKVAACGICGTDLHIYEG----EFGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 119 V------------------------FGALHPTaVRGTYADYAILAEDELTRKPESISHVEASAI-PFA-ALTAWRALR-- 170
Cdd:cd08234    80 VavdpniycgecfycrrgrpnlcenLTAVGVT-RNGGFAEYVVVPAKQVYKIPDNLSFEEAALAePLScAVHGLDLLGik 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 171 --STARIkqgqrvlvvggggavgFSA-------IQLAVAAGCHVSTTCGGESIERILAA--GAEQAVDYTTEDYELSIKG 239
Cdd:cd08234   159 pgDSVLV----------------FGAgpiglllAQLLKLNGASRVTVAEPNEEKLELAKklGATETVDPSREDPEAQKED 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 240 Y---FDAVLDTIGVPETEKMGVNLLKRGGHYMT--LQGEAASFTdryglavglpMATAVLAKKQIQYRFSHGIDYqwTYM 314
Cdd:cd08234   223 NpygFDVVIEATGVPKTLEQAIEYARRGGTVLVfgVYAPDARVS----------ISPFEIFQKELTIIGSFINPY--TFP 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1276242734 315 RADAeglheirqLSEAGKLKIP--IERTFPIAQVREAHEAKDKRiISGKVV 363
Cdd:cd08234   291 RAIA--------LLESGKIDVKglVSHRLPLEEVPEALEGMRSG-GALKVV 332
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
24-366 1.40e-12

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: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 67.40  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  24 MRRSLVTSCRAVllpRFGGPEVLElrddvnvPDLKPNEVLVRARAVSVNPLDTR---MRSGyGRslfepllpvILGRDIS 100
Cdd:cd08270     1 MRALVVDPDAPL---RLRLGEVPD-------PQPAPHEALVRVAAISLNRGELKfaaERPD-GA---------VPGWDAA 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 101 GEVAAVGNSVRSLSVGQEVFGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRALRSTARIKQGQR 180
Cdd:cd08270    61 GVVERAAADGSGPAVGARVVGLGAM----GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLLGRRV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 181 VLVVGGGGAVGFsAIQLAVAAGCHVSTTCGGES-IERILAAGAEQAVdyttEDYELSIKGYFDAVLDTIGVPeTEKMGVN 259
Cdd:cd08270   137 LVTGASGGVGRF-AVQLAALAGAHVVAVVGSPArAEGLRELGAAEVV----VGGSELSGAPVDLVVDSVGGP-QLARALE 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 260 LLKRGGhymTLQGeaasftdrYGLAVGLPMA--TAVLAKKQIQYRFSHGIDYQWTYMRADAEGLHEirqLSEAGKLKIPI 337
Cdd:cd08270   211 LLAPGG---TVVS--------VGSSSGEPAVfnPAAFVGGGGGRRLYTFFLYDGEPLAADLARLLG---LVAAGRLDPRI 276
                         330       340
                  ....*....|....*....|....*....
gi 1276242734 338 ERTFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:cd08270   277 GWRGSWTEIDEAAEALLARRFRGKAVLDV 305
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
39-266 1.94e-12

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish 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 GroES-like catalytic domain. 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: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 67.62  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  39 RFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRM-RSGYgrslFEPLLPVILGRDISGEVAAVGNSVRSLSVGQ 117
Cdd:cd08235     5 VLHGPNDVRLEE-VPVPEPGPGEVLVKVRACGICGTDVKKiRGGH----TDLKPPRILGHEIAGEIVEVGDGVTGFKVGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 118 EVFGALH------PTAVRGTY-----------------ADYA-----ILAEDELTRKPESISHVEASAI-PFAalTAWRA 168
Cdd:cd08235    80 RVFVAPHvpcgecHYCLRGNEnmcpnykkfgnlydggfAEYVrvpawAVKRGGVLKLPDNVSFEEAALVePLA--CCINA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 169 LRStARIKQgqrvlvvgGGGAVGFSA-------IQLAVAAGCHVSTTC--GGESIERILAAGAEQAVDYTTEDYELSIK- 238
Cdd:cd08235   158 QRK-AGIKP--------GDTVLVIGAgpigllhAMLAKASGARKVIVSdlNEFRLEFAKKLGADYTIDAAEEDLVEKVRe 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1276242734 239 ---GY-FDAVLDTIGVPETEKMGVNLLKRGGH 266
Cdd:cd08235   229 ltdGRgADVVIVATGSPEAQAQALELVRKGGR 260
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
34-234 2.21e-12

