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Conserved domains on  [gi|156849077|ref|XP_001647419|]
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uncharacterized protein Kpol_1018p94 [Vanderwaltozyma polyspora DSM 70294]

Protein Classification

AST1_like domain-containing protein( domain architecture ID 10169542)

AST1_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 38-411 1.28e-151

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: 433.23  E-value: 1.28e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTyenKIKTPI----GSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIGLGREYFGVISDIGSKLe 113
Cdd:cd08247    2 KALTFKNNTSPLTIT---TIKLPLpncyKDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKGLGRDYSGVIVKVGSNV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 114 sDNRWKIGDEVMGIYYHPHIGYGSLQTSILVDPKQD--PLVLKPENVTMPEAGGSLFCLASAFEILEKLNslKKLTPNAN 191
Cdd:cd08247   78 -ASEWKVGDEVCGIYPHPYGGQGTLSQYLLVDPKKDkkSITRKPENISLEEAAAWPLVLGTAYQILEDLG--QKLGPDSK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 192 ILINGGTSSVGLFALQLLKNYYHIvSKVTIVTSGTGPKVIKqhMPGFEKdfiFIDYLACRGKasKPLLKLLEDNTytyfd 271
Cdd:cd08247  155 VLVLGGSTSVGRFAIQLAKNHYNI-GTVVGTCSSRSAELNK--KLGADH---FIDYDAHSGV--KLLKPVLENVK----- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 272 eengtesienySQGKYDIVLDFIGGYDILSQSQSLIHS---GGHYVTTVGDYVADYKTDVFEHWDNPSASARKMFGNI-L 347
Cdd:cd08247  222 -----------GQGKFDLILDCVGGYDLFPHINSILKPkskNGHYVTIVGDYKANYKKDTFNSWDNPSANARKLFGSLgL 290

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156849077 348 WSYNYTHYKFDPNGktELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILKV 411
Cdd:cd08247  291 WSYNYQFFLLDPNA--DWIEKCAELIADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVIKV 352
 
Name Accession Description Interval E-value
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 38-411 1.28e-151

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: 433.23  E-value: 1.28e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTyenKIKTPI----GSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIGLGREYFGVISDIGSKLe 113
Cdd:cd08247    2 KALTFKNNTSPLTIT---TIKLPLpncyKDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKGLGRDYSGVIVKVGSNV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 114 sDNRWKIGDEVMGIYYHPHIGYGSLQTSILVDPKQD--PLVLKPENVTMPEAGGSLFCLASAFEILEKLNslKKLTPNAN 191
Cdd:cd08247   78 -ASEWKVGDEVCGIYPHPYGGQGTLSQYLLVDPKKDkkSITRKPENISLEEAAAWPLVLGTAYQILEDLG--QKLGPDSK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 192 ILINGGTSSVGLFALQLLKNYYHIvSKVTIVTSGTGPKVIKqhMPGFEKdfiFIDYLACRGKasKPLLKLLEDNTytyfd 271
Cdd:cd08247  155 VLVLGGSTSVGRFAIQLAKNHYNI-GTVVGTCSSRSAELNK--KLGADH---FIDYDAHSGV--KLLKPVLENVK----- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 272 eengtesienySQGKYDIVLDFIGGYDILSQSQSLIHS---GGHYVTTVGDYVADYKTDVFEHWDNPSASARKMFGNI-L 347
Cdd:cd08247  222 -----------GQGKFDLILDCVGGYDLFPHINSILKPkskNGHYVTIVGDYKANYKKDTFNSWDNPSANARKLFGSLgL 290

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156849077 348 WSYNYTHYKFDPNGktELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILKV 411
Cdd:cd08247  291 WSYNYQFFLLDPNA--DWIEKCAELIADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVIKV 352
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 38-412 6.29e-29

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: 115.25  E-value: 6.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTYENkIKTP-IGSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIGLGREYFGVISDIGsklESDN 116
Cdd:COG0604    2 KAIVITEFGGPEVLELEE-VPVPePGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVG---EGVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 117 RWKIGDEVMGiyyhpHIGYGSLQTSILVDPKQdpLVLKPENVTMPEAGGSLFCLASAFEILEKLNslkKLTPNANILING 196
Cdd:COG0604   78 GFKVGDRVAG-----LGRGGGYAEYVVVPADQ--LVPLPDGLSFEEAAALPLAGLTAWQALFDRG---RLKPGETVLVHG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 197 GTSSVGLFALQLLKNY-YHIvskvtIVTSGTGPKV--IKQHmpGFEkdfIFIDYlacrgkaskpllklledntytyfDEE 273
Cdd:COG0604  148 AAGGVGSAAVQLAKALgARV-----IATASSPEKAelLRAL--GAD---HVIDY-----------------------REE 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 274 NGTESIENYSQGK-YDIVLDFIGGyDILSQSQSLIHSGGHYVTTVGDYVADYKTDVFEHWdnpsASARKMFGNILWSYny 352
Cdd:COG0604  195 DFAERVRALTGGRgVDVVLDTVGG-DTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLL----LKGLTLTGFTLFAR-- 267

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 353 thykfDPNGKTELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILKVE 412
Cdd:COG0604  268 -----DPAERRAALAELARLLAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 68-409 2.71e-13

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 69.72  E-value: 2.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077    68 VDVRYVGLNPVDLMIkngynQQGFY-GEIGLGREYFGVISDIGSkleSDNRWKIGDEVMGiyyhphIGYGSLQTSILVDP 146
Cdd:smart00829   1 IEVRAAGLNFRDVLI-----ALGLYpGEAVLGGECAGVVTRVGP---GVTGLAVGDRVMG------LAPGAFATRVVTDA 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077   147 KQdpLVLKPENVTMPEAGG----------SLFCLAsafeileklnslkKLTPNANILINGGTSSVGLFALQLLKnyyHIV 216
Cdd:smart00829  67 RL--VVPIPDGWSFEEAATvpvvfltayyALVDLA-------------RLRPGESVLIHAAAGGVGQAAIQLAR---HLG 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077   217 SKVtIVTSGTGPKviKQHM--PGFEKDFIFidylacrgkaskpllklleDNTYTYFDEEngtesIENYSQGK-YDIVLDF 293
Cdd:smart00829 129 AEV-FATAGSPEK--RDFLraLGIPDDHIF-------------------SSRDLSFADE-----ILRATGGRgVDVVLNS 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077   294 IGGyDILSQSQSLIHSGGHYVtTVGdyvadyKTDVfehWDNPSASARKMFGNIlwSY---NYTHYKFDPNGKTELIEKCA 370
Cdd:smart00829 182 LSG-EFLDASLRCLAPGGRFV-EIG------KRDI---RDNSQLAMAPFRPNV--SYhavDLDALEEGPDRIRELLAEVL 248

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 156849077   371 ELLGKRYVKCIVDNVYDWKDYKEAFNYMklQRAQ--GKLIL 409
Cdd:smart00829 249 ELFAEGVLRPLPVTVFPISDAEDAFRYM--QQGKhiGKVVL 287
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 97-414 1.68e-11

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 65.05  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  97 LGREYFGVISDIGSkleSDNRWKIGDEVMGIYyhPHIGYGSLQTSilvdpKQDPLVLKPENVTMPEAGGSLFCLASAFEI 176
Cdd:PTZ00354  62 LGLEVAGYVEDVGS---DVKRFKEGDRVMALL--PGGGYAEYAVA-----HKGHVMHIPQGYTFEEAAAIPEAFLTAWQL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 177 LEKLNSLKKltpNANILINGGTSSVGLFALQLLKNYYhivsKVTIVTSGTGPKV--IKQHmpgfeKDFIFIDYLACRGKA 254
Cdd:PTZ00354 132 LKKHGDVKK---GQSVLIHAGASGVGTAAAQLAEKYG----AATIITTSSEEKVdfCKKL-----AAIILIRYPDEEGFA 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 255 SKPLLKLLEDNTYTYFDEENGTESIENYSQGKYD---IVLDFIGG-----YDILsqsqSLIHSGGHYV-TTVGDYVADYK 325
Cdd:PTZ00354 200 PKVKKLTGEKGVNLVLDCVGGSYLSETAEVLAVDgkwIVYGFMGGakvekFNLL----PLLRKRASIIfSTLRSRSDEYK 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 326 TDVFEHWdnpsasarkmfgnilwsynythykfdpngKTELIekcaELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQG 405
Cdd:PTZ00354 276 ADLVASF-----------------------------EREVL----PYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIG 322


                 ....*....
gi 156849077 406 KLILKVEKF 414
Cdd:PTZ00354 323 KVVLTVNEP 331
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
285-409 1.11e-09

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 56.18  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  285 GKYDIVLDFIGGyDILSQSQSLIHSGGHYVTTVGDYVADyktdvfehwDNPSASARKMFGNILWSYNYTHykfdPNGKTE 364
Cdd:pfam13602  21 EGVDVVLDTVGG-EAFEASLRVLPGGGRLVTIGGPPLSA---------GLLLPARKRGGRGVKYLFLFVR----PNLGAD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 156849077  365 LIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLIL 409
Cdd:pfam13602  87 ILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
 
Name Accession Description Interval E-value
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 38-411 1.28e-151

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: 433.23  E-value: 1.28e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTyenKIKTPI----GSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIGLGREYFGVISDIGSKLe 113
Cdd:cd08247    2 KALTFKNNTSPLTIT---TIKLPLpncyKDNEIVVKVHAAALNPVDLKLYNSYTFHFKVKEKGLGRDYSGVIVKVGSNV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 114 sDNRWKIGDEVMGIYYHPHIGYGSLQTSILVDPKQD--PLVLKPENVTMPEAGGSLFCLASAFEILEKLNslKKLTPNAN 191
Cdd:cd08247   78 -ASEWKVGDEVCGIYPHPYGGQGTLSQYLLVDPKKDkkSITRKPENISLEEAAAWPLVLGTAYQILEDLG--QKLGPDSK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 192 ILINGGTSSVGLFALQLLKNYYHIvSKVTIVTSGTGPKVIKqhMPGFEKdfiFIDYLACRGKasKPLLKLLEDNTytyfd 271
Cdd:cd08247  155 VLVLGGSTSVGRFAIQLAKNHYNI-GTVVGTCSSRSAELNK--KLGADH---FIDYDAHSGV--KLLKPVLENVK----- 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 272 eengtesienySQGKYDIVLDFIGGYDILSQSQSLIHS---GGHYVTTVGDYVADYKTDVFEHWDNPSASARKMFGNI-L 347
Cdd:cd08247  222 -----------GQGKFDLILDCVGGYDLFPHINSILKPkskNGHYVTIVGDYKANYKKDTFNSWDNPSANARKLFGSLgL 290

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156849077 348 WSYNYTHYKFDPNGktELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILKV 411
Cdd:cd08247  291 WSYNYQFFLLDPNA--DWIEKCAELIADGKVKPPIDSVYPFEDYKEAFERLKSNRAKGKVVIKV 352
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 38-409 3.93e-36

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: 134.23  E-value: 3.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFqTKTGPVDFTYENKIKTP-IGSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGE--IGLGREYFGVISDIGSKles 114
Cdd:cd05289    2 KAVRI-HEYGGPEVLELADVPTPePGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTlpLIPGHDVAGVVVAVGPG--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 115 DNRWKIGDEVMGiyYHPHIGYGSLQTSILVDPKQdpLVLKPENVTMPEAGgSLFCLA-SAFEILEKLNSLKkltPNANIL 193
Cdd:cd05289   78 VTGFKVGDEVFG--MTPFTRGGAYAEYVVVPADE--LALKPANLSFEEAA-ALPLAGlTAWQALFELGGLK---AGQTVL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 194 INGGTSSVGLFALQLLKNYyhivskvtivtsgtGPKVIkqhmpgfekdfifidylACRGKASKPLLK-LLEDNTYTYfde 272
Cdd:cd05289  150 IHGAAGGVGSFAVQLAKAR--------------GARVI-----------------ATASAANADFLRsLGADEVIDY--- 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 273 enGTESIENYSQ-GKYDIVLDFIGGyDILSQSQSLIHSGGHYVTTVGDyvadyktdvfehwdnPSASARKMFGNIlwsyN 351
Cdd:cd05289  196 --TKGDFERAAApGGVDAVLDTVGG-ETLARSLALVKPGGRLVSIAGP---------------PPAEQAAKRRGV----R 253

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 156849077 352 YTHYKFDPNGktELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLIL 409
Cdd:cd05289  254 AGFVFVEPDG--EQLAELAELVEAGKLRPVVDRVFPLEDAAEAHERLESGHARGKVVL 309
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 68-409 2.24e-34

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: 130.03  E-value: 2.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  68 VDVRYVGLNPVDLMIKNGynqqGFYGEIG------LGREYFGVISDIGSKlesDNRWKIGDEVMGiyYHPHIGYGSLQTS 141
Cdd:cd08267   31 VKVHAASVNPVDWKLRRG----PPKLLLGrpfppiPGMDFAGEVVAVGSG---VTRFKVGDEVFG--RLPPKGGGALAEY 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 142 ILVDPkqDPLVLKPENVTMPEAGGSLFCLASAFEILEKLNSLKkltPNANILINGGTSSVGLFALQLLKnyyHIVSKVTI 221
Cdd:cd08267  102 VVAPE--SGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVK---PGQRVLINGASGGVGTFAVQIAK---ALGAHVTG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 222 VTSgtGPKVikqhmpgfekDFifidylaCRGkaskpllkLLEDNTYTYFDEENGTESienYSQGKYDIVLDFIGGYDI-L 300
Cdd:cd08267  174 VCS--TRNA----------EL-------VRS--------LGADEVIDYTTEDFVALT---AGGEKYDVIFDAVGNSPFsL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 301 SQSQSLIHSGGHYVTTVGdyvadyktdvfehwDNPSASARKMFGNILWSYNYTHYK-FDPNGKTELIEKCAELLGKRYVK 379
Cdd:cd08267  224 YRASLALKPGGRYVSVGG--------------GPSGLLLVLLLLPLTLGGGGRRLKfFLAKPNAEDLEQLAELVEEGKLK 289

                        330       340       350
                 ....*....|....*....|....*....|
gi 156849077 380 CIVDNVYDWKDYKEAFNYMKLQRAQGKLIL 409
Cdd:cd08267  290 PVIDSVYPLEDAPEAYRRLKSGRARGKVVI 319
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 38-412 6.29e-29

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: 115.25  E-value: 6.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTYENkIKTP-IGSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIGLGREYFGVISDIGsklESDN 116
Cdd:COG0604    2 KAIVITEFGGPEVLELEE-VPVPePGPGEVLVRVKAAGVNPADLLIRRGLYPLPPGLPFIPGSDAAGVVVAVG---EGVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 117 RWKIGDEVMGiyyhpHIGYGSLQTSILVDPKQdpLVLKPENVTMPEAGGSLFCLASAFEILEKLNslkKLTPNANILING 196
Cdd:COG0604   78 GFKVGDRVAG-----LGRGGGYAEYVVVPADQ--LVPLPDGLSFEEAAALPLAGLTAWQALFDRG---RLKPGETVLVHG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 197 GTSSVGLFALQLLKNY-YHIvskvtIVTSGTGPKV--IKQHmpGFEkdfIFIDYlacrgkaskpllklledntytyfDEE 273
Cdd:COG0604  148 AAGGVGSAAVQLAKALgARV-----IATASSPEKAelLRAL--GAD---HVIDY-----------------------REE 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 274 NGTESIENYSQGK-YDIVLDFIGGyDILSQSQSLIHSGGHYVTTVGDYVADYKTDVFEHWdnpsASARKMFGNILWSYny 352
Cdd:COG0604  195 DFAERVRALTGGRgVDVVLDTVGG-DTLARSLRALAPGGRLVSIGAASGAPPPLDLAPLL----LKGLTLTGFTLFAR-- 267

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 353 thykfDPNGKTELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILKVE 412
Cdd:COG0604  268 -----DPAERRAALAELARLLAAGKLRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 67-332 1.76e-26

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: 107.02  E-value: 1.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  67 VVDVRYVGLNPVDLMIKNGYNQQGFYGEIGLGREYFGVISDIGSKLESdnrWKIGDEVMGiyyHPHIG------------ 134
Cdd:cd05188    3 LVRVEAAGLCGTDLHIRRGGYPPPPKLPLILGHEGAGVVVEVGPGVTG---VKVGDRVVV---LPNLGcgtcelcrelcp 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 135 ---------YGSLQTSILVDPKQdpLVLKPENVTMPEAGGSLFCLASAFEILEKLNslkKLTPNANILINGGtSSVGLFA 205
Cdd:cd05188   77 gggilgeglDGGFAEYVVVPADN--LVPLPDGLSLEEAALLPEPLATAYHALRRAG---VLKPGDTVLVLGA-GGVGLLA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 206 LQLLKNYYHIVskvtIVTSGTGPKvikqhmpgFEKdfifidylacrgkaskpLLKLLEDNTYTYfDEENGTESIENYSQG 285
Cdd:cd05188  151 AQLAKAAGARV----IVTDRSDEK--------LEL-----------------AKELGADHVIDY-KEEDLEEELRLTGGG 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 156849077 286 KYDIVLDFIGGYDILSQSQSLIHSGGHYVTTVGDYVADYKTDVFEHW 332
Cdd:cd05188  201 GADVVIDAVGGPETLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLL 247
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 56-410 1.14e-23

Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member of the medium chain dehydrogenase/ reductase (MDR) family. Riticulons are endoplasmic reticulum associated proteins involved in membrane trafficking and neuroendocrine secretion. The MDR/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 101.15  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  56 KIKTPI--GSSKLVVDVRYVGLNPVDLMIKNGY----------NQQGFYGEIG----LGREYFGVISDIGSKLesdNRWK 119
Cdd:cd08248   20 NARIPVirKPNQVLIKVHAASVNPIDVLMRSGYgrtllnkkrkPQSCKYSGIEfpltLGRDCSGVVVDIGSGV---KSFE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 120 IGDEVMGIYyhPHIGYGSLQTSILVDPKQdpLVLKPENVTMPEAGGSLF--CLA-SAFEILEKLNslKKLTPNANILING 196
Cdd:cd08248   97 IGDEVWGAV--PPWSQGTHAEYVVVPENE--VSKKPKNLSHEEAASLPYagLTAwSALVNVGGLN--PKNAAGKRVLILG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 197 GTSSVGLFALQLLKNYyhivsKVTIVTSgtgpkvikqhmpgfekdfifidylaCRGKASkPLLKLL-EDNTytyFDEENG 275
Cdd:cd08248  171 GSGGVGTFAIQLLKAW-----GAHVTTT-------------------------CSTDAI-PLVKSLgADDV---IDYNNE 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 276 TESIENYSQGKYDIVLDFIGGYDIlSQSQSLIHSGGHYVTTVGDYVADykTD--------VFEHWDNPSASARKMFGNIL 347
Cdd:cd08248  217 DFEEELTERGKFDVILDTVGGDTE-KWALKLLKKGGTYVTLVSPLLKN--TDklglvggmLKSAVDLLKKNVKSLLKGSH 293

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156849077 348 WSYNYthykFDPNGktELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILK 410
Cdd:cd08248  294 YRWGF----FSPSG--SALDELAKLVEDGKIKPVIDKVFPFEEVPEAYEKVESGHARGKTVIK 350
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 66-411 1.45e-20

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: 91.88  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  66 LVVDVRYVGLNPVDLMIKngynqQGFY-----GEIGLGREYFGVISDIGsklESDNRWKIGDEVMGIYYhphigYGSLQT 140
Cdd:cd08275   29 VRVRVEACGLNFADLMAR-----QGLYdsapkPPFVPGFECAGTVEAVG---EGVKDFKVGDRVMGLTR-----FGGYAE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 141 SILVDPKQdpLVLKPENVTMPEAGGSLFCLASAFEILEKLNSLKkltPNANILIN---GGtssVGLFALQLLKnyyhIVS 217
Cdd:cd08275   96 VVNVPADQ--VFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLR---PGQSVLVHsaaGG---VGLAAGQLCK----TVP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 218 KVTIVtsgtgpkvikqhmpgfekdfifidylacrGKASKPLLKLLEDNTYTY-FDE--ENGTESIENYSQGKYDIVLDFI 294
Cdd:cd08275  164 NVTVV-----------------------------GTASASKHEALKENGVTHvIDYrtQDYVEEVKKISPEGVDIVLDAL 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 295 GGyDILSQSQSLIHSGGHYVTtvgdY-VADYKTdvfehwdnpsASARKMFgNILWSYNYTHyKFDP------N------- 360
Cdd:cd08275  215 GG-EDTRKSYDLLKPMGRLVV----YgAANLVT----------GEKRSWF-KLAKKWWNRP-KVDPmkliseNksvlgfn 277

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 361 -----GKTELIEKCAELLGKRY----VKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILKV 411
Cdd:cd08275  278 lgwlfEERELLTEVMDKLLKLYeegkIKPKIDSVFPFEEVGEAMRRLQSRKNIGKVVLTP 337
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 38-318 2.23e-20

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: 91.49  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTYEnkIKTP-IGSSKLVVDVRYVGLNPVDLMIKnGYNQQGFYGEIgLGREYFGVISDIGSKLEsdn 116
Cdd:cd08249    2 KAAVLTGPGGGLLVVVD--VPVPkPGPDEVLVKVKAVALNPVDWKHQ-DYGFIPSYPAI-LGCDFAGTVVEVGSGVT--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 117 RWKIGDEVMGI---YYHPHIGYGSLQTSILVDPKqdpLVLK-PENVTMPEAGGSLFCLASA----FEILE-KLNSLKKLT 187
Cdd:cd08249   75 RFKVGDRVAGFvhgGNPNDPRNGAFQEYVVADAD---LTAKiPDNISFEEAATLPVGLVTAalalFQKLGlPLPPPKPSP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 188 PNAN--ILINGGTSSVGLFALQLLKNYYHIVskvtIVTSGTgpkviKQHmpgfekdfifiDYlacrgkaskpLLKLLEDN 265
Cdd:cd08249  152 ASKGkpVLIWGGSSSVGTLAIQLAKLAGYKV----ITTASP-----KNF-----------DL----------VKSLGADA 201

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 266 TYTYFDEEnGTESIENYSQGKYDIVLDFIG-------GYDILSQSqslihSGGHYVTTVG 318
Cdd:cd08249  202 VFDYHDPD-VVEDIRAATGGKLRYALDCIStpesaqlCAEALGRS-----GGGKLVSLLP 255
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 68-409 1.47e-19

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: 88.39  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  68 VDVRYVGLNPVDLMIKNGynqQGFYGEIGLGREYFGVISDIGSKlesDNRWKIGDEVMGIyyhphiGYGSLQTSILVDpk 147
Cdd:cd05195    5 VEVKAAGLNFRDVLVALG---LLPGDETPLGLECSGIVTRVGSG---VTGLKVGDRVMGL------APGAFATHVRVD-- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 148 QDPLVLKPENVTMPEAGGSLFCLASAFEILeklNSLKKLTPNANILINGGTSSVGLFALQLLKnyyHIVSKVtIVTSGTG 227
Cdd:cd05195   71 ARLVVKIPDSLSFEEAATLPVAYLTAYYAL---VDLARLQKGESVLIHAAAGGVGQAAIQLAQ---HLGAEV-FATVGSE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 228 PKviKQHMpgfEKDFIFIDYLAcrgkaskpllklleDNTYTYFDEEngtesIENYSQGKY-DIVLDFIGGyDILSQSQSL 306
Cdd:cd05195  144 EK--REFL---RELGGPVDHIF--------------SSRDLSFADG-----ILRATGGRGvDVVLNSLSG-ELLRASWRC 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 307 IHSGGHYVtTVGdyvadyKTDVfehWDNPSASARKMFGNIlwSYnythYKFD--------PNGKTELIEKCAELLGKRYV 378
Cdd:cd05195  199 LAPFGRFV-EIG------KRDI---LSNSKLGMRPFLRNV--SF----SSVDldqlarerPELLRELLREVLELLEAGVL 262

                        330       340       350
                 ....*....|....*....|....*....|.
gi 156849077 379 KCIVDNVYDWKDYKEAFNYMKLQRAQGKLIL 409
Cdd:cd05195  263 KPLPPTVVPSASEIDAFRLMQSGKHIGKVVL 293
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 62-409 2.69e-16

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: 79.02  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  62 GSSKLVVDVRYVGLNPVDLMikngynQ-QGFYG------EIgLGREYFGVISDIGsklESDNRWKIGDEVMGIYyhPHIG 134
Cdd:cd05276   26 GPGEVLIRVAAAGVNRADLL------QrQGLYPpppgasDI-LGLEVAGVVVAVG---PGVTGWKVGDRVCALL--AGGG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 135 YGSLqtsILVDPKQdpLVLKPENVTMPEAGG----------SLFCLAsafeileklnslkKLTPNANILINGGTSSVGLF 204
Cdd:cd05276   94 YAEY---VVVPAGQ--LLPVPEGLSLVEAAAlpevfftawqNLFQLG-------------GLKAGETVLIHGGASGVGTA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 205 ALQLLKNYYHIVskvtIVTSGTGPKVikqhmpgfekdfifidyLACRgkaskpllKLLEDNTYTYfDEENGTESIENYSQ 284
Cdd:cd05276  156 AIQLAKALGARV----IATAGSEEKL-----------------EACR--------ALGADVAINY-RTEDFAEEVKEATG 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 285 GK-YDIVLDFIGGyDILSQSQSLIHSGGHYVtTVGdYVADYKTDVFehwdnpsasARKMF-------GNILWSYnythyk 356
Cdd:cd05276  206 GRgVDVILDMVGG-DYLARNLRALAPDGRLV-LIG-LLGGAKAELD---------LAPLLrkrltltGSTLRSR------ 267

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 156849077 357 fDPNGKTELI----EKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLIL 409
Cdd:cd05276  268 -SLEEKAALAaafrEHVWPLFASGRIRPVIDKVFPLEEAAEAHRRMESNEHIGKIVL 323
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 38-411 4.11e-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: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 75.67  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTYENKIKTPIGSSKLVVDVRYVGLNPVDLMIKNGynqQGFYGE----IgLGREYFGVISDIGsklE 113
Cdd:cd08272    2 KALVLESFGGPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRG---GAAARPplpaI-LGCDVAGVVEAVG---E 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 114 SDNRWKIGDEVmgIYYHPHIGY--GSLQTSILVDpkQDPLVLKPENVTMPEAGGSLFCLASAFEIL-EKLNslkkLTPNA 190
Cdd:cd08272   75 GVTRFRVGDEV--YGCAGGLGGlqGSLAEYAVVD--ARLLALKPANLSMREAAALPLVGITAWEGLvDRAA----VQAGQ 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 191 NILINGGTSSVGLFALQLLKnyyHIVSKVTIVTSGTGPKVIKQHmpGfeKDFIfIDYlacrgkaskpllklledntytyf 270
Cdd:cd08272  147 TVLIHGGAGGVGHVAVQLAK---AAGARVYATASSEKAAFARSL--G--ADPI-IYY----------------------- 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 271 dEENGTESIENYSQGK-YDIVLDFIGGyDILSQSQSLIHSGGHYVTTVGDYVADYKTdvfehwdnpsASARkmfgNILWS 349
Cdd:cd08272  196 -RETVVEYVAEHTGGRgFDVVFDTVGG-ETLDASFEAVALYGRVVSILGGATHDLAP----------LSFR----NATYS 259

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156849077 350 YNYT----HYKFDPNGKTELIEKCAELLGKRYVKCIVDN-VYDWKDYKEAFNYMKLQRAQGKLILKV 411
Cdd:cd08272  260 GVFTllplLTGEGRAHHGEILREAARLVERGQLRPLLDPrTFPLEEAAAAHARLESGSARGKIVIDV 326
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 38-211 7.26e-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: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 71.92  E-value: 7.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTYENKIKTPIGSSKLVVDVRYVGLNPVD-LMIKNGYNQQGfYGEIgLGREYFGVISDIGSKLESdn 116
Cdd:cd08271    2 KAWVLPKPGAALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDwKVIAWGPPAWS-YPHV-PGVDGAGVVVAVGAKVTG-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 117 rWKIGDEVMgiyYHPHIG-YGSLQTSILVDpkQDPLVLKPENVTMPEAGGSLFCLASAFEILEKLNslkKLTPNANILIN 195
Cdd:cd08271   78 -WKVGDRVA---YHASLArGGSFAEYTVVD--ARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKL---RIEAGRTILIT 148

                        170
                 ....*....|....*.
gi 156849077 196 GGTSSVGLFALQLLKN 211
Cdd:cd08271  149 GGAGGVGSFAVQLAKR 164
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 68-409 2.71e-13

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 69.72  E-value: 2.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077    68 VDVRYVGLNPVDLMIkngynQQGFY-GEIGLGREYFGVISDIGSkleSDNRWKIGDEVMGiyyhphIGYGSLQTSILVDP 146
Cdd:smart00829   1 IEVRAAGLNFRDVLI-----ALGLYpGEAVLGGECAGVVTRVGP---GVTGLAVGDRVMG------LAPGAFATRVVTDA 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077   147 KQdpLVLKPENVTMPEAGG----------SLFCLAsafeileklnslkKLTPNANILINGGTSSVGLFALQLLKnyyHIV 216
Cdd:smart00829  67 RL--VVPIPDGWSFEEAATvpvvfltayyALVDLA-------------RLRPGESVLIHAAAGGVGQAAIQLAR---HLG 128

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077   217 SKVtIVTSGTGPKviKQHM--PGFEKDFIFidylacrgkaskpllklleDNTYTYFDEEngtesIENYSQGK-YDIVLDF 293
Cdd:smart00829 129 AEV-FATAGSPEK--RDFLraLGIPDDHIF-------------------SSRDLSFADE-----ILRATGGRgVDVVLNS 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077   294 IGGyDILSQSQSLIHSGGHYVtTVGdyvadyKTDVfehWDNPSASARKMFGNIlwSY---NYTHYKFDPNGKTELIEKCA 370
Cdd:smart00829 182 LSG-EFLDASLRCLAPGGRFV-EIG------KRDI---RDNSQLAMAPFRPNV--SYhavDLDALEEGPDRIRELLAEVL 248

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 156849077   371 ELLGKRYVKCIVDNVYDWKDYKEAFNYMklQRAQ--GKLIL 409
Cdd:smart00829 249 ELFAEGVLRPLPVTVFPISDAEDAFRYM--QQGKhiGKVVL 287
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 97-414 1.68e-11

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 65.05  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  97 LGREYFGVISDIGSkleSDNRWKIGDEVMGIYyhPHIGYGSLQTSilvdpKQDPLVLKPENVTMPEAGGSLFCLASAFEI 176
Cdd:PTZ00354  62 LGLEVAGYVEDVGS---DVKRFKEGDRVMALL--PGGGYAEYAVA-----HKGHVMHIPQGYTFEEAAAIPEAFLTAWQL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 177 LEKLNSLKKltpNANILINGGTSSVGLFALQLLKNYYhivsKVTIVTSGTGPKV--IKQHmpgfeKDFIFIDYLACRGKA 254
Cdd:PTZ00354 132 LKKHGDVKK---GQSVLIHAGASGVGTAAAQLAEKYG----AATIITTSSEEKVdfCKKL-----AAIILIRYPDEEGFA 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 255 SKPLLKLLEDNTYTYFDEENGTESIENYSQGKYD---IVLDFIGG-----YDILsqsqSLIHSGGHYV-TTVGDYVADYK 325
Cdd:PTZ00354 200 PKVKKLTGEKGVNLVLDCVGGSYLSETAEVLAVDgkwIVYGFMGGakvekFNLL----PLLRKRASIIfSTLRSRSDEYK 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 326 TDVFEHWdnpsasarkmfgnilwsynythykfdpngKTELIekcaELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQG 405
Cdd:PTZ00354 276 ADLVASF-----------------------------EREVL----PYMEEGEIKPIVDRTYPLEEVAEAHTFLEQNKNIG 322


                 ....*....
gi 156849077 406 KLILKVEKF 414
Cdd:PTZ00354 323 KVVLTVNEP 331
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 38-411 5.22e-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: 63.39  E-value: 5.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTY-ENKIKTPiGSSKLVVDVRYVGLNPVDLMIKNG-YNQQGFYGEiGLGREYFGVISDIGSklESD 115
Cdd:cd08268    2 RAVRFHQFGGPEVLRIeELPVPAP-GAGEVLIRVEAIGLNRADAMFRRGaYIEPPPLPA-RLGYEAAGVVEAVGA--GVT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 116 NRWkIGDEVMGIYYHPHIGYGSLQTSILVdPKQDpLVLKPENVTMPEAGGSLFCLASAFEILEklnSLKKLTPNANILIN 195
Cdd:cd08268   78 GFA-VGDRVSVIPAADLGQYGTYAEYALV-PAAA-VVKLPDGLSFVEAAALWMQYLTAYGALV---ELAGLRPGDSVLIT 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 196 GGTSSVGLFALQLLKnyyhIVSKVTIVTSGTGPKvikqhmpgfeKDFifidylacrgkaskpLLKLLEDNTYTYfDEENG 275
Cdd:cd08268  152 AASSSVGLAAIQIAN----AAGATVIATTRTSEK----------RDA---------------LLALGAAHVIVT-DEEDL 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 276 TESIENYSQGK-YDIVLDFIGGydilSQSQSLIHSgGHYVTTVGDYVAdyktdvFEHWDNP---SASARKMFgnILWSYN 351
Cdd:cd08268  202 VAEVLRITGGKgVDVVFDPVGG----PQFAKLADA-LAPGGTLVVYGA------LSGEPTPfplKAALKKSL--TFRGYS 268

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 352 YTHYKFDPNGKTELIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILKV 411
Cdd:cd08268  269 LDEITLDPEARRRAIAFILDGLASGALKPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP 328
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 37-411 4.91e-10

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 60.63  E-value: 4.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  37 TKALVFQTKTGPVDFTYENKIKTPIGSSKLVVDVRYVGLNPVDLMIKNGynqqgfygEIGLGREyFGVI--SD------- 107
Cdd:cd08276    1 MKAWRLSGGGGLDNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNG--------RYPPPVK-DPLIplSDgagevva 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 108 IGSKLEsdnRWKIGDEVMGIyYHPHIGYGSLQTSILVDP---------------KQDPLVLKPENVTMPEAgGSLFCLA- 171
Cdd:cd08276   72 VGEGVT---RFKVGDRVVPT-FFPNWLDGPPTAEDEASAlggpidgvlaeyvvlPEEGLVRAPDHLSFEEA-ATLPCAGl 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 172 ---SAfeilekLNSLKKLTPNANILInGGTSSVGLFALQLLKnyyhIVSKVTIVTSGTGPKVIKqhmpgfekdfifidyl 248
Cdd:cd08276  147 tawNA------LFGLGPLKPGDTVLV-QGTGGVSLFALQFAK----AAGARVIATSSSDEKLER---------------- 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 249 acrgkaskpLLKLLEDNTYTYFDEENGTESIENYSQGK-YDIVLDfIGGYDILSQSQSLIHSGGHyVTTVGdYVADYKTD 327
Cdd:cd08276  200 ---------AKALGADHVINYRTTPDWGEEVLKLTGGRgVDHVVE-VGGPGTLAQSIKAVAPGGV-ISLIG-FLSGFEAP 267

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 328 VfehwdNPSASARK-------MFGNilwsynythykfdpngKTELIEKCAeLLGKRYVKCIVDNVYDWKDYKEAFNYMKL 400
Cdd:cd08276  268 V-----LLLPLLTKgatlrgiAVGS----------------RAQFEAMNR-AIEAHRIRPVIDRVFPFEEAKEAYRYLES 325

                        410
                 ....*....|.
gi 156849077 401 QRAQGKLILKV 411
Cdd:cd08276  326 GSHFGKVVIRV 336
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
285-409 1.11e-09

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 56.18  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  285 GKYDIVLDFIGGyDILSQSQSLIHSGGHYVTTVGDYVADyktdvfehwDNPSASARKMFGNILWSYNYTHykfdPNGKTE 364
Cdd:pfam13602  21 EGVDVVLDTVGG-EAFEASLRVLPGGGRLVTIGGPPLSA---------GLLLPARKRGGRGVKYLFLFVR----PNLGAD 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 156849077  365 LIEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLIL 409
Cdd:pfam13602  87 ILQELADLIEEGKLRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 38-210 1.78e-08

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: 55.58  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTYENKIKTPIGSSKLVVDVRYVGLNