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Conserved domains on  [gi|1972254588|ref|NP_001379459|]
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Prostaglandin reductase 2 [Caenorhabditis elegans]

Protein Classification

prostaglandin reductase 2( domain architecture ID 10169693)

prostaglandin reductase 2 functions as a 15-oxo-prostaglandin 13-reductase and acts on 15-keto-PGE1, 15-keto-PGE2, 15-keto-PGE1-alpha and 15-keto-PGE2-alpha, with highest activity towards 15-keto-PGE2; belongs to the medium chain dehydrogenase/reductase (MDR) superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
22-373 0e+00

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


:

Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 612.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  22 ADNKVVIFVKRPGENNAPTIDCFDVVPIDSPSEKDitSDQCIVRTLFLSVDPAQRCRMNPSTGVDYLGPYEIgepVDGME 101
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELN--EGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQL---SQVLD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 102 GVGVVERVGSA-CTLEVGDLVTGCIrlWTWTKYFVCDSSDLVKVNlPSSRNFSPSVILSCAGLSGITALLGIRKKALIDR 180
Cdd:cd08293    76 GGGVGVVEESKhQKFAVGDIVTSFN--WPWQTYAVLDGSSLEKVD-PQLVDGHLSYFLGAVGLPGLTALIGIQEKGHITP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 181 SRPQTIVVSGAAGSCGSLAGQIARIEGCSKVIGICGSDDKCTVLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDNV 260
Cdd:cd08293   153 GANQTMVVSGAAGACGSLAGQIGRLLGCSRVVGICGSDEKCQLLKSELGFDAAINYKTDNVAERLRELCPEGVDVYFDNV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 261 GGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPPPLPEHTTKIIKERNIQRERYLVLMYKDEIDEAVAQLSEWLQQDKI 340
Cdd:cd08293   233 GGEISDTVISQMNENSHIILCGQISQYNKDVPYPPPLPEATEAILKERNITRERFLVLNYKDKFEEAIAQLSQWVKEGKL 312
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1972254588 341 KVKETIYDGLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:cd08293   313 KVKETVYEGLENAGEAFQSMMNGGNIGKQIVKV 345
 
Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
22-373 0e+00

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


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 612.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  22 ADNKVVIFVKRPGENNAPTIDCFDVVPIDSPSEKDitSDQCIVRTLFLSVDPAQRCRMNPSTGVDYLGPYEIgepVDGME 101
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELN--EGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQL---SQVLD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 102 GVGVVERVGSA-CTLEVGDLVTGCIrlWTWTKYFVCDSSDLVKVNlPSSRNFSPSVILSCAGLSGITALLGIRKKALIDR 180
Cdd:cd08293    76 GGGVGVVEESKhQKFAVGDIVTSFN--WPWQTYAVLDGSSLEKVD-PQLVDGHLSYFLGAVGLPGLTALIGIQEKGHITP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 181 SRPQTIVVSGAAGSCGSLAGQIARIEGCSKVIGICGSDDKCTVLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDNV 260
Cdd:cd08293   153 GANQTMVVSGAAGACGSLAGQIGRLLGCSRVVGICGSDEKCQLLKSELGFDAAINYKTDNVAERLRELCPEGVDVYFDNV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 261 GGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPPPLPEHTTKIIKERNIQRERYLVLMYKDEIDEAVAQLSEWLQQDKI 340
Cdd:cd08293   233 GGEISDTVISQMNENSHIILCGQISQYNKDVPYPPPLPEATEAILKERNITRERFLVLNYKDKFEEAIAQLSQWVKEGKL 312
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1972254588 341 KVKETIYDGLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:cd08293   313 KVKETVYEGLENAGEAFQSMMNGGNIGKQIVKV 345
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
24-372 3.29e-116

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: 340.50  E-value: 3.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  24 NKVVIFVKRP-GEnnaPTIDCFDVVPIDSPSEKDitsDQCIVRTLFLSVDPAQRCRMNPSTGvdYLGPYEIGEPVDGMeG 102
Cdd:COG2130     5 NRQIVLASRPeGE---PTPEDFRLEEVPVPEPGD---GEVLVRNLYLSVDPYMRGRMSDAKS--YAPPVELGEVMRGG-A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 103 VGVVERVGSAcTLEVGDLVTGcirLWTWTKYFVCDSSDLVKVNLPSSrnfSPSVILSCAGLSGITALLGirkkaLIDRSR 182
Cdd:COG2130    76 VGEVVESRHP-DFAVGDLVLG---MLGWQDYAVSDGAGLRKVDPSLA---PLSAYLGVLGMPGLTAYFG-----LLDIGK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 183 PQ---TIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDN 259
Cdd:COG2130   144 PKageTVVVSAAAGAVGSVVGQIAKLKGC-RVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAAACPDGIDVYFDN 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 260 VGGVISDDVIRAMNNEGRVVLCGQIAVYNTDlpYPPPLPEHTTKIIKERnIQRERYLVLMYKDEIDEAVAQLSEWLQQDK 339
Cdd:COG2130   223 VGGEILDAVLPLLNTFARIAVCGAISQYNAT--EPPPGPRNLGQLLVKR-LRMQGFIVFDHADRFPEFLAELAGWVAEGK 299
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1972254588 340 IKVKETIYDGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:COG2130   300 LKYRETVVEGLENAPEAFLGLFEGENFGKLLVK 332
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
39-372 9.01e-53

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


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 177.88  E-value: 9.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  39 PTIDCFDVVPIDSPSekdITSDQCIVRTLFLSVDPAQRcrmnpsTGVDYLgpyEIGEPVDGMEGVGVVERVGSActLEVG 118
Cdd:TIGR02825  14 PTDSDFELKTVELPP---LNNGEVLLEALFLSVDPYMR------VAAKRL---KEGDTMMGQQVARVVESKNVA--LPKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 119 DLVtgcIRLWTWTKYFVCDSSDLVKVNLPSSRNFSPSVILSCAGLSGITALLGIRKkaLIDRSRPQTIVVSGAAGSCGSL 198
Cdd:TIGR02825  80 TIV---LASPGWTSHSISDGKDLEKLLTEWPDTLPLSLALGTVGMPGLTAYFGLLE--ICGVKGGETVMVNAAAGAVGSV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 199 AGQIARIEGCsKVIGICGSDDKCTVLKReFGFNDTINYKT-ENVSERLGHLAPEGIDIYWDNVGGVISDDVIRAMNNEGR 277
Cdd:TIGR02825 155 VGQIAKLKGC-KVVGAAGSDEKVAYLKK-LGFDVAFNYKTvKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 278 VVLCGQIAVYNTDLPYPP-PLPEhttkIIKERNIQRERYLVLMYKDEI-DEAVAQLSEWLQQDKIKVKETIYDGLNAAPS 355
Cdd:TIGR02825 233 IAICGAISTYNRTGPLPPgPPPE----IVIYQELRMEGFIVNRWQGEVrQKALKELLKWVLEGKIQYKEYVIEGFENMPA 308
                         330
                  ....*....|....*..
gi 1972254588 356 AFVDMMNGKNIGKMLIR 372
Cdd:TIGR02825 309 AFMGMLKGENLGKTIVK 325
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
63-372 3.68e-43

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 153.07  E-value: 3.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  63 IVRTLFLSVDPAQRCRMNPSTGvDYLGPYEIGEPVdgmEGVGVVERVGSACT-LEVGDLVTGCIrlwTWTKYFVCDSSDL 141
Cdd:PLN03154   47 LVKNLYLSCDPYMRGRMRDFHD-SYLPPFVPGQRI---EGFGVSKVVDSDDPnFKPGDLISGIT---GWEEYSLIRSSDN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 142 VKVNLPSSRNFSPSVILSCAGLSGITALLGIRKkaLIDRSRPQTIVVSGAAGSCGSLAGQIARIEGCSkVIGICGSDDKC 221
Cdd:PLN03154  120 QLRKIQLQDDIPLSYHLGLLGMAGFTAYAGFYE--VCSPKKGDSVFVSAASGAVGQLVGQLAKLHGCY-VVGSAGSSQKV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 222 TVLKREFGFNDTINYKTE-NVSERLGHLAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVynTDLPYPPPLPEH 300
Cdd:PLN03154  197 DLLKNKLGFDEAFNYKEEpDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSL--NSLSASQGIHNL 274
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972254588 301 TTKIIKErnIQRERYLVLMYKDEIDEAVAQLSEWLQQDKIKVKETIYDGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:PLN03154  275 YNLISKR--IRMQGFLQSDYLHLFPQFLENVSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIR 344
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
25-144 5.69e-20

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


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 84.17  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  25 KVVIFVKRP-GEnnaPTIDCFDVVPIDSPSEKDitsDQCIVRTLFLSVDPAQRCRMNPSTGvdYLGPYEIGEPVDGMeGV 103
Cdd:pfam16884   1 KQWLLAKRPeGV---PTPSDFELVEAELPELGD---GEVLVRTLYLSVDPYMRGRMNDAKS--YVPPVELGDVMRGG-AV 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1972254588 104 GVVERVGSAcTLEVGDLVTGcirLWTWTKYFVCDSSDLVKV 144
Cdd:pfam16884  72 GEVVESNNP-DFPVGDLVLG---MLGWQDYAVSDGKGLTKV 108
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
87-371 5.28e-10

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 59.71  E-value: 5.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588   87 YLGPYEiGEPVDGMEGVGVVERVGSACT-LEVGD----LVTGCirlwtWTKYFVCDSSDLVKVnlPSSRNFS-----PSV 156
Cdd:smart00829  16 ALGLYP-GEAVLGGECAGVVTRVGPGVTgLAVGDrvmgLAPGA-----FATRVVTDARLVVPI--PDGWSFEeaatvPVV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  157 ILscaglsgiTALLGIRKKAlidRSRP-QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLkREFGFNDT-- 233
Cdd:smart00829  88 FL--------TAYYALVDLA---RLRPgESVLIHAAAGGVGQAAIQLARHLGA-EVFATAGSPEKRDFL-RALGIPDDhi 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  234 INYKTENVSER-LGHLAPEGIDIywdnvggVI---SDDVIRA----MNNEGRVVLCGQIAVY-NTDLPYPPplpehttki 304
Cdd:smart00829 155 FSSRDLSFADEiLRATGGRGVDV-------VLnslSGEFLDAslrcLAPGGRFVEIGKRDIRdNSQLAMAP--------- 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972254588  305 iKERNIqreRY----LVLMYK--DEIDEAVAQLSEWLQQDKIK-VKETIYDgLNAAPSAFVDMMNGKNIGKMLI 371
Cdd:smart00829 219 -FRPNV---SYhavdLDALEEgpDRIRELLAEVLELFAEGVLRpLPVTVFP-ISDAEDAFRYMQQGKHIGKVVL 287
 
Name Accession Description Interval E-value
PTGR2 cd08293
Prostaglandin reductase; Prostaglandins and related eicosanoids are metabolized by the ...
22-373 0e+00

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


Pssm-ID: 176253 [Multi-domain]  Cd Length: 345  Bit Score: 612.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  22 ADNKVVIFVKRPGENNAPTIDCFDVVPIDSPSEKDitSDQCIVRTLFLSVDPAQRCRMNPSTGVDYLGPYEIgepVDGME 101
Cdd:cd08293     1 MINKRVVLNSRPGKNGNPVAENFRVEECTLPDELN--EGQVLVRTLYLSVDPYMRCRMNEDTGTDYLAPWQL---SQVLD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 102 GVGVVERVGSA-CTLEVGDLVTGCIrlWTWTKYFVCDSSDLVKVNlPSSRNFSPSVILSCAGLSGITALLGIRKKALIDR 180
Cdd:cd08293    76 GGGVGVVEESKhQKFAVGDIVTSFN--WPWQTYAVLDGSSLEKVD-PQLVDGHLSYFLGAVGLPGLTALIGIQEKGHITP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 181 SRPQTIVVSGAAGSCGSLAGQIARIEGCSKVIGICGSDDKCTVLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDNV 260
Cdd:cd08293   153 GANQTMVVSGAAGACGSLAGQIGRLLGCSRVVGICGSDEKCQLLKSELGFDAAINYKTDNVAERLRELCPEGVDVYFDNV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 261 GGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPPPLPEHTTKIIKERNIQRERYLVLMYKDEIDEAVAQLSEWLQQDKI 340
Cdd:cd08293   233 GGEISDTVISQMNENSHIILCGQISQYNKDVPYPPPLPEATEAILKERNITRERFLVLNYKDKFEEAIAQLSQWVKEGKL 312
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1972254588 341 KVKETIYDGLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:cd08293   313 KVKETVYEGLENAGEAFQSMMNGGNIGKQIVKV 345
CurA COG2130
NADPH-dependent curcumin reductase CurA [Secondary metabolites biosynthesis, transport and ...
24-372 3.29e-116

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: 340.50  E-value: 3.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  24 NKVVIFVKRP-GEnnaPTIDCFDVVPIDSPSEKDitsDQCIVRTLFLSVDPAQRCRMNPSTGvdYLGPYEIGEPVDGMeG 102
Cdd:COG2130     5 NRQIVLASRPeGE---PTPEDFRLEEVPVPEPGD---GEVLVRNLYLSVDPYMRGRMSDAKS--YAPPVELGEVMRGG-A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 103 VGVVERVGSAcTLEVGDLVTGcirLWTWTKYFVCDSSDLVKVNLPSSrnfSPSVILSCAGLSGITALLGirkkaLIDRSR 182
Cdd:COG2130    76 VGEVVESRHP-DFAVGDLVLG---MLGWQDYAVSDGAGLRKVDPSLA---PLSAYLGVLGMPGLTAYFG-----LLDIGK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 183 PQ---TIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDN 259
Cdd:COG2130   144 PKageTVVVSAAAGAVGSVVGQIAKLKGC-RVVGIAGGAEKCRYLVEELGFDAAIDYKAGDLAAALAAACPDGIDVYFDN 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 260 VGGVISDDVIRAMNNEGRVVLCGQIAVYNTDlpYPPPLPEHTTKIIKERnIQRERYLVLMYKDEIDEAVAQLSEWLQQDK 339
Cdd:COG2130   223 VGGEILDAVLPLLNTFARIAVCGAISQYNAT--EPPPGPRNLGQLLVKR-LRMQGFIVFDHADRFPEFLAELAGWVAEGK 299
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1972254588 340 IKVKETIYDGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:COG2130   300 LKYRETVVEGLENAPEAFLGLFEGENFGKLLVK 332
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
24-371 2.68e-115

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: 338.30  E-value: 2.68e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  24 NKVVIFVKRPGENnaPTIDCFDVV--PIDSPSEkditsDQCIVRTLFLSVDPAQRCRMNPstGVDYLGPYEIGEPVDGMe 101
Cdd:cd05288     2 NRQVVLAKRPEGP--PPPDDFELVevPLPELKD-----GEVLVRTLYLSVDPYMRGWMSD--AKSYSPPVQLGEPMRGG- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 102 GVGVVERVGSAcTLEVGDLVTGcirLWTWTKYFVCDSSDLVKVnLPSSRNFSPSVILSCAGLSGITALLGIRKkalIDRS 181
Cdd:cd05288    72 GVGEVVESRSP-DFKVGDLVSG---FLGWQEYAVVDGASGLRK-LDPSLGLPLSAYLGVLGMTGLTAYFGLTE---IGKP 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 182 RP-QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDNV 260
Cdd:cd05288   144 KPgETVVVSAAAGAVGSVVGQIAKLLGA-RVVGIAGSDEKCRWLVEELGFDAAINYKTPDLAEALKEAAPDGIDVYFDNV 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 261 GGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPPPLPEHttkiIKERNIQRERYLVLMYKDEIDEAVAQLSEWLQQDKI 340
Cdd:cd05288   223 GGEILDAALTLLNKGGRIALCGAISQYNATEPPGPKNLGN----IITKRLTMQGFIVSDYADRFPEALAELAKWLAEGKL 298
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1972254588 341 KVKETIYDGLNAAPSAFVDMMNGKNIGKMLI 371
Cdd:cd05288   299 KYREDVVEGLENAPEAFLGLFTGKNTGKLVV 329
leukotriene_B4_DH_like cd08294
13-PGR is a bifunctional enzyme with delta-13 15-prostaglandin reductase and leukotriene B4 12 ...
38-372 2.69e-79

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


Pssm-ID: 176254 [Multi-domain]  Cd Length: 329  Bit Score: 246.41  E-value: 2.69e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  38 APTIDCFDVVPIDSPSEKDitsDQCIVRTLFLSVDPAQRCRMNPSTgvdyLGPYEIGEPVdgmegVGVVERVGSActLEV 117
Cdd:cd08294    15 KPKESDFELVEEELPPLKD---GEVLCEALFLSVDPYMRPYSKRLN----EGDTMIGTQV-----AKVIESKNSK--FPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 118 GDLVTGcirLWTWTKYFVCDSS---DLVKVNLPSSRNFSPSVILSCAGLSGITALLGirkkaLIDRSRPQ---TIVVSGA 191
Cdd:cd08294    81 GTIVVA---SFGWRTHTVSDGKdqpDLYKLPADLPDDLPPSLALGVLGMPGLTAYFG-----LLEICKPKageTVVVNGA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 192 AGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKrEFGFNDTINYKTENVSERLGHLAPEGIDIYWDNVGGVISDDVIRA 271
Cdd:cd08294   153 AGAVGSLVGQIAKIKGC-KVIGCAGSDDKVAWLK-ELGFDAVFNYKTVSLEEALKEAAPDGIDCYFDNVGGEFSSTVLSH 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 272 MNNEGRVVLCGQIAVYNTDLPYPPPLPeHTTKIIKErnIQRERYLVLMYKDEIDEAVAQLSEWLQQDKIKVKETIYDGLN 351
Cdd:cd08294   231 MNDFGRVAVCGSISTYNDKEPKKGPYV-QETIIFKQ--LKMEGFIVYRWQDRWPEALKQLLKWIKEGKLKYREHVTEGFE 307
                         330       340
                  ....*....|....*....|.
gi 1972254588 352 AAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd08294   308 NMPQAFIGMLKGENTGKAIVK 328
double_bond_reductase_like cd08295
Arabidopsis alkenal double bond reductase and leukotriene B4 12-hydroxydehydrogenase; This ...
55-372 4.11e-71

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


Pssm-ID: 176255 [Multi-domain]  Cd Length: 338  Bit Score: 225.66  E-value: 4.11e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  55 KDITSDQCIVRTLFLSVDPAQRCRMNPSTGVDYLGPYEIGEPVDGMegvGVVERVGSAC-TLEVGDLVTGcirlWT-WTK 132
Cdd:cd08295    33 PPGGSGDVLVKNLYLSCDPYMRGRMKGHDDSLYLPPFKPGEVITGY---GVAKVVDSGNpDFKVGDLVWG----FTgWEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 133 YFVCD-SSDLVKVN---LPssrnfsPSVILSCAGLSGITALLGirkkaLIDRSRPQ---TIVVSGAAGSCGSLAGQIARI 205
Cdd:cd08295   106 YSLIPrGQDLRKIDhtdVP------LSYYLGLLGMPGLTAYAG-----FYEVCKPKkgeTVFVSAASGAVGQLVGQLAKL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 206 EGCsKVIGICGSDDKCTVLKREFGFNDTINYKTE-NVSERLGHLAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQI 284
Cdd:cd08295   175 KGC-YVVGSAGSDEKVDLLKNKLGFDDAFNYKEEpDLDAALKRYFPNGIDIYFDNVGGKMLDAVLLNMNLHGRIAACGMI 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 285 AVYNTDLPYPPP-LPEhttkIIKERnIQRERYLVLMYKDEIDEAVAQLSEWLQQDKIKVKETIYDGLNAAPSAFVDMMNG 363
Cdd:cd08295   254 SQYNLEWPEGVRnLLN----IIYKR-VKIQGFLVGDYLHRYPEFLEEMSGYIKEGKLKYVEDIADGLESAPEAFVGLFTG 328

                  ....*....
gi 1972254588 364 KNIGKMLIR 372
Cdd:cd08295   329 SNIGKQVVK 337
B4_12hDH TIGR02825
leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase; Leukotriene B4 ...
39-372 9.01e-53

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


Pssm-ID: 131872 [Multi-domain]  Cd Length: 325  Bit Score: 177.88  E-value: 9.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  39 PTIDCFDVVPIDSPSekdITSDQCIVRTLFLSVDPAQRcrmnpsTGVDYLgpyEIGEPVDGMEGVGVVERVGSActLEVG 118
Cdd:TIGR02825  14 PTDSDFELKTVELPP---LNNGEVLLEALFLSVDPYMR------VAAKRL---KEGDTMMGQQVARVVESKNVA--LPKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 119 DLVtgcIRLWTWTKYFVCDSSDLVKVNLPSSRNFSPSVILSCAGLSGITALLGIRKkaLIDRSRPQTIVVSGAAGSCGSL 198
Cdd:TIGR02825  80 TIV---LASPGWTSHSISDGKDLEKLLTEWPDTLPLSLALGTVGMPGLTAYFGLLE--ICGVKGGETVMVNAAAGAVGSV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 199 AGQIARIEGCsKVIGICGSDDKCTVLKReFGFNDTINYKT-ENVSERLGHLAPEGIDIYWDNVGGVISDDVIRAMNNEGR 277
Cdd:TIGR02825 155 VGQIAKLKGC-KVVGAAGSDEKVAYLKK-LGFDVAFNYKTvKSLEETLKKASPDGYDCYFDNVGGEFSNTVIGQMKKFGR 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 278 VVLCGQIAVYNTDLPYPP-PLPEhttkIIKERNIQRERYLVLMYKDEI-DEAVAQLSEWLQQDKIKVKETIYDGLNAAPS 355
Cdd:TIGR02825 233 IAICGAISTYNRTGPLPPgPPPE----IVIYQELRMEGFIVNRWQGEVrQKALKELLKWVLEGKIQYKEYVIEGFENMPA 308
                         330
                  ....*....|....*..
gi 1972254588 356 AFVDMMNGKNIGKMLIR 372
Cdd:TIGR02825 309 AFMGMLKGENLGKTIVK 325
PLN03154 PLN03154
putative allyl alcohol dehydrogenase; Provisional
63-372 3.68e-43

putative allyl alcohol dehydrogenase; Provisional


Pssm-ID: 215606 [Multi-domain]  Cd Length: 348  Bit Score: 153.07  E-value: 3.68e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  63 IVRTLFLSVDPAQRCRMNPSTGvDYLGPYEIGEPVdgmEGVGVVERVGSACT-LEVGDLVTGCIrlwTWTKYFVCDSSDL 141
Cdd:PLN03154   47 LVKNLYLSCDPYMRGRMRDFHD-SYLPPFVPGQRI---EGFGVSKVVDSDDPnFKPGDLISGIT---GWEEYSLIRSSDN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 142 VKVNLPSSRNFSPSVILSCAGLSGITALLGIRKkaLIDRSRPQTIVVSGAAGSCGSLAGQIARIEGCSkVIGICGSDDKC 221
Cdd:PLN03154  120 QLRKIQLQDDIPLSYHLGLLGMAGFTAYAGFYE--VCSPKKGDSVFVSAASGAVGQLVGQLAKLHGCY-VVGSAGSSQKV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 222 TVLKREFGFNDTINYKTE-NVSERLGHLAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVynTDLPYPPPLPEH 300
Cdd:PLN03154  197 DLLKNKLGFDEAFNYKEEpDLDAALKRYFPEGIDIYFDNVGGDMLDAALLNMKIHGRIAVCGMVSL--NSLSASQGIHNL 274
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972254588 301 TTKIIKErnIQRERYLVLMYKDEIDEAVAQLSEWLQQDKIKVKETIYDGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:PLN03154  275 YNLISKR--IRMQGFLQSDYLHLFPQFLENVSRYYKQGKIVYIEDMSEGLESAPAALVGLFSGKNVGKQVIR 344
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
99-373 3.17e-41

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: 147.22  E-value: 3.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGCIRLWTWTKYFVCDSSDLVKvnLPSSrnfspsviLS-----CAGLSGITALLgi 172
Cdd:COG0604    62 GSDAAGVVVAVGEGVTgFKVGDRVAGLGRGGGYAEYVVVPADQLVP--LPDG--------LSfeeaaALPLAGLTAWQ-- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 173 rkkALIDRSRP---QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLkREFGFNDTINYKTENVSERLGHL- 248
Cdd:COG0604   130 ---ALFDRGRLkpgETVLVHGAAGGVGSAAVQLAKALGA-RVIATASSPEKAELL-RALGADHVIDYREEDFAERVRALt 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 249 APEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPPPLPehttkiiKERNIQRErYLVLMYKDEIDEAV 328
Cdd:COG0604   205 GGRGVDVVLDTVGGDTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLLL-------KGLTLTGF-TLFARDPAERRAAL 276
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1972254588 329 AQLSEWLQQDKIKVK-ETIYDgLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:COG0604   277 AELARLLAAGKLRPViDRVFP-LEEAAEAHRLLESGKHRGKVVLTV 321
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
96-372 1.74e-38

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: 140.08  E-value: 1.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  96 PVD-GMEGVGVVERVGSACT-LEVGDLVtGCIRLWTWTKYFVCDSSDLVKVNLPSsrnfsPSVILSCagLSGITALLGIR 173
Cdd:cd08250    61 PFDcGFEGVGEVVAVGEGVTdFKVGDAV-ATMSFGAFAEYQVVPARHAVPVPELK-----PEVLPLL--VSGLTASIALE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 174 KKAliDRSRPQTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKrEFGFNDTINYKTENVSERLGHLAPEGI 253
Cdd:cd08250   133 EVG--EMKSGETVLVTAAAGGTGQFAVQLAKLAGC-HVIGTCSSDEKAEFLK-SLGCDRPINYKTEDLGEVLKKEYPKGV 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 254 DIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPP----PLPEhttKIIKERNIQRERYLVlMYKDEIDEAVA 329
Cdd:cd08250   209 DVVYESVGGEMFDTCVDNLALKGRLIVIGFISGYQSGTGPSPvkgaTLPP---KLLAKSASVRGFFLP-HYAKLIPQHLD 284
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1972254588 330 QLSEWLQQDKIKVK--ETIYDGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd08250   285 RLLQLYQRGKLVCEvdPTRFRGLESVADAVDYLYSGKNIGKVVVE 329
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
99-372 4.48e-26

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: 106.43  E-value: 4.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGCIRLWTWTKYFVCDSSDLVKVnlPSSRNFSPSVILscaGLSGITALLgirkkAL 177
Cdd:cd08241    62 GSEVAGVVEAVGEGVTgFKVGDRVVALTGQGGFAEEVVVPAAAVFPL--PDGLSFEEAAAL---PVTYGTAYH-----AL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 178 IDRSRPQ---TIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLkREFGFNDTINYKTENVSERLGHL-APEGI 253
Cdd:cd08241   132 VRRARLQpgeTVLVLGAAGGVGLAAVQLAKALGA-RVIAAASSEEKLALA-RALGADHVIDYRDPDLRERVKALtGGRGV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 254 DIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAvyntdlPYPPPLPehtTKIIKERNIQ----RERYLVLMYKDEIDEAVA 329
Cdd:cd08241   210 DVVYDPVGGDVFEASLRSLAWGGRLLVIGFAS------GEIPQIP---ANLLLLKNISvvgvYWGAYARREPELLRANLA 280
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1972254588 330 QLSEWLQQDKIKVKETIYDGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd08241   281 ELFDLLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
90-373 5.66e-26

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: 106.13  E-value: 5.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  90 PYEIGEP-VDGMEGVGVVERVGSACT-LEVGDlvtgciRLWTW-----------TKYFVCDSSDLVKvnLPSSRNFSPSV 156
Cdd:cd08253    52 PGLPPLPyVPGSDGAGVVEAVGEGVDgLKVGD------RVWLTnlgwgrrqgtaAEYVVVPADQLVP--LPDGVSFEQGA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 157 ilsCAGLSGITALLgirkkALIDRSRP---QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKcTVLKREFGFNDT 233
Cdd:cd08253   124 ---ALGIPALTAYR-----ALFHRAGAkagETVLVHGGSGAVGHAAVQLARWAGA-RVIATASSAEG-AELVRQAGADAV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 234 INYKTENVSER-LGHLAPEGIDIYWDNVGGV-ISDDVIRAMNNegrvvlcGQIAVY-NTDLPYPPPLPEHTTKIIKERNI 310
Cdd:cd08253   194 FNYRAEDLADRiLAATAGQGVDVIIEVLANVnLAKDLDVLAPG-------GRIVVYgSGGLRGTIPINPLMAKEASIRGV 266
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972254588 311 qrerYLVLMYKDEIDEAVAQLSEWLQQDKIKVKET-IYDgLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:cd08253   267 ----LLYTATPEERAAAAEAIAAGLADGALRPVIArEYP-LEEAAAAHEAVESGGAIGKVVLDP 325
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
99-373 2.33e-24

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: 101.75  E-value: 2.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGCIRLWTWTKYFVCDSSDLVKvnLPSSRNFSpsvILSCAGLSGITALlgirkkAL 177
Cdd:cd05286    59 GVEGAGVVEAVGPGVTgFKVGDRVAYAGPPGAYAEYRVVPASRLVK--LPDGISDE---TAAALLLQGLTAH------YL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 178 IDRSRP----QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTvLKREFGFNDTINYKTENVSERLGHLA-PEG 252
Cdd:cd05286   128 LRETYPvkpgDTVLVHAAAGGVGLLLTQWAKALGA-TVIGTVSSEEKAE-LARAAGADHVINYRDEDFVERVREITgGRG 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 253 IDIYWDNVGGV---ISDDVIRamnNEGRVVLCGQIAvyntdlPYPPPLPehtTKIIKERNIQRERYLVLMY---KDEIDE 326
Cdd:cd05286   206 VDVVYDGVGKDtfeGSLDSLR---PRGTLVSFGNAS------GPVPPFD---LLRLSKGSLFLTRPSLFHYiatREELLA 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1972254588 327 AVAQLSEWLQQDKIKVKE-TIYDgLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:cd05286   274 RAAELFDAVASGKLKVEIgKRYP-LADAAQAHRDLESRKTTGKLLLIP 320
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
96-371 1.06e-23

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: 99.98  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  96 PVDGMEGVGVVERVGSA-CTLEVGDLVTGCIRLW---TWTKYFVCDSSDLVKVnlPSSRNFspsVILSCAGLSGITALLG 171
Cdd:cd08267    60 PIPGMDFAGEVVAVGSGvTRFKVGDEVFGRLPPKgggALAEYVVAPESGLAKK--PEGVSF---EEAAALPVAGLTALQA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 172 IRKKAlidRSRP-QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDdkctvlKREF----GFNDTINYKTENVSERLG 246
Cdd:cd08267   135 LRDAG---KVKPgQRVLINGASGGVGTFAVQIAKALGA-HVTGVCSTR------NAELvrslGADEVIDYTTEDFVALTA 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 247 HLAPegIDIYWDNVGGVISD--DVIRAMNNEGRVVLCG----QIAVYNTDLPYPPPLPEHttkiikerniqreRYLVLMY 320
Cdd:cd08267   205 GGEK--YDVIFDAVGNSPFSlyRASLALKPGGRYVSVGggpsGLLLVLLLLPLTLGGGGR-------------RLKFFLA 269
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1972254588 321 KDEIdEAVAQLSEWLQQDKIK-VKETIYDgLNAAPSAFVDMMNGKNIGKMLI 371
Cdd:cd08267   270 KPNA-EDLEQLAELVEEGKLKpVIDSVYP-LEDAPEAYRRLKSGRARGKVVI 319
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
99-368 1.45e-23

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: 99.17  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGCIRLW---TWTKYFVCDSSDLVKVnlPSSrnfspsviLS-----CAGLSGITAL 169
Cdd:cd05289    64 GHDVAGVVVAVGPGVTgFKVGDEVFGMTPFTrggAYAEYVVVPADELALK--PAN--------LSfeeaaALPLAGLTAW 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 170 LGIRKkaLIDRSRPQTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVlkREFGFNDTINYKTENVSERlghLA 249
Cdd:cd05289   134 QALFE--LGGLKAGQTVLIHGAAGGVGSFAVQLAKARGA-RVIATASAANADFL--RSLGADEVIDYTKGDFERA---AA 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 250 PEGIDIYWDNVGGVISDDVIRAMNNEGRVVlcgqiavyntDLPYPPPLPehttKIIKERNIQRERYLVlmykdEID-EAV 328
Cdd:cd05289   206 PGGVDAVLDTVGGETLARSLALVKPGGRLV----------SIAGPPPAE----QAAKRRGVRAGFVFV-----EPDgEQL 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1972254588 329 AQLSEWLQQDKIKVK-ETIYDgLNAAPSAFVDMMNGKNIGK 368
Cdd:cd05289   267 AELAELVEAGKLRPVvDRVFP-LEDAAEAHERLESGHARGK 306
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
99-289 9.49e-23

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: 96.24  E-value: 9.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGCIRLW-----------------------TWTKYFVCDSSDLVKVnlPSSrnfSP 154
Cdd:cd05188    34 GHEGAGVVVEVGPGVTgVKVGDRVVVLPNLGcgtcelcrelcpgggilgegldgGFAEYVVVPADNLVPL--PDG---LS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 155 SVILSCAGLSGITALLGIRKKALIdrsRP-QTIVVSGAaGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKrEFGFNDT 233
Cdd:cd05188   109 LEEAALLPEPLATAYHALRRAGVL---KPgDTVLVLGA-GGVGLLAAQLAKAAGA-RVIVTDRSDEKLELAK-ELGADHV 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972254588 234 INYKTENVSERLGHLAPEGIDIYWDNVGGVIS-DDVIRAMNNEGRVVLCGQIAVYNT 289
Cdd:cd05188   183 IDYKEEDLEEELRLTGGGGADVVIDAVGGPETlAQALRLLRPGGRIVVVGGTSGGPP 239
ADH_N_2 pfam16884
N-terminal domain of oxidoreductase; N-terminal region of oxidoreductase and prostaglandin ...
25-144 5.69e-20

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


Pssm-ID: 465297 [Multi-domain]  Cd Length: 108  Bit Score: 84.17  E-value: 5.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  25 KVVIFVKRP-GEnnaPTIDCFDVVPIDSPSEKDitsDQCIVRTLFLSVDPAQRCRMNPSTGvdYLGPYEIGEPVDGMeGV 103
Cdd:pfam16884   1 KQWLLAKRPeGV---PTPSDFELVEAELPELGD---GEVLVRTLYLSVDPYMRGRMNDAKS--YVPPVELGDVMRGG-AV 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1972254588 104 GVVERVGSAcTLEVGDLVTGcirLWTWTKYFVCDSSDLVKV 144
Cdd:pfam16884  72 GEVVESNNP-DFPVGDLVLG---MLGWQDYAVSDGKGLTKV 108
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
97-373 1.51e-19

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: 88.41  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  97 VDGMEGVGVVERVGSACT-LEVGDLVTGCIRLWTWTKYFVCDSSDLVKvnLPSSRNFSPSVILSCAGLsgiTALLGIRKK 175
Cdd:cd08275    59 VPGFECAGTVEAVGEGVKdFKVGDRVMGLTRFGGYAEVVNVPADQVFP--LPDGMSFEEAAAFPVNYL---TAYYALFEL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 176 ALIdrsRP-QTIVVSGAAGSCGSLAGQIARIEGCSKVIGICgSDDKCTVLKrEFGFNDTINYKTENVSERLGHLAPEGID 254
Cdd:cd08275   134 GNL---RPgQSVLVHSAAGGVGLAAGQLCKTVPNVTVVGTA-SASKHEALK-ENGVTHVIDYRTQDYVEEVKKISPEGVD 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 255 IYWDNVGGVISDDVIRAMNNEGRVVLCGQiavyntdlpyppplpeHTTKIIKERNI--------QRERY----------- 315
Cdd:cd08275   209 IVLDALGGEDTRKSYDLLKPMGRLVVYGA----------------ANLVTGEKRSWfklakkwwNRPKVdpmklisenks 272
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972254588 316 -----LVLMY--KDEIDEAVAQLSEWLQQDKIKVK-ETIYDgLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:cd08275   273 vlgfnLGWLFeeRELLTEVMDKLLKLYEEGKIKPKiDSVFP-FEEVGEAMRRLQSRKNIGKVVLTP 337
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
88-371 4.03e-17

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: 80.69  E-value: 4.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  88 LGPYEIGEPVDGMEGVGVVERVGSACT-LEVGDLVTGCIRLwTWTKYFVCDSSDLVKVnlPSSRNFSPSVILSCAGLsgi 166
Cdd:cd05195    21 LGLLPGDETPLGLECSGIVTRVGSGVTgLKVGDRVMGLAPG-AFATHVRVDARLVVKI--PDSLSFEEAATLPVAYL--- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 167 TALLGIRKKALIdrSRPQTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKREFGFNDTInyktenVSERLG 246
Cdd:cd05195    95 TAYYALVDLARL--QKGESVLIHAAAGGVGQAAIQLAQHLGA-EVFATVGSEEKREFLRELGGPVDHI------FSSRDL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 247 HLAPE--------GIDIywdnvggVI---SDDVIRA----MNNEGRVVLCGQIAVY-NTDLPYPPPLPEHTTKIIKERNI 310
Cdd:cd05195   166 SFADGilratggrGVDV-------VLnslSGELLRAswrcLAPFGRFVEIGKRDILsNSKLGMRPFLRNVSFSSVDLDQL 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972254588 311 QRERylvlmyKDEIDEAVAQLSEWLQQDKIK-VKETIYDGLNAApSAFVDMMNGKNIGKMLI 371
Cdd:cd05195   239 ARER------PELLRELLREVLELLEAGVLKpLPPTVVPSASEI-DAFRLMQSGKHIGKVVL 293
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
80-304 2.35e-15

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: 76.16  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  80 NPstgVDYL----GPYEIGEP-VDGMEGVGVVERVGSACTL-EVGDLVTGCIRLW---TWTKYFVCDSSDLVKVnlPSSR 150
Cdd:cd08271    40 NP---VDWKviawGPPAWSYPhVPGVDGAGVVVAVGAKVTGwKVGDRVAYHASLArggSFAEYTVVDARAVLPL--PDSL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 151 NFSPSVILSCAGLsgiTALLGIRKKALIDRSRpqTIVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKCTVLKRefGF 230
Cdd:cd08271   115 SFEEAAALPCAGL---TAYQALFKKLRIEAGR--TILITGGAGGVGSFAVQLAKRAG-LRVITTCSKRNFEYVKSL--GA 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972254588 231 NDTINYKTENVSERL-GHLAPEGIDIYWDNVGGvisDDVIRamnNEGRVVLCGQIAVYNtDLPYPPPLPEHTTKI 304
Cdd:cd08271   187 DHVIDYNDEDVCERIkEITGGRGVDAVLDTVGG---ETAAA---LAPTLAFNGHLVCIQ-GRPDASPDPPFTRAL 254
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
99-372 2.29e-14

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: 72.98  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGCI-----RLWTWTKYFVCDSSDLVKvnLPSSRNFSPSvilSCAGLSGITALlgi 172
Cdd:cd08272    62 GCDVAGVVEAVGEGVTrFRVGDEVYGCAgglggLQGSLAEYAVVDARLLAL--KPANLSMREA---AALPLVGITAW--- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 173 rkKALIDRSRP---QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVlkREFGFNDTINYKTENVSERLGHLA 249
Cdd:cd08272   134 --EGLVDRAAVqagQTVLIHGGAGGVGHVAVQLAKAAGA-RVYATASSEKAAFA--RSLGADPIIYYRETVVEYVAEHTG 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 250 PEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAvyNTDLpyppplpehTTKIIKERNIQRERYLVLMYKDEIDEA-- 327
Cdd:cd08272   209 GRGFDVVFDTVGGETLDASFEAVALYGRVVSILGGA--THDL---------APLSFRNATYSGVFTLLPLLTGEGRAHhg 277
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1972254588 328 --VAQLSEWLQQDKIK--VKETIYdGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd08272   278 eiLREAARLVERGQLRplLDPRTF-PLEEAAAAHARLESGSARGKIVID 325
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
99-372 3.16e-14

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: 72.73  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVG-SACTLEVGDLVTGCIRLWTWT---------------------------KYFVCDSSDLVKvnLPSSR 150
Cdd:cd08259    59 GHEIVGTVEEVGeGVERFKPGDRVILYYYIPCGKceyclsgeenlcrnraeygeevdggfaEYVKVPERSLVK--LPDNV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 151 NFSPSVILSCAGLSGITALLGIRKKalidrsRPQTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKrEFGF 230
Cdd:cd08259   137 SDESAALAACVVGTAVHALKRAGVK------KGDTVLVTGAGGGVGIHAIQLAKALGA-RVIAVTRSPEKLKILK-ELGA 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 231 NDTINykTENVSERLGHLApeGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGqiavyNTDlPYPPPLPEHTTkIIKERNI 310
Cdd:cd08259   209 DYVID--GSKFSEDVKKLG--GADVVIELVGSPTIEESLRSLNKGGRLVLIG-----NVT-PDPAPLRPGLL-ILKEIRI 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972254588 311 QRErylVLMYKDEIDEAVAQLSEwlqqDKIKVKETIYDGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd08259   278 IGS---ISATKADVEEALKLVKE----GKIKPVIDRVVSLEDINEALEDLKSGKVVGRIVLK 332
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
97-373 3.40e-14

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 72.76  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  97 VDGMEGVGVVERVGSACT-LEVGDLVTGCIRLWTWT---------------------------KYFVCDSSDLVKVnlPS 148
Cdd:PRK13771   57 ILGHEVVGTVEEVGENVKgFKPGDRVASLLYAPDGTceycrsgeeaycknrlgygeeldgffaEYAKVKVTSLVKV--PP 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 149 SRNFSPSVILSCaglsgITALL--GIRKkalIDRSRPQTIVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKCTVLKR 226
Cdd:PRK13771  135 NVSDEGAVIVPC-----VTGMVyrGLRR---AGVKKGETVLVTGAGGGVGIHAIQVAKALG-AKVIAVTSSESKAKIVSK 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 227 efgFNDTI---NYKTENVsERLGhlapeGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIavyNTDLPYPPPLpehTTK 303
Cdd:PRK13771  206 ---YADYVivgSKFSEEV-KKIG-----GADIVIETVGTPTLEESLRSLNMGGKIIQIGNV---DPSPTYSLRL---GYI 270
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 304 IIKERNIqreRYLVLMYKDEIDEAVAQLSEwlqqDKIKVKETIYDGLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:PRK13771  271 ILKDIEI---IGHISATKRDVEEALKLVAE----GKIKPVIGAEVSLSEIDKALEELKDKSRIGKILVKP 333
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
167-364 1.03e-13

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: 71.49  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 167 TALLGIRKkalIDRSRPQTIVVSGAaGSCGSLAGQIARIEGCSKVIGICGSDDKCTVLkREFGFNDTINYKTENVSERLG 246
Cdd:cd08236   147 VALHAVRL---AGITLGDTVVVIGA-GTIGLLAIQWLKILGAKRVIAVDIDDEKLAVA-RELGADDTINPKEEDVEKVRE 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 247 HLAPEGIDIYWDNVGGVIS-DDVIRAMNNEGRVVLCGqiavyntdLPYPPPlpeHTTKIIKERNIQRER--------YLV 317
Cdd:cd08236   222 LTEGRGADLVIEAAGSPATiEQALALARPGGKVVLVG--------IPYGDV---TLSEEAFEKILRKELtiqgswnsYSA 290
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1972254588 318 LMYKDEIDEAVAqlseWLQQDKIKVKETIYD--GLNAAPSAFVDMMNGK 364
Cdd:cd08236   291 PFPGDEWRTALD----LLASGKIKVEPLITHrlPLEDGPAAFERLADRE 335
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
99-373 2.21e-13

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: 70.36  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVT-----GCIRLWTWT--KYFVCDSSDLV----------KVNLPSsRNFSPS----- 155
Cdd:cd08266    62 GSDGAGVVEAVGPGVTnVKPGQRVViypgiSCGRCEYCLagRENLCAQYGILgehvdggyaeYVAVPA-RNLLPIpdnls 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 156 -VILSCAGLSGITALlgirkKALIDRS--RP-QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKctvLKR--EFG 229
Cdd:cd08266   141 fEEAAAAPLTFLTAW-----HMLVTRArlRPgETVLVHGAGSGVGSAAIQIAKLFGA-TVIATAGSEDK---LERakELG 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 230 FNDTINYKTENVSERLGHLA-PEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVY--NTDLpyppplpehttkiik 306
Cdd:cd08266   212 ADYVIDYRKEDFVREVRELTgKRGVDVVVEHVGAATWEKSLKSLARGGRLVTCGATTGYeaPIDL--------------- 276
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972254588 307 eRNI-QRERYLVLMY---KDEIDEAVaqlsEWLQQDKIK-VKETIYdGLNAAPSAFVDMMNGKNIGKMLIRP 373
Cdd:cd08266   277 -RHVfWRQLSILGSTmgtKAELDEAL----RLVFRGKLKpVIDSVF-PLEEAAEAHRRLESREQFGKIVLTP 342
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
185-285 3.49e-13

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: 70.02  E-value: 3.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 185 TIVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKCTVlkREFGfNDTINYKTENVSERLGHLAPEGIDIYWDNVGGVI 264
Cdd:cd08274   180 TVLVTGASGGVGSALVQLAKRRG-AIVIAVAGAAKEEAV--RALG-ADTVILRDAPLLADAKALGGEPVDVVADVVGGPL 255
                          90       100
                  ....*....|....*....|.
gi 1972254588 265 SDDVIRAMNNEGRVVLCGQIA 285
Cdd:cd08274   256 FPDLLRLLRPGGRYVTAGAIA 276
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
196-311 4.10e-13

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 65.71  E-value: 4.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 196 GSLAGQIARIEGCsKVIGICGSDDKCTVLKrEFGFNDTINYKTENVSERLGHLA-PEGIDIYWDNVG-GVISDDVIRAMN 273
Cdd:pfam00107   3 GLAAIQLAKAAGA-KVIAVDGSEEKLELAK-ELGADHVINPKETDLVEEIKELTgGKGVDVVFDCVGsPATLEQALKLLR 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1972254588 274 NEGRVVLCGQIAvynTDLPYPPPlpehtTKIIKERNIQ 311
Cdd:pfam00107  81 PGGRVVVVGLPG---GPLPLPLA-----PLLLKELTIL 110
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
97-371 1.02e-12

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: 67.84  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  97 VDGMEGVGVVERVGSACT-LEVGDLVTGCI--RLWTWTKYFVCDSSDLVKVnlPSSRNFSPSVILSCAGLSGITALlgiR 173
Cdd:cd08251    40 TPGFEASGVVRAVGPHVTrLAVGDEVIAGTgeSMGGHATLVTVPEDQVVRK--PASLSFEEACALPVVFLTVIDAF---A 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 174 KKALidrSRPQTIVVSGAAGSCGSLAGQIARIEGCSkVIGICGSDDKCTVLKReFGFNDTINYKTENVSERLGHL-APEG 252
Cdd:cd08251   115 RAGL---AKGEHILIQTATGGTGLMAVQLARLKGAE-IYATASSDDKLEYLKQ-LGVPHVINYVEEDFEEEIMRLtGGRG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 253 IDIYWDNVGGVISDDVIRAMNNEGRVVlcgQIAVynTDLPYPPPLpehttKIIKERNIQR-----ERYLVLMYKDEIDEA 327
Cdd:cd08251   190 VDVVINTLSGEAIQKGLNCLAPGGRYV---EIAM--TALKSAPSV-----DLSVLSNNQSfhsvdLRKLLLLDPEFIADY 259
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1972254588 328 VAQLSEWLQQDKIKVKETIYDGLNAAPSAFVDMMNGKNIGKMLI 371
Cdd:cd08251   260 QAEMVSLVEEGELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
184-282 1.67e-12

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: 67.47  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 184 QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLkREFGFNDTINYKTENVSERL-GHLAPEGIDIYWDNVGG 262
Cdd:cd05276   141 ETVLIHGGASGVGTAAIQLAKALGA-RVIATAGSEEKLEAC-RALGADVAINYRTEDFAEEVkEATGGRGVDVILDMVGG 218
                          90       100
                  ....*....|....*....|
gi 1972254588 263 VISDDVIRAMNNEGRVVLCG 282
Cdd:cd05276   219 DYLARNLRALAPDGRLVLIG 238
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
46-372 1.77e-12

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: 67.30  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  46 VVPIDSPSEKDitsDQCIVRTLFLSVDPAQrcrMNPSTGVdylgpYEIGEP---VDGMEGVGVVERVGSACT-LEVGDLV 121
Cdd:cd05282    16 LVSLPIPPPGP---GEVLVRMLAAPINPSD---LITISGA-----YGSRPPlpaVPGNEGVGVVVEVGSGVSgLLVGQRV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 122 -----TGcirlwTWTKYFVCDSSDLVKVnlPssrNFSPSVILSCAGLSGITALLGIRKkalIDRSRPQTIVVSGAAGS-C 195
Cdd:cd05282    85 lplggEG-----TWQEYVVAPADDLIPV--P---DSISDEQAAMLYINPLTAWLMLTE---YLKLPPGDWVIQNAANSaV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 196 GSLAGQIARIEGCsKVIGIcGSDDKCTVLKREFGFNDTINYKTENVSERLGHLA-PEGIDIYWDNVGGVISDDVIRAMNN 274
Cdd:cd05282   152 GRMLIQLAKLLGF-KTINV-VRRDEQVEELKALGADEVIDSSPEDLAQRVKEATgGAGARLALDAVGGESATRLARSLRP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 275 EGRVVLCGqiAVYNTDLPYPPPLPEHTTKIIK---ERNiqrerYLVLMYKDEIDEAVAQLSEWLQQDKIKVKETIYDGLN 351
Cdd:cd05282   230 GGTLVNYG--LLSGEPVPFPRSVFIFKDITVRgfwLRQ-----WLHSATKEAKQETFAEVIKLVEAGVLTTPVGAKFPLE 302
                         330       340
                  ....*....|....*....|.
gi 1972254588 352 AAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd05282   303 DFEEAVAAAEQPGRGGKVLLT 323
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
101-373 2.12e-12

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: 67.47  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 101 EGVGVVERVGSACT-LEVGDLVTGCIRLW----------------------------TWTKYFVCDSSDLVKVnlpsSRN 151
Cdd:COG1063    60 EFVGEVVEVGEGVTgLKVGDRVVVEPNIPcgecrycrrgrynlcenlqflgiagrdgGFAEYVRVPAANLVKV----PDG 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 152 FSPSV-----ILSCAgLSGItALLGIRKkalidrsrPQTIVVSGAaGSCGSLAGQIARIEGCSKVIGICGSDDKCTVLkR 226
Cdd:COG1063   136 LSDEAaalvePLAVA-LHAV-ERAGVKP--------GDTVLVIGA-GPIGLLAALAARLAGAARVIVVDRNPERLELA-R 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 227 EFGFNDTINYKTENVSERL-GHLAPEGIDIYWDNVGGVIS-DDVIRAMNNEGRVVLCGqiaVYNTDLPYPPPLpehttki 304
Cdd:COG1063   204 ELGADAVVNPREEDLVEAVrELTGGRGADVVIEAVGAPAAlEQALDLVRPGGTVVLVG---VPGGPVPIDLNA------- 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 305 ikerniqrerylvLMYKdEID---------EAVAQLSEWLQQDKIKVKETIYD--GLNAAPSAFVDMMNGK-NIGKMLIR 372
Cdd:COG1063   274 -------------LVRK-ELTlrgsrnytrEDFPEALELLASGRIDLEPLITHrfPLDDAPEAFEAAADRAdGAIKVVLD 339

                  .
gi 1972254588 373 P 373
Cdd:COG1063   340 P 340
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
97-372 6.37e-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: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 65.75  E-value: 6.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  97 VDGMEGVGVVERVGSACT-LEVGDLVTGCIRLWTWTKYFVCDSSDLVKVnlPSSrnfSPSVILSCAGLSGITALLGIRKK 175
Cdd:cd08273    60 TPGYDLVGRVDALGSGVTgFEVGDRVAALTRVGGNAEYINLDAKYLVPV--PEG---VDAAEAVCLVLNYVTAYQMLHRA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 176 AlidRSRP-QTIVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKCTVlkREFGfNDTINYKTENVSERLghLAPEGID 254
Cdd:cd08273   135 A---KVLTgQRVLIHGASGGVGQALLELALLAG-AEVYGTASERNHAAL--RELG-ATPIDYRTKDWLPAM--LTPGGVD 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 255 IYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPPPLPEHTTKIIKERNIQRERYLVLMYkdeIDEAVAQLSEW 334
Cdd:cd08273   206 VVFDGVGGESYEESYAALAPGGTLVCYGGNSSLLQGRRSLAALGSLLARLAKLKLLPTGRRATFYY---VWRDRAEDPKL 282
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972254588 335 LQQD-------------KIKVKETIydGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd08273   283 FRQDltelldllakgkiRPKIAKRL--PLSEVAEAHRLLESGKVVGKIVLL 331
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
99-292 1.55e-11

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 64.54  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVtgCIRLW-------TWTKYFVCDSSDLVKvnLPSSRNFSPSVILscaGLSGITALL 170
Cdd:cd08268    62 GYEAAGVVEAVGAGVTgFAVGDRV--SVIPAadlgqygTYAEYALVPAAAVVK--LPDGLSFVEAAAL---WMQYLTAYG 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 171 GIRKKALIdrSRPQTIVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKCTVLkREFGFNDTINYKTENVSERL-GHLA 249
Cdd:cd08268   135 ALVELAGL--RPGDSVLITAASSSVGLAAIQIANAAG-ATVIATTRTSEKRDAL-LALGAAHVIVTDEEDLVAEVlRITG 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1972254588 250 PEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVYNTDLP 292
Cdd:cd08268   211 GKGVDVVFDPVGGPQFAKLADALAPGGTLVVYGALSGEPTPFP 253
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
99-372 4.05e-11

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: 63.71  E-value: 4.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLV------------TGCIRLW----------------TWTKYFVCDSSDLVKvnLPSS 149
Cdd:cd08297    61 GHEGAGVVVAVGPGVSgLKVGDRVgvkwlydacgkcEYCRTGDetlcpnqknsgytvdgTFAEYAIADARYVTP--IPDG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 150 RNFSPSVILSCAGlsgITALLGIRKKALidrsRP-QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTvLKREF 228
Cdd:cd08297   139 LSFEQAAPLLCAG---VTVYKALKKAGL----KPgDWVVISGAGGGLGHLGVQYAKAMGL-RVIAIDVGDEKLE-LAKEL 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 229 GFNDTINYKTENVSERLGHLApegidiywDNVG--GVI-----------SDDVIRAMnneGRVVLCGqiavyntdLPYPP 295
Cdd:cd08297   210 GADAFVDFKKSDDVEAVKELT--------GGGGahAVVvtavsaaayeqALDYLRPG---GTLVCVG--------LPPGG 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 296 PLPEHTTKII-KERNIQ------RErylvlmykdEIDEAVaqlsEWLQQDKIKVKETIYdGLNAAPSAFVDMMNGKNIGK 368
Cdd:cd08297   271 FIPLDPFDLVlRGITIVgslvgtRQ---------DLQEAL----EFAARGKVKPHIQVV-PLEDLNEVFEKMEEGKIAGR 336

                  ....
gi 1972254588 369 MLIR 372
Cdd:cd08297   337 VVVD 340
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
46-373 7.14e-11

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: 62.60  E-value: 7.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  46 VVPIDSPSEKDitsDQCIVRTLFLSVdpaqrcrmNPstgVDYLGPY--EIGEP--VDGMEGVGVVERVGSACT-LEVGDL 120
Cdd:cd08249    16 VVDVPVPKPGP---DEVLVKVKAVAL--------NP---VDWKHQDygFIPSYpaILGCDFAGTVVEVGSGVTrFKVGDR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 121 VTGCIR-LWTWTK-------YFVCDSSDLVKvnLPSSRNFSPSVILscaGLSGITALLGIRKKALID--------RSRPQ 184
Cdd:cd08249    82 VAGFVHgGNPNDPrngafqeYVVADADLTAK--IPDNISFEEAATL---PVGLVTAALALFQKLGLPlpppkpspASKGK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 185 TIVVSGAAGSCGSLAGQIARIEGCsKVIGICG--SDDKCtvlkREFGFNDTINYKTENVSERLGHLAPEGIDIYWDNVGG 262
Cdd:cd08249   157 PVLIWGGSSSVGTLAIQLAKLAGY-KVITTASpkNFDLV----KSLGADAVFDYHDPDVVEDIRAATGGKLRYALDCIST 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 263 VISDDVI-RAMNNEGRvvlcGQIAVYNtdlpyPPPLPEHTTKIIKERNIQRERYLVLMYKDEIDEAV--AQLSEWLQQDK 339
Cdd:cd08249   232 PESAQLCaEALGRSGG----GKLVSLL-----PVPEETEPRKGVKVKFVLGYTVFGEIPEDREFGEVfwKYLPELLEEGK 302
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1972254588 340 IKVKETIY--DGLNAAPSAFVDMMNGKNIG-KMLIRP 373
Cdd:cd08249   303 LKPHPVRVveGGLEGVQEGLDLLRKGKVSGeKLVVRL 339
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
87-371 5.28e-10

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 59.71  E-value: 5.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588   87 YLGPYEiGEPVDGMEGVGVVERVGSACT-LEVGD----LVTGCirlwtWTKYFVCDSSDLVKVnlPSSRNFS-----PSV 156
Cdd:smart00829  16 ALGLYP-GEAVLGGECAGVVTRVGPGVTgLAVGDrvmgLAPGA-----FATRVVTDARLVVPI--PDGWSFEeaatvPVV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  157 ILscaglsgiTALLGIRKKAlidRSRP-QTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLkREFGFNDT-- 233
Cdd:smart00829  88 FL--------TAYYALVDLA---RLRPgESVLIHAAAGGVGQAAIQLARHLGA-EVFATAGSPEKRDFL-RALGIPDDhi 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  234 INYKTENVSER-LGHLAPEGIDIywdnvggVI---SDDVIRA----MNNEGRVVLCGQIAVY-NTDLPYPPplpehttki 304
Cdd:smart00829 155 FSSRDLSFADEiLRATGGRGVDV-------VLnslSGEFLDAslrcLAPGGRFVEIGKRDIRdNSQLAMAP--------- 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972254588  305 iKERNIqreRY----LVLMYK--DEIDEAVAQLSEWLQQDKIK-VKETIYDgLNAAPSAFVDMMNGKNIGKMLI 371
Cdd:smart00829 219 -FRPNV---SYhavdLDALEEgpDRIRELLAEVLELFAEGVLRpLPVTVFP-ISDAEDAFRYMQQGKHIGKVVL 287
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
47-341 9.74e-10

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: 59.16  E-value: 9.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  47 VPIDSPSEkditSDQCIVRTLFLSVDPAQRcrmNPSTGVdYLGP---YEIGEPVDGMEGVGVVERVGSACT-LEVGDLV- 121
Cdd:cd08290    21 YEIPPPGP----PNEVLVKMLAAPINPADI---NQIQGV-YPIKpptTPEPPAVGGNEGVGEVVKVGSGVKsLKPGDWVi 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 122 ---TGcirLWTWTKYFVCDSSDLVKVNlpssrnfSPSVILSCAGLS--GITA--LLgirkKALIDRSRPQTIVVSGAAGS 194
Cdd:cd08290    93 plrPG---LGTWRTHAVVPADDLIKVP-------NDVDPEQAATLSvnPCTAyrLL----EDFVKLQPGDWVIQNGANSA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 195 CGSLAGQIARIEGCsKVIGICGSDDKCTVLK---REFG----FNDTINYKTENvSERLGHLAPEGIDIYWDNVGGVISDD 267
Cdd:cd08290   159 VGQAVIQLAKLLGI-KTINVVRDRPDLEELKerlKALGadhvLTEEELRSLLA-TELLKSAPGGRPKLALNCVGGKSATE 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972254588 268 VIRAMNNEGRVVLCGQIAvyNTDLPYPPPLpeHTTKIIKERNIQRERYLVLMYKDEIDEAVAQLSEWLQQDKIK 341
Cdd:cd08290   237 LARLLSPGGTMVTYGGMS--GQPVTVPTSL--LIFKDITLRGFWLTRWLKRANPEEKEDMLEELAELIREGKLK 306
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
228-371 1.62e-08

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 52.72  E-value: 1.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 228 FGFNDTINYKTENVSERLGhlaPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQiavyntdlpypPPLPEHTTKIIKE 307
Cdd:pfam13602   1 LGADEVIDYRTTDFVQATG---GEGVDVVLDTVGGEAFEASLRVLPGGGRLVTIGG-----------PPLSAGLLLPARK 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972254588 308 RNIQRERYLVLMYK-DEIDEAVAQLSEWLQQDKIKVK-ETIYdGLNAAPSAFVDMMNGKNIGKMLI 371
Cdd:pfam13602  67 RGGRGVKYLFLFVRpNLGADILQELADLIEEGKLRPViDRVF-PLEEAAEAHRYLESGRARGKIVL 131
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
130-282 1.64e-08

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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: 55.84  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 130 WTKYFVCDSSDLVKvnLPSSRNFSPSVILSCAGLSGITALlgirKKALIDRSrPQTIVVSGAAGsCGSLAGQIARIEGCS 209
Cdd:cd08263   142 LAEYAVVPATALAP--LPESLDYTESAVLGCAGFTAYGAL----KHAADVRP-GETVAVIGVGG-VGSSAIQLAKAFGAS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 210 KVIGICGSDDKctvLK--REFGFNDTINYKTENVSERLGH-LAPEGIDIYWDNVGGV----ISDDVIRamnNEGRVVLCG 282
Cdd:cd08263   214 PIIAVDVRDEK---LAkaKELGATHTVNAAKEDAVAAIREiTGGRGVDVVVEALGKPetfkLALDVVR---DGGRAVVVG 287
PRK10754 PRK10754
NADPH:quinone reductase;
99-261 3.04e-08

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 54.74  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTgcirlwtWTKYFVCDSSDLVKVN------LPSSRNFSPSvilSCAGLSGITALLG 171
Cdd:PRK10754   62 GTEAAGVVSKVGSGVKhIKVGDRVV-------YAQSALGAYSSVHNVPadkaaiLPDAISFEQA---AASFLKGLTVYYL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 172 IRKKALIdrsRP-QTIVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKCTvLKREFGFNDTINYKTENVSERLGHL-A 249
Cdd:PRK10754  132 LRKTYEI---KPdEQFLFHAAAGGVGLIACQWAKALG-AKLIGTVGSAQKAQ-RAKKAGAWQVINYREENIVERVKEItG 206
                         170
                  ....*....|..
gi 1972254588 250 PEGIDIYWDNVG 261
Cdd:PRK10754  207 GKKVRVVYDSVG 218
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
99-297 8.13e-08

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: 53.13  E-value: 8.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTgCIRLWTWTKYFVCDSSDLVKvnLPSS---RNFsPSVILSCaglsgitALLGIRk 174
Cdd:cd08269    56 GHEGWGRVVALGPGVRgLAVGDRVA-GLSGGAFAEYDLADADHAVP--LPSLldgQAF-PGEPLGC-------ALNVFR- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 175 kalidRSRP---QTIVVSGaAGSCGSLAGQIARIEGCSKVIGIcgsDDKCTVLK--REFGFNDTINYKTENVSERLGHLA 249
Cdd:cd08269   124 -----RGWIragKTVAVIG-AGFIGLLFLQLAAAAGARRVIAI---DRRPARLAlaRELGATEVVTDDSEAIVERVRELT 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1972254588 250 P-EGIDIYWDNVG-GVISDDVIRAMNNEGRVVlcgqIAVYNTDLPYPPPL 297
Cdd:cd08269   195 GgAGADVVIEAVGhQWPLDLAGELVAERGRLV----IFGYHQDGPRPVPF 240
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
25-264 8.65e-08

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: 53.30  E-value: 8.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  25 KVVIFvKRPGENNAPTIDCFDVVPIDSPSEKDItsdqcIVRTLFLSVDPA---QRCRMNPSTGvdylgpyeigEP-VDGM 100
Cdd:cd08252     2 KAIGF-TQPLPITDPDSLIDIELPKPVPGGRDL-----LVRVEAVSVNPVdtkVRAGGAPVPG----------QPkILGW 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 101 EGVGVVERVGSACTL-EVGDLV--TGCI-RLWTWTKYFVCDSSdLV--KvnlPSSRNFSPSVILScagLSGITA------ 168
Cdd:cd08252    66 DASGVVEAVGSEVTLfKVGDEVyyAGDItRPGSNAEYQLVDER-IVghK---PKSLSFAEAAALP---LTSLTAwealfd 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 169 LLGIRKkalIDRSRPQTIVVSGAAGSCGSLAGQIARIEGCSKVIGICG---SDDKCtvlkREFGFNDTINYKtENVSERL 245
Cdd:cd08252   139 RLGISE---DAENEGKTLLIIGGAGGVGSIAIQLAKQLTGLTVIATASrpeSIAWV----KELGADHVINHH-QDLAEQL 210
                         250       260
                  ....*....|....*....|....*...
gi 1972254588 246 GHLAPEGID-I--------YWDNVGGVI 264
Cdd:cd08252   211 EALGIEPVDyIfcltdtdqHWDAMAELI 238
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
165-282 5.89e-07

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: 50.83  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 165 GITALlgirkkALIDRSRPQT---IVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKcTVLKREFGFNDTINYKTENV 241
Cdd:cd08244   128 GRTAL------GLLDLATLTPgdvVLVTAAAGGLGSLLVQLAKAAG-ATVVGAAGGPAK-TALVRALGADVAVDYTRPDW 199
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1972254588 242 SERL-GHLAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCG 282
Cdd:cd08244   200 PDQVrEALGGGGVTVVLDGVGGAIGRAALALLAPGGRFLTYG 241
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
129-263 8.52e-07

Plant 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: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 50.37  E-value: 8.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 129 TWTKYFVCDSSDLVKVNlPSSrNFSPSVILSCAGLSGITALLGIRKKAlidrsRPQTIVVSGAaGSCGSLAGQIARIEGC 208
Cdd:cd08301   141 TFSEYTVVHVGCVAKIN-PEA-PLDKVCLLSCGVSTGLGAAWNVAKVK-----KGSTVAIFGL-GAVGLAVAEGARIRGA 212
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972254588 209 SKVIGICGSDDKCTVLKrEFGFNDTINYK--TENVSERLGHLAPEGIDIYWDNVGGV 263
Cdd:cd08301   213 SRIIGVDLNPSKFEQAK-KFGVTEFVNPKdhDKPVQEVIAEMTGGGVDYSFECTGNI 268
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
99-372 1.40e-06

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: 49.64  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGCIRLWTWTKYFVCDSSDLVKVNLPSSRNFSPSVIlscagLSGITALLGIRkkaL 177
Cdd:cd08292    63 GSEAVGVVDAVGEGVKgLQVGQRVAVAPVHGTWAEYFVAPADGLVPLPDGISDEVAAQLI-----AMPLSALMLLD---F 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 178 IDRSRPQTIVVSGAAGSCGSLAGQIARIEGCsKVIGICGSDDKCTVLKRefgFNDTINYKTEN------VSERLGHlapE 251
Cdd:cd08292   135 LGVKPGQWLIQNAAGGAVGKLVAMLAAARGI-NVINLVRRDAGVAELRA---LGIGPVVSTEQpgwqdkVREAAGG---A 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 252 GIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVYNTDLPYPPPLPEHTTkiIKERNIQreRYLVLMYKDEIDEAVAQL 331
Cdd:cd08292   208 PISVALDSVGGKLAGELLSLLGEGGTLVSFGSMSGEPMQISSGDLIFKQAT--VRGFWGG--RWSQEMSVEYRKRMIAEL 283
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1972254588 332 SEWLQQDKIKVK-ETIYDGLNAAPSAFVDMMNGKnIGKMLIR 372
Cdd:cd08292   284 LTLALKGQLLLPvEAVFDLGDAAKAAAASMRPGR-AGKVLLR 324
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
99-282 2.74e-06

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: 48.65  E-value: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLV--------------TG----CIRLW------------------------------- 128
Cdd:cd08278    60 GHEGAGVVEAVGSAVTgLKPGDHVvlsfascgecanclSGhpayCENFFplnfsgrrpdgstplslddgtpvhghffgqs 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 129 TWTKYFVCDSSDLVKV--NLPSSRnFSPsviLSCAGLSGITALLgirkKALidRSRP-QTIVVSGAaGSCGSLAGQIARI 205
Cdd:cd08278   140 SFATYAVVHERNVVKVdkDVPLEL-LAP---LGCGIQTGAGAVL----NVL--KPRPgSSIAVFGA-GAVGLAAVMAAKI 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972254588 206 EGCSKVIGICGSDDKcTVLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDNVG--GVIsDDVIRAMNNEGRVVLCG 282
Cdd:cd08278   209 AGCTTIIAVDIVDSR-LELAKELGATHVINPKEEDLVAAIREITGGGVDYALDTTGvpAVI-EQAVDALAPRGTLALVG 285
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
28-371 3.74e-06

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 48.10  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  28 IFVKRPGENNAPTIDCfdvVPIDSPSEKDItsdqcIVRTLFLSV---DPAQR-CRMNPSTGVDylgpyeigePVDGMEGV 103
Cdd:PTZ00354    5 VTLKGFGGVDVLKIGE---SPKPAPKRNDV-----LIKVSAAGVnraDTLQRqGKYPPPPGSS---------EILGLEVA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 104 GVVERVGS-ACTLEVGDLVTGCIRLWTWTKYFVCDSSDLVKVnlPSSRNFSpsvilSCAGLSG--ITALLGIRKKAliDR 180
Cdd:PTZ00354   68 GYVEDVGSdVKRFKEGDRVMALLPGGGYAEYAVAHKGHVMHI--PQGYTFE-----EAAAIPEafLTAWQLLKKHG--DV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 181 SRPQTIVVSGAAGSCGSLAGQIARIEGCSKVIGICgSDDKCTVLKrEFGFNDTINYKTE-NVSERLGHL-APEGIDIYWD 258
Cdd:PTZ00354  139 KKGQSVLIHAGASGVGTAAAQLAEKYGAATIITTS-SEEKVDFCK-KLAAIILIRYPDEeGFAPKVKKLtGEKGVNLVLD 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 259 NVGGVISDDVIRAMNNEGRVVLCGQIA---VYNTDLpypPPLPEHTTKII----KERNIQRERYLVLMYKDEIdeaVAQL 331
Cdd:PTZ00354  217 CVGGSYLSETAEVLAVDGKWIVYGFMGgakVEKFNL---LPLLRKRASIIfstlRSRSDEYKADLVASFEREV---LPYM 290
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1972254588 332 SEwlQQDKIKVKETIydGLNAAPSAFVDMMNGKNIGKMLI 371
Cdd:PTZ00354  291 EE--GEIKPIVDRTY--PLEEVAEAHTFLEQNKNIGKVVL 326
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
99-282 4.88e-06

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: 47.65  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLVTGcirLWTWTKYFVCDSSDLVKVnlPSSRNFSPSVilsCAGLsGITALLGIRkkal 177
Cdd:cd08255    25 GYSSVGRVVEVGSGVTgFKPGDRVFC---FGPHAERVVVPANLLVPL--PDGLPPERAA---LTAL-AATALNGVR---- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 178 idRSRPQ---TIVVSGAaGSCGSLAGQIARIEGCSKVIGICGSDDKCTvLKREFGFNDTINyktenvserlghlAPEGID 254
Cdd:cd08255    92 --DAEPRlgeRVAVVGL-GLVGLLAAQLAKAAGAREVVGVDPDAARRE-LAEALGPADPVA-------------ADTADE 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1972254588 255 IYWDNVGGVIS--------DDVIRAMNNEGRVVLCG 282
Cdd:cd08255   155 IGGRGADVVIEasgspsalETALRLLRDRGRVVLVG 190
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
99-372 1.27e-05

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: 46.38  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSAcTLEVGD--LVTGC-IRLWTWTKY--FVCDSSDLVkVNLPssRNFSP--SVILSCAGLsgiTALLG 171
Cdd:cd05280    62 GIDAAGTVVSSDDP-RFREGDevLVTGYdLGMNTDGGFaeYVRVPADWV-VPLP--EGLSLreAMILGTAGF---TAALS 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 172 IRKkaLID-RSRPQT--IVVSGAAGSCGSLAGQIARIEGCSkVIGICGSDDKCTVLKrEFGFNDTINYKT-ENVSERlgH 247
Cdd:cd05280   135 VHR--LEDnGQTPEDgpVLVTGATGGVGSIAVAILAKLGYT-VVALTGKEEQADYLK-SLGASEVLDREDlLDESKK--P 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 248 LAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAVYN---TDLPYppplpehttkiikernIQRERYLV----LMY 320
Cdd:cd05280   209 LLKARWAGAIDTVGGDVLANLLKQTKYGGVVASCGNAAGPElttTVLPF----------------ILRGVSLLgidsVNC 272
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972254588 321 KDEIDEAVAQL--SEW-LQQDKIKVKETiydGLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd05280   273 PMELRKQVWQKlaTEWkPDLLEIVVREI---SLEELPEAIDRLLAGKHRGRTVVK 324
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
99-298 3.48e-05

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


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 45.34  E-value: 3.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLV-----TGCIRLW-------------TWTKYFVCDS----SDLVKVN--------LP 147
Cdd:cd05278    59 GHEFVGEVVEVGSDVKrLKPGDRVsvpciTFCGRCRfcrrgyhahcengLWGWKLGNRIdggqAEYVRVPyadmnlakIP 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 148 SSRNFSPSVILSCAGLSGITA--LLGIRKKAlidrsrpqTIVVSGAaGSCGSLAGQIARIEGCSKVIGIcGSDDKCTVLK 225
Cdd:cd05278   139 DGLPDEDALMLSDILPTGFHGaeLAGIKPGS--------TVAVIGA-GPVGLCAVAGARLLGAARIIAV-DSNPERLDLA 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972254588 226 REFGFNDTINYKTENVSER-LGHLAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVlcGQIAVYNTDLPYPPPLP 298
Cdd:cd05278   209 KEAGATDIINPKNGDIVEQiLELTGGRGVDCVIEAVGFEETFEQAVKVVRPGGTI--ANVGVYGKPDPLPLLGE 280
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
85-368 1.14e-04

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: 43.51  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  85 VDYLGPYEIGEpVDGMEGVGVVERV---GSActLEVGDLVTGCIRLWTWTKYFVCDSSDLVKVnlPSSRNFSPSVILSCA 161
Cdd:cd08270    43 LKFAAERPDGA-VPGWDAAGVVERAaadGSG--PAVGARVVGLGAMGAWAELVAVPTGWLAVL--PDGVSFAQAATLPVA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 162 GLSGITALLgiRKKALIDRSrpqtIVVSGAAGSCGSLAGQIARIEGcSKVIGICGSDDKCTVLKREFGfndtinyktENV 241
Cdd:cd08270   118 GVTALRALR--RGGPLLGRR----VLVTGASGGVGRFAVQLAALAG-AHVVAVVGSPARAEGLRELGA---------AEV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 242 SERLGHLAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCG----QIAVYNTDLPYPPPLPehttkiikerniQRERYLV 317
Cdd:cd08270   182 VVGGSELSGAPVDLVVDSVGGPQLARALELLAPGGTVVSVGsssgEPAVFNPAAFVGGGGG------------RRLYTFF 249
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972254588 318 LMYKDEIDEAVAQLSEWLQQDKIKVKETIYDGLNAAPSAFVDMMNGKNIGK 368
Cdd:cd08270   250 LYDGEPLAADLARLLGLVAAGRLDPRIGWRGSWTEIDEAAEALLARRFRGK 300
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
97-254 1.26e-04

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: 43.48  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  97 VDGMEGVGVVERVGSACT-LEVGDLV----TG---------------CIRLW---------------------------- 128
Cdd:cd08277    58 ILGHEGAGIVESVGEGVTnLKPGDKViplfIGqcgecsncrsgktnlCQKYRanesglmpdgtsrftckgkkiyhflgts 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 129 TWTKYFVCDSSDLVKVNlPSSrNFSPSVILSCAGLSGITALLgirKKALIDRSrpQTIVVSGaAGSCGSLAGQIARIEGC 208
Cdd:cd08277   138 TFSQYTVVDENYVAKID-PAA-PLEHVCLLGCGFSTGYGAAW---NTAKVEPG--STVAVFG-LGAVGLSAIMGAKIAGA 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1972254588 209 SKVIGICGSDDKCTVLKrEFGFNDTINYK--TENVSERLGHLAPEGID 254
Cdd:cd08277   210 SRIIGVDINEDKFEKAK-EFGATDFINPKdsDKPVSEVIREMTGGGVD 256
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
97-364 3.90e-04

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: 41.92  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  97 VDGMEGVGVVERVGSAC-TLEVGDLV----------------------------TGCIRLWTWTKYFVCDSSDLVKvnLP 147
Cdd:cd08245    56 VPGHEIVGEVVEVGAGVeGRKVGDRVgvgwlvgscgrceycrrglenlcqkavnTGYTTQGGYAEYMVADAEYTVL--LP 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 148 SSRNFSPSVILSCAGlsgITALLGIRKKALIDRSRpqtIVVSGAAGScGSLAGQIARIEGcSKVIGICGSDDKCTvLKRE 227
Cdd:cd08245   134 DGLPLAQAAPLLCAG---ITVYSALRDAGPRPGER---VAVLGIGGL-GHLAVQYARAMG-FETVAITRSPDKRE-LARK 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 228 FGFNDTINYKTEN-VSERLGhlapeGIDIYWDNV-GGVISDDVIRAMNNEGRVVLCGqiavyntdLPY-PPPLPEHTTKI 304
Cdd:cd08245   205 LGADEVVDSGAELdEQAAAG-----GADVILVTVvSGAAAEAALGGLRRGGRIVLVG--------LPEsPPFSPDIFPLI 271
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972254588 305 IKERNIQRERYLVLMYKDEIDEAVAqlsewlqqdKIKVK---ETIydGLNAAPSAFVDMMNGK 364
Cdd:cd08245   272 MKRQSIAGSTHGGRADLQEALDFAA---------EGKVKpmiETF--PLDQANEAYERMEKGD 323
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
162-372 7.98e-04

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: 41.00  E-value: 7.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 162 GLSGITALLGIrkKALIDRS-RPQ--TIVVSGAAGSCGSLAGQIARIEGCSkVIGICGSDDKCTVLkREFGFNDTINYKT 238
Cdd:TIGR02823 124 GTAGFTAALSV--MALERNGlTPEdgPVLVTGATGGVGSLAVAILSKLGYE-VVASTGKAEEEDYL-KELGASEVIDRED 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 239 ENVSERlgHLAPEGIDIYWDNVGGVISDDVIRAMNNEGRVVLCGQIAvyNTDLP---YPPPLpehttkiikeRNIQrery 315
Cdd:TIGR02823 200 LSPPGK--PLEKERWAGAVDTVGGHTLANVLAQLKYGGAVAACGLAG--GPDLPttvLPFIL----------RGVS---- 261
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972254588 316 L-----VLMYKDEIDEAVAQLSEWLqqdKIKVKETIYD--GLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:TIGR02823 262 LlgidsVYCPMALREAAWQRLATDL---KPRNLESITReiTLEELPEALEQILAGQHRGRTVVD 322
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
99-263 1.20e-03

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: 40.44  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588  99 GMEGVGVVERVGSACT-LEVGDLV-----------------------------------TGCIRLW-------------T 129
Cdd:cd08281    66 GHEAAGVVVEVGEGVTdLEVGDHVvlvfvpscghcrpcaegrpalcepgaaangagtllSGGRRLRlrggeinhhlgvsA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 130 WTKYFVCDSSDLVKV--NLPssrnFSPSVILSCAGLSGITALLgirKKALIDRSRPQTIVVSGAAGSCGSLAgqiARIEG 207
Cdd:cd08281   146 FAEYAVVSRRSVVKIdkDVP----LEIAALFGCAVLTGVGAVV---NTAGVRPGQSVAVVGLGGVGLSALLG---AVAAG 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972254588 208 CSKVIGICGSDDKCTvLKREFGFNDTINYKTENVSERLGHLAPEGIDIYWDNVGGV 263
Cdd:cd08281   216 ASQVVAVDLNEDKLA-LARELGATATVNAGDPNAVEQVRELTGGGVDYAFEMAGSV 270
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
190-299 1.96e-03

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


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 39.92  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 190 GAAGSCgSLAGqiARIEGCSKVIGIcGSDDKCTVLKREFGFNDTINYKTENVSERLGHL-APEGIDIYWDNVGGV-ISDD 267
Cdd:cd08285   176 GPVGLM-AVAG--ARLRGAGRIIAV-GSRPNRVELAKEYGATDIVDYKNGDVVEQILKLtGGKGVDAVIIAGGGQdTFEQ 251
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1972254588 268 VIRAMNNEGRVvlcGQIAVYNTDLPYPPPLPE 299
Cdd:cd08285   252 ALKVLKPGGTI---SNVNYYGEDDYLPIPREE 280
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
104-372 2.49e-03

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: 39.56  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 104 GVVERVGS--ACTLEVGDLVTGCirLW-------TWTKYFVCDSSDLVKVNLPSSRNFS----PSVILsCAGlsgiTALL 170
Cdd:cd08247    68 GVIVKVGSnvASEWKVGDEVCGI--YPhpyggqgTLSQYLLVDPKKDKKSITRKPENISleeaAAWPL-VLG----TAYQ 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 171 GI--RKKALIDRSRpqtIVVSGAAGSCGSLAGQIARIE-GCSKVIGICGSddKCTVLKREFGFNDTINYKTENVSERLGH 247
Cdd:cd08247   141 ILedLGQKLGPDSK---VLVLGGSTSVGRFAIQLAKNHyNIGTVVGTCSS--RSAELNKKLGADHFIDYDAHSGVKLLKP 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972254588 248 L-----APEGIDIYWDNVGG--VI--SDDVIRAMNNEGR-VVLCGQ-IAVYNTD-LPYPPPLPEHTTKIIKERNIQRERY 315
Cdd:cd08247   216 VlenvkGQGKFDLILDCVGGydLFphINSILKPKSKNGHyVTIVGDyKANYKKDtFNSWDNPSANARKLFGSLGLWSYNY 295
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972254588 316 LVLMYkDEIDEAVAQLSEWLQQDKIKVK-ETIYDgLNAAPSAFVDMMNGKNIGKMLIR 372
Cdd:cd08247   296 QFFLL-DPNADWIEKCAELIADGKVKPPiDSVYP-FEDYKEAFERLKSNRAKGKVVIK 351
 
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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