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like 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: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 67.83  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  34 AVLLPRFGGPEVLELRDDVNVPDLKPNEVLVRARAVSVN----------PLDT-RMRSGYGRSL-FEpllpvILGRDISG 101
Cdd:cd08246    17 AIRPERYGDPAQAIQLEDVPVPELGPGEVLVAVMAAGVNynnvwaalgePVSTfAARQRRGRDEpYH-----IGGSDASG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 102 EVAAVGNSVRSLSVGQEVfgALHPTAVR--------------------------GTYADYAILAEDELTRKPESISHVEA 155
Cdd:cd08246    92 IVWAVGEGVKNWKVGDEV--VVHCSVWDgndperaggdpmfdpsqriwgyetnyGSFAQFALVQATQLMPKPKHLSWEEA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 156 SAIPFAALTAWRAL--RSTARIKQGQRVLVVGGGGAVGFSAIQLAVAAG----CHVSTTcggESIERILAAGAEQAVDYT 229
Cdd:cd08246   170 AAYMLVGATAYRMLfgWNPNTVKPGDNVLIWGASGGLGSMAIQLARAAGanpvAVVSSE---EKAEYCRALGAEGVINRR 246

                  ....*
gi 1276242734 230 TEDYE 234
Cdd:cd08246   247 DFDHW 251
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
33-365 3.23e-12

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: 67.01  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygRSLFEPllPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08263     2 KAAVLKGPNPPLTIE---EIPVPRPKEGEILIRVAACGVCHSDLHVLKG--ELPFPP--PFVLGHEISGEVVEVGPNVEN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 ---LSVGQEVFGA-----------------------------------------LHPTAVR----GTYADYAILAEDELT 144
Cdd:cd08263    75 pygLSVGDRVVGSfimpcgkcrycargkenlcedffaynrlkgtlydgttrlfrLDGGPVYmysmGGLAEYAVVPATALA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 145 RKPESISHVEASAIPFAALTAWRALRStARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCH--VSTTCGGESIERILAAGA 222
Cdd:cd08263   155 PLPESLDYTESAVLGCAGFTAYGALKH-AADVRPGETVAVIGVGGVGSSAIQLAKAFGASpiIAVDVRDEKLAKAKELGA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 223 EQAVDYTTED-----YELSIKGYFDAVLDTIGVPETEKMGVNLLKRGGHyMTLQGEAASftdryGLAVGLPMATavLAKK 297
Cdd:cd08263   234 THTVNAAKEDavaaiREITGGRGVDVVVEALGKPETFKLALDVVRDGGR-AVVVGLAPG-----GATAEIPITR--LVRR 305
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 298 QIQYRFSHGidyqwTYMRADaegLHEIRQLSEAGKLKIP--IERTFPIAQVREAHEAKDKRIISGKVVLE 365
Cdd:cd08263   306 GIKIIGSYG-----ARPRQD---LPELVGLAASGKLDPEalVTHKYKLEEINEAYENLRKGLIHGRAIVE 367
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
33-174 4.64e-11

2-enoyl thioester reductase (ETR) like proteins, child 1; 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: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 63.01  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGP-EVLELR-DDVNVPDLKPNEVLVRARAVSVNPLD-TRMRSGYGrslFEPLLPVILGRDISGEVAAVGNS 109
Cdd:cd08291     2 KALLLEEYGKPlEVKELSlPEPEVPEPGPGEVLIKVEAAPINPSDlGFLKGQYG---STKALPVPPGFEGSGTVVAAGGG 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276242734 110 VRSLS-VGQEVFGAlhpTAVRGTYADYAILAEDELTRKPESISHvEASAIPFA-ALTAWrALRSTAR 174
Cdd:cd08291    79 PLAQSlIGKRVAFL---AGSYGTYAEYAVADAQQCLPLPDGVSF-EQGASSFVnPLTAL-GMLETAR 140
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
33-265 6.75e-11

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 62.75  E-value: 6.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLelrDDVNVPDLKPNEVLVRARAVSVNPLD-TRMRSGYGRSLfeplLPVILGRDISGEVAAVGNSVR 111
Cdd:PRK13771    2 KAVILPGFKQGYRI---EEVPDPKPGKDEVVIKVNYAGLCYRDlLQLQGFYPRMK----YPVILGHEVVGTVEEVGENVK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQEVFGALHP-----------------------TAVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRA 168
Cdd:PRK13771   75 GFKPGDRVASLLYApdgtceycrsgeeaycknrlgygEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 169 LRStARIKQGQRVLVVGGGGAVGFSAIQLAVAAGCHVSTTCGGESIERILAAGAEQAVDYTTEDYELSIKGYFDAVLDTI 248
Cdd:PRK13771  155 LRR-AGVKKGETVLVTGAGGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSKYADYVIVGSKFSEEVKKIGGADIVIETV 233
                         250
                  ....*....|....*..
gi 1276242734 249 GVPETEKmGVNLLKRGG 265
Cdd:PRK13771  234 GTPTLEE-SLRSLNMGG 249
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
194-265 6.83e-11

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 59.16  E-value: 6.83e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276242734 194 AIQLAVAAGCHVSTTCGGES-IERILAAGAEQAVDYTTEDY-----ELSIKGYFDAVLDTIGVPETEKMGVNLLKRGG 265
Cdd:pfam00107   6 AIQLAKAAGAKVIAVDGSEEkLELAKELGADHVINPKETDLveeikELTGGKGVDVVFDCVGSPATLEQALKLLRPGG 83
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
41-352 1.02e-10

Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 62.41  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  41 GGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYgrslFEPLLPVILGRDISGEVAAVGNSVRSLSVGQEVF 120
Cdd:COG1062     1 GGPLEIE---EVELDEPRPGEVLVRIVAAGLCHSDLHVRDGD----LPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHVV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 121 GALHP----------------------------------------TAVR-----GTYADYAILAEDELTRKPESISHVEA 155
Cdd:COG1062    74 LSFIPscghcrycasgrpalceagaalngkgtlpdgtsrlssadgEPVGhffgqSSFAEYAVVPERSVVKVDKDVPLELA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 156 SAIPFAALTAWRALRSTARIKqgqrvlvvggggavgFSAIQLAVAAGCHvsttcggesieRILAA-------------GA 222
Cdd:COG1062   154 ALLGCGVQTGAGAVLNTAKVRpgdtvav-fglggvgLSAVQGARIAGAS-----------RIIAVdpvpeklelarelGA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 223 EQAVDYTTED-----YELSiKGYFDAVLDTIGVPETEKMGVNLLKRGGHyMTLQGEAASftdryGLAVGLPMATAVLAKK 297
Cdd:COG1062   222 THTVNPADEDaveavRELT-GGGVDYAFETTGNPAVIRQALEALRKGGT-VVVVGLAPP-----GAEISLDPFQLLLTGR 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 298 QIQyrfshGIdyqwtYMrADAEGLHEIRQLSE---AGKLKI--PIERTFPIAQVREAHEA 352
Cdd:COG1062   295 TIR-----GS-----YF-GGAVPRRDIPRLVDlyrAGRLPLdeLITRRYPLDEINEAFDD 343
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
33-265 4.31e-10

Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) 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: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 60.27  E-value: 4.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELR-DDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrSLFEPLLPVILGRDISGEVAAVGNSVR 111
Cdd:cd08298     2 KAMVLEKPGPIEENPLRlTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEG---DLPPPKLPLIPGHEIVGRVEAVGPGVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQEVfGA--LHPT-----------------------AVRGTYADYAILAEDELTRKPESISHVEASAIPFAALTAW 166
Cdd:cd08298    79 RFSVGDRV-GVpwLGSTcgecrycrsgrenlcdnarftgyTVDGGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 167 RALR----------------STARIkqgqrvlvvggggavgfsAIQLAVAAGCHVST-TCGGESIERILAAGAEQAVDYT 229
Cdd:cd08298   158 RALKlaglkpgqrlglygfgASAHL------------------ALQIARYQGAEVFAfTRSGEHQELARELGADWAGDSD 219
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1276242734 230 TEDYELsikgyFDAVLDTIGVPETEKMGVNLLKRGG 265
Cdd:cd08298   220 DLPPEP-----LDAAIIFAPVGALVPAALRAVKKGG 250
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
33-170 1.17e-09

Cinnamyl alcohol dehydrogenases (CAD); 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 (ADHs), 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: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 58.80  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdvnVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEPLLPvilGRDISGEVAAVGNSVRS 112
Cdd:cd08296     2 KAVQVTEPGGPLELVERD---VPLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVP---GHEVVGRIDAVGEGVSR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 113 LSVGQEVFGALH-----------------------PTAVR-GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRA 168
Cdd:cd08296    76 WKVGDRVGVGWHgghcgtcdacrrgdfvhcengkvTGVTRdGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNA 155

                  ..
gi 1276242734 169 LR 170
Cdd:cd08296   156 LR 157
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
60-119 2.95e-09

Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol dehydrogenases. Many of them contain an inserted zinc binding domain. This domain has a GroES-like structure.


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 54.15  E-value: 2.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  60 NEVLVRARAVSVNPLDTRMRSGYgrsLFEPLLPVILGRDISGEVAAVGNSVRSLSVGQEV 119
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGG---NPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRV 57
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
33-125 4.47e-09

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. 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. 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. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. 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 an 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.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 57.17  E-value: 4.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYgrslFEPLLPVILGRDISGEVAAVGNSVRS 112
Cdd:cd08279     2 RAAVLHEVGKPLEIE---EVELDDPGPGEVLVRIAAAGLCHSDLHVVTGD----LPAPLPAVLGHEGAGVVEEVGPGVTG 74
                          90
                  ....*....|...
gi 1276242734 113 LSVGQEVFGALHP 125
Cdd:cd08279    75 VKPGDHVVLSWIP 87
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
91-268 9.73e-09

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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. 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.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 56.39  E-value: 9.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  91 LPVILGRDISGEVAAVGNSVRSLSVGQEV------FGALHPTAVRGTY------------------ADYAILAEDELTRK 146
Cdd:cd08233    64 APVTLGHEFSGVVVEVGSGVTGFKVGDRVvveptiKCGTCGACKRGLYnlcdslgfiglggggggfAEYVVVPAYHVHKL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 147 PESISHVEASAI-PFAalTAWRALR-------STARIkqgqrvlvvggggavgFSA-------IQLAVAAGCH---VSTT 208
Cdd:cd08233   144 PDNVPLEEAALVePLA--VAWHAVRrsgfkpgDTALV----------------LGAgpiglltILALKAAGASkiiVSEP 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276242734 209 cggeSIERILAA---GAEQAVDYTTED-----YELSIKGYFDAVLDTIGVPETEKMGVNLLKRGGHYM 268
Cdd:cd08233   206 ----SEARRELAeelGATIVLDPTEVDvvaevRKLTGGGGVDVSFDCAGVQATLDTAIDALRPRGTAV 269
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
52-294 1.75e-08

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: 55.24  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  52 VNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLfePLLPVILGRDISGEVAAVGNSvrSLSVGQEV------FGALHP 125
Cdd:cd05280    20 LPLDDLPEGDVLIRVHYSSLNYKDALAATGNGGVT--RNYPHTPGIDAAGTVVSSDDP--RFREGDEVlvtgydLGMNTD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 126 tavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAwrALrSTARIKQGQRVLVVGGGGAVGFS------AIQLAV 199
Cdd:cd05280    96 ----GGFAEYVRVPADWVVPLPEGLSLREAMILGTAGFTA--AL-SVHRLEDNGQTPEDGPVLVTGATggvgsiAVAILA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 200 AAGCHVSTTCGGES-IERILAAGAEQAVD----YTTEDYELSiKGYFDAVLDTIGvpetEKMGVNLLKrgghYMTLQGEA 274
Cdd:cd05280   169 KLGYTVVALTGKEEqADYLKSLGASEVLDredlLDESKKPLL-KARWAGAIDTVG----GDVLANLLK----QTKYGGVV 239
                         250       260
                  ....*....|....*....|
gi 1276242734 275 ASftdrYGLAVGLPMATAVL 294
Cdd:cd05280   240 AS----CGNAAGPELTTTVL 255
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
43-267 6.37e-08

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: 53.73  E-value: 6.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  43 PEVLELRDdVNVPDLKPNEVLVRARAVSV-----------NPLDTrmrsgygrslfeplLPVILGRDISGEVAAVGNSVR 111
Cdd:cd08261     9 PGRLEVVD-IPEPVPGAGEVLVRVKRVGIcgsdlhiyhgrNPFAS--------------YPRILGHELSGEVVEVGEGVA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 112 SLSVGQ---------------------------EVFGaLHptaVRGTYADYAILAEDELtRKPESISHVEASAIPFAALT 164
Cdd:cd08261    74 GLKVGDrvvvdpyiscgecyacrkgrpnccenlQVLG-VH---RDGGFAEYIVVPADAL-LVPEGLSLDQAALVEPLAIG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 165 AWRALRstARIKQgqrvlvvgggGAVGF---------SAIQLAVAAGCHVSTTCGGEsiERILAA---GAEQAVDYTTED 232
Cdd:cd08261   149 AHAVRR--AGVTA----------GDTVLvvgagpiglGVIQVAKARGARVIVVDIDD--ERLEFArelGADDTINVGDED 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1276242734 233 YELSIK-----GYFDAVLDTIGVPETEKMGVNLLKRGGHY 267
Cdd:cd08261   215 VAARLReltdgEGADVVIDATGNPASMEEAVELVAHGGRV 254
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
43-349 4.53e-07

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: 50.94  E-value: 4.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  43 PEVLELRDdVNVPDLKPNEVLVRARAVSVNP-LDTRMRSGygRSLFEPLLP--VILGRDIsGEVAAVGNSvrSLSVGQEV 119
Cdd:cd05288    17 PDDFELVE-VPLPELKDGEVLVRTLYLSVDPyMRGWMSDA--KSYSPPVQLgePMRGGGV-GEVVESRSP--DFKVGDLV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 120 FGALHptavrgtYADYAILAEDELTRKpesISHVEASAIPFA-------ALTAWRALRSTARIK---------------Q 177
Cdd:cd05288    91 SGFLG-------WQEYAVVDGASGLRK---LDPSLGLPLSAYlgvlgmtGLTAYFGLTEIGKPKpgetvvvsaaagavgS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 178 GqrvlvvggggavgfsAIQLAVAAGCHVSTTCGG-ESIERIL-AAGAEQAVDYTTEDY-----ELSIKG---YFD----A 243
Cdd:cd05288   161 V---------------VGQIAKLLGARVVGIAGSdEKCRWLVeELGFDAAINYKTPDLaealkEAAPDGidvYFDnvggE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 244 VLDTigvpetekmGVNLLKRGGHyMTLQGEAASFTDRYGLAVGLPMataVLAKKQIQYRfshGIDYQwTYMRADAEGLHE 323
Cdd:cd05288   226 ILDA---------ALTLLNKGGR-IALCGAISQYNATEPPGPKNLG---NIITKRLTMQ---GFIVS-DYADRFPEALAE 288
                         330       340
                  ....*....|....*....|....*.
gi 1276242734 324 IRQLSEAGKLKIPIERTFPIAQVREA 349
Cdd:cd05288   289 LAKWLAEGKLKYREDVVEGLENAPEA 314
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
30-119 5.37e-07

Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + 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: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 50.96  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  30 TSCRAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrsLFEPLLPVILGRDISGEVAAVGNS 109
Cdd:cd08278     1 MKTTAAVVREPGGPFVLE---DVELDDPRPDEVLVRIVATGICHTDLVVRDG----GLPTPLPAVLGHEGAGVVEAVGSA 73
                          90
                  ....*....|
gi 1276242734 110 VRSLSVGQEV 119
Cdd:cd08278    74 VTGLKPGDHV 83
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
51-119 7.02e-07

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: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 50.31  E-value: 7.02e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276242734  51 DVNVPDLKPNEVLVRARAVSVNPLDTRMrsgY-----GRSLFEPllPVILGRDISGEVAAVGNSVRSLSVGQEV 119
Cdd:cd05281    17 EVPVPKPGPGEVLIKVLAASICGTDVHI---YewdewAQSRIKP--PLIFGHEFAGEVVEVGEGVTRVKVGDYV 85
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
32-119 1.67e-06

Liver alcohol dehydrogenase and related 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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 an 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.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 49.36  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  32 CRAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYgrslFEPLLPVILGRDISGEVAAVGNSVR 111
Cdd:cd05279     1 CKAAVLWEKGKPLSIE---EIEVAPPKAGEVRIKVVATGVCHTDLHVIDGK----LPTPLPVILGHEGAGIVESIGPGVT 73

                  ....*...
gi 1276242734 112 SLSVGQEV 119
Cdd:cd05279    74 TLKPGDKV 81
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
78-362 7.02e-06

Cinnamyl alcohol dehydrogenases (CAD); 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: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 47.49  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  78 MRSGYGRSLFepllPVILGRDISGEVAAVGNSVRSLSVGQEV-FGALH-----------------PTAV----------- 128
Cdd:cd05283    44 LRNEWGPTKY----PLVPGHEIVGIVVAVGSKVTKFKVGDRVgVGCQVdscgtceqcksgeeqycPKGVvtyngkypdgt 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 129 --RGTYADYAILAEDELTRKPESIShvEASAIPF--AALTAWRALRstarikqgqrvlvvggggavGFS----------- 193
Cdd:cd05283   120 itQGGYADHIVVDERFVFKIPEGLD--SAAAAPLlcAGITVYSPLK--------------------RNGvgpgkrvgvvg 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 194 -------AIQLAVAAGCHV---STTcggES-IERILAAGAEQAVDYTTEDYELSIKGYFDAVLDTIGVP-ETEKMgVNLL 261
Cdd:cd05283   178 igglghlAVKFAKALGAEVtafSRS---PSkKEDALKLGADEFIATKDPEAMKKAAGSLDLIIDTVSAShDLDPY-LSLL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 262 KRGGHYMTlqgeaasftdryglaVGLPMATAV-----LAKKQIQYRFSH-GidyqwtymradaeGLHEIRQLSE-AGKLK 334
Cdd:cd05283   254 KPGGTLVL---------------VGAPEEPLPvppfpLIFGRKSVAGSLiG-------------GRKETQEMLDfAAEHG 305
                         330       340
                  ....*....|....*....|....*....
gi 1276242734 335 I-PIERTFPIAQVREAHEakdkRIISGKV 362
Cdd:cd05283   306 IkPWVEVIPMDGINEALE----RLEKGDV 330
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
38-267 9.25e-06

Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination 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 an 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: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 46.92  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  38 PRFGGPEVLelrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSlfePLLPVILGRDISGEVAAVGNSVRSLSVGQ 117
Cdd:cd08258     9 PGPGNVELR----EVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDP---VETPVVLGHEFSGTIVEVGPDVEGWKVGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 118 EV----------------------------FGalhpTAVRGTYADYAILAEDELTRKPESISHVEasaipfAALT----- 164
Cdd:cd08258    82 RVvsettfstcgrcpycrrgdynlcphrkgIG----TQADGGFAEYVLVPEESLHELPENLSLEA------AALTeplav 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 165 AWRALRSTARIKQGQRVLVVGGGGAVGFSAiQLAVAAGCHVSTTCGGESIERILAA---GAEqAVDYTTEDY-----ELS 236
Cdd:cd08258   152 AVHAVAERSGIRPGDTVVVFGPGPIGLLAA-QVAKLQGATVVVVGTEKDEVRLDVAkelGAD-AVNGGEEDLaelvnEIT 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1276242734 237 IKGYFDAVLDTIGVPETEKMGVNLLKRGGHY 267
Cdd:cd08258   230 DGDGADVVIECSGAVPALEQALELLRKGGRI 260
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
33-165 1.03e-05

putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of pfam00107 as defined by Pfam, a superfamily in which some members are zinc-binding medium-chain alcohol dehydrogenases while others are quinone oxidoreductases with no bound zinc. This subfamily includes proteins studied crystallographically for insight into function: YhdH from Escherichia coli and YhfP from Bacillus subtilis. Members bind NADPH or NAD, but not zinc. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 46.78  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEplLPVILGRDISGEVAAVGNSvrS 112
Cdd:TIGR02823   1 KALVVEKEDGKVSAQVET-LDLSDLPEGDVLIKVAYSSLNYKDALAITGKGGVVRS--YPMIPGIDAAGTVVSSEDP--R 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1276242734 113 LSVGQEV------FGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTA 165
Cdd:TIGR02823  76 FREGDEVivtgygLGVSHD----GGYSQYARVPADWLVPLPEGLSLREAMALGTAGFTA 130
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
51-124 1.22e-05

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 46.74  E-value: 1.22e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276242734  51 DVNVPDLKPNEVLVRARAVSVNPLDTRMRS--GYGRSLFEPllPVILGRDISGEVAAVGNSVRSLSVGQEVFGALH 124
Cdd:PRK05396   17 DVPVPEPGPNDVLIKVKKTAICGTDVHIYNwdEWAQKTIPV--PMVVGHEFVGEVVEVGSEVTGFKVGDRVSGEGH 90
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
38-170 1.74e-05

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These 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: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 46.16  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  38 PRFGGPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRM-RSGYGRSLFEPllpVILGRDISGEVAAVGNSVRSLSVG 116
Cdd:cd08239     4 AVFPGDRTVELRE-FPVPVPGPGEVLLRVKASGLCGSDLHYyYHGHRAPAYQG---VIPGHEPAGVVVAVGPGVTHFRVG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 117 QEV----------------------------FGALHPtavrGTYADYAILAEDELTRKPESISHVEASAIPFAALTAWRA 168
Cdd:cd08239    80 DRVmvyhyvgcgacrncrrgwmqlctskraaYGWNRD----GGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHA 155

                  ..
gi 1276242734 169 LR 170
Cdd:cd08239   156 LR 157
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
31-119 5.44e-05

Liver alcohol dehydrogenase; 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. 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. 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 an 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.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 44.64  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  31 SCRAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFepllPVILGRDISGEVAAVGNSV 110
Cdd:cd08277     2 KCKAAVAWEAGKPLVIE---EIEVAPPKANEVRIKMLATSVCHTDILAIEGFKATLF----PVILGHEGAGIVESVGEGV 74

                  ....*....
gi 1276242734 111 RSLSVGQEV 119
Cdd:cd08277    75 TNLKPGDKV 83
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
52-300 7.12e-05

Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group contains members identified as zinc dependent alcohol dehydrogenases (ADH), and class III ADG (aka formaldehyde dehydrogenase, FDH). 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. 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. Class III ADH are also know as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to the corresponding carboxylic acid and alcohol. 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: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 44.29  E-value: 7.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  52 VNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrSLFEPLlPVILGRDISGEVAAVGNSVRSLSVGQEVF----------- 120
Cdd:cd08281    26 VELDPPGPGEVLVKIAAAGLCHSDLSVING---DRPRPL-PMALGHEAAGVVVEVGEGVTDLEVGDHVVlvfvpscghcr 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 121 -------------------GALHPTAVR--------------GTYADYAILAEDELTRKPESISHVEASAIPFAALTAWR 167
Cdd:cd08281   102 pcaegrpalcepgaaangaGTLLSGGRRlrlrggeinhhlgvSAFAEYAVVSRRSVVKIDKDVPLEIAALFGCAVLTGVG 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 168 ALRSTARIKqGQRVLVVGGGGAVGFSAIQLAVAAGCH--VSTTCGGESIERILAAGAEQAVDYTTEDYELSIKGY----F 241
Cdd:cd08281   182 AVVNTAGVR-PGQSVAVVGLGGVGLSALLGAVAAGASqvVAVDLNEDKLALARELGATATVNAGDPNAVEQVRELtgggV 260
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1276242734 242 DAVLDTIGVPETEKMGVNLLKRGGHYMTlqgeaasftdryglaVGLPMATAVLAKKQIQ 300
Cdd:cd08281   261 DYAFEMAGSVPALETAYEITRRGGTTVT---------------AGLPDPEARLSVPALS 304
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
32-119 1.12e-04

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, 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: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 43.79  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  32 CRAVLLPRFGGPevLELRDdVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygRSLFEPLlPVILGRDISGEVAAVGNSVR 111
Cdd:cd08231     1 ARAAVLTGPGKP--LEIRE-VPLPDLEPGAVLVRVRLAGVCGSDVHTVAG--RRPRVPL-PIILGHEGVGRVVALGGGVT 74

                  ....*...
gi 1276242734 112 SLSVGQEV 119
Cdd:cd08231    75 TDVAGEPL 82
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
42-365 1.66e-04

Sorbitol dehydrogenase; 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. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 43.25  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  42 GPEVLELRDdVNVPDLKPNEVLVRARAVSVNPLD----TRMRSGygrsLFEPLLPVILGRDISGEVAAVGNSVRSLSVGQ 117
Cdd:cd05285     6 GPGDLRLEE-RPIPEPGPGEVLVRVRAVGICGSDvhyyKHGRIG----DFVVKEPMVLGHESAGTVVAVGSGVTHLKVGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 118 EVfgALHP-------------------------TA-VRGTYADYAILAEDELTRKPESISHVEASAI-PFA-ALTAWR-- 167
Cdd:cd05285    81 RV--AIEPgvpcrtcefcksgrynlcpdmrfaaTPpVDGTLCRYVNHPADFCHKLPDNVSLEEGALVePLSvGVHACRra 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 168 --ALRSTARIkqgqrvlvvggggavgFSA-------IQLAVAAGCH--VSTTCGGESIERILAAGAEQAVDYTTEDYELS 236
Cdd:cd05285   159 gvRPGDTVLV----------------FGAgpiglltAAVAKAFGATkvVVTDIDPSRLEFAKELGATHTVNVRTEDTPES 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 237 IK--------GYFDAVLDTIGVPETEKMGVNLLKRGGHYMtLQGEAASftdryglAVGLPMATAVLakKQIQYRFShgID 308
Cdd:cd05285   223 AEkiaellggKGPDVVIECTGAESCIQTAIYATRPGGTVV-LVGMGKP-------EVTLPLSAASL--REIDIRGV--FR 290
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1276242734 309 YQWTYMRAdaeglheIRQL-SEAGKLKIPIERTFPIAQVREAHE-AKDKRIISGKVVLE 365
Cdd:cd05285   291 YANTYPTA-------IELLaSGKVDVKPLITHRFPLEDAVEAFEtAAKGKKGVIKVVIE 342
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
55-356 2.20e-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: 42.73  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  55 PDLKPNEVLVRARAVSVNPLDtrMRSGY-GRSLF-EPLLPVILGRDISGEVAAVGNSVRSLSVGQEVFGAlhptaVRGTY 132
Cdd:cd08269    15 PTPGPGQVLVRVEGCGVCGSD--LPAFNqGRPWFvYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAGL-----SGGAF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 133 ADYAILAEDELTRKPESIshvEASAIPFAAL-TAWRALRSTaRIKQGQRVLVVGGGGAVGFsAIQLAVAAGCHVSTTCGG 211
Cdd:cd08269    88 AEYDLADADHAVPLPSLL---DGQAFPGEPLgCALNVFRRG-WIRAGKTVAVIGAGFIGLL-FLQLAAAAGARRVIAIDR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 212 ESIERILAA--GAEQAVDYTTED-----YELSIKGYFDAVLDTIGVPETEKMGVNLLKRGGHYMtlqgeAASFTDryGLA 284
Cdd:cd08269   163 RPARLALARelGATEVVTDDSEAivervRELTGGAGADVVIEAVGHQWPLDLAGELVAERGRLV-----IFGYHQ--DGP 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276242734 285 VGLPMATAvlakkqiqyrFSHGIDYQWTYMRADA---EGLHEIRQLSEAGKLK--IPIERTFPIAQVREAHEAKDKR 356
Cdd:cd08269   236 RPVPFQTW----------NWKGIDLINAVERDPRiglEGMREAVKLIADGRLDlgSLLTHEFPLEELGDAFEAARRR 302
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
33-203 1.12e-03

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. 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: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 40.37  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  33 RAVLLPrfGGPEVLelrDDVNVPDLKPNEVLVRARAVSVNPLDTRMRSG--------YGRSLFEPLLPVILGRDISGEVA 104
Cdd:cd08262     2 RAAVFR--DGPLVV---RDVPDPEPGPGQVLVKVLACGICGSDLHATAHpeamvddaGGPSLMDLGADIVLGHEFCGEVV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 105 AVGNSVRS-LSVGQEV--------------FGALHPTAVrGTYADYAILAEDELTRKPESISHvEASAI--PFAalTAWR 167
Cdd:cd08262    77 DYGPGTERkLKVGTRVtslplllcgqgascGIGLSPEAP-GGYAEYMLLSEALLLRVPDGLSM-EDAALtePLA--VGLH 152
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1276242734 168 ALRStARIKQGQRVLVVGGggavgfSAIQLAVAAGC 203
Cdd:cd08262   153 AVRR-ARLTPGEVALVIGC------GPIGLAVIAAL 181
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
48-366 1.84e-03

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays 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 GroES-like catalytic domain. 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. 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: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 39.91  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  48 LR-DDVNVPDLKPNEVLVRARAVSVNPLDTRM----RSGYGRsLFEPLlpvILGRDISGEVAAVGNSVRSLSVGQEVfgA 122
Cdd:cd08232     9 LRvEERPAPEPGPGEVRVRVAAGGICGSDLHYyqhgGFGTVR-LREPM---VLGHEVSGVVEAVGPGVTGLAPGQRV--A 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 123 LHPTA------------------------------VRGTYADYAILAEDELTRKPESISHVEAS-AIPFA-ALTAwralr 170
Cdd:cd08232    83 VNPSRpcgtcdycragrpnlclnmrflgsamrfphVQGGFREYLVVDASQCVPLPDGLSLRRAAlAEPLAvALHA----- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 171 stARIKQGQRVLVVGGGGAVGFSAIQLAVA----AGCHVSTTCGGESIERILAAGAEQAVDYTTEDYEL--SIKGYFDAV 244
Cdd:cd08232   158 --VNRAGDLAGKRVLVTGAGPIGALVVAAArragAAEIVATDLADAPLAVARAMGADETVNLARDPLAAyaADKGDFDVV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 245 LDTIGVPETEKMGVNLLKRGGHYMTLqGEAasftdryGLAVGLPMATAVlaKKQIQYRFSHgidyqwtymRADAEGLHEI 324
Cdd:cd08232   236 FEASGAPAALASALRVVRPGGTVVQV-GML-------GGPVPLPLNALV--AKELDLRGSF---------RFDDEFAEAV 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1276242734 325 RQLSEAGKLKIP-IERTFPIAQVREAHEAKDKRIISGKVVLEL 366
Cdd:cd08232   297 RLLAAGRIDVRPlITAVFPLEEAAEAFALAADRTRSVKVQLSF 339
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
43-244 2.98e-03

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: 39.27  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  43 PEVLELRDdVNVPDLKPNEVLVRARAVSVNPLdTRMRSGYGRSLFEPllpVILGRDISGevAAVGNSVRS----LSVGQE 118
Cdd:COG2130    20 PEDFRLEE-VPVPEPGDGEVLVRNLYLSVDPY-MRGRMSDAKSYAPP---VELGEVMRG--GAVGEVVESrhpdFAVGDL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 119 VFGalhptavRGTYADYAILAEDELTRKPESISHVEA--SAIPFAALTAWRALRSTARIKQGQRVLVVGGggavgfS--- 193
Cdd:COG2130    93 VLG-------MLGWQDYAVSDGAGLRKVDPSLAPLSAylGVLGMPGLTAYFGLLDIGKPKAGETVVVSAA------Agav 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276242734 194 ---AIQLAVAAGCHVSTTCGG-ESIERIL-AAGAEQAVDYTTEDYELSIK--------GYFDAV 244
Cdd:COG2130   160 gsvVGQIAKLKGCRVVGIAGGaEKCRYLVeELGFDAAIDYKAGDLAAALAaacpdgidVYFDNV 223
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
51-165 5.05e-03

Yhfp putative quinone oxidoreductases; yhfp 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: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 38.46  E-value: 5.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  51 DVNVPDLKPNEVLVRARAVSVNPLDTRMRSGYGRSLFEplLPVILGRDISGEVAAVGNSvrSLSVGQEV------FGALH 124
Cdd:cd08289    19 NLTLDDLPEGDVLIRVAYSSVNYKDGLASIPGGKIVKR--YPFIPGIDLAGTVVESNDP--RFKPGDEVivtsydLGVSH 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1276242734 125 ptavRGTYADYAILAEDELTRKPESISHVEASAIPFAALTA 165
Cdd:cd08289    95 ----HGGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFTA 131
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
90-170 5.34e-03

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: 38.02  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  90 LLPVILGRDISGEVAAVGNSVRSLSVGQEVFGAlhptavrGTYADYAILAEDELTRKPESISHVEASAIPFAAlTAWRAL 169
Cdd:cd08255    19 PLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCF-------GPHAERVVVPANLLVPLPDGLPPERAALTALAA-TALNGV 90

                  .
gi 1276242734 170 R 170
Cdd:cd08255    91 R 91
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
47-202 7.58e-03

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 37.88  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  47 ELR-DDVNVPDLKPNEVLVRARAVSVNPLDTRM----RSGYgrSLFEPL--LPVILGRDISGEVAAVGNSVRSLSVG--- 116
Cdd:cd08265    38 ELRvEDVPVPNLKPDEILIRVKACGICGSDIHLyetdKDGY--ILYPGLteFPVVIGHEFSGVVEKTGKNVKNFEKGdpv 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734 117 --QEVF--GALHPTA----------------VRGTYADYAILAE------DELTRKPESISHVEASAIPFAALTAWRALR 170
Cdd:cd08265   116 taEEMMwcGMCRACRsgspnhcknlkelgfsADGAFAEYIAVNAryaweiNELREIYSEDKAFEAGALVEPTSVAYNGLF 195
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1276242734 171 STARIKQGQRVLVVGGGGAVGFSAIQLAVAAG 202
Cdd:cd08265   196 IRGGGFRPGAYVVVYGAGPIGLAAIALAKAAG 227
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
29-119 9.89e-03

class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. This group includes alcohol dehydrogenases corresponding to mammalian classes I, II, IV. 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: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 37.68  E-value: 9.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276242734  29 VTSCRAVLLPRFGGPEVLElrdDVNVPDLKPNEVLVRARAVSVNPLDTRMRSGygrsLFEPLLPVILGRDISGEVAAVGN 108
Cdd:cd08299     5 VIKCKAAVLWEPKKPFSIE---EIEVAPPKAHEVRIKIVATGICRSDDHVVSG----KLVTPFPVILGHEAAGIVESVGE 77
                          90
                  ....*....|.
gi 1276242734 109 SVRSLSVGQEV 119
Cdd:cd08299    78 GVTTVKPGDKV 88
 
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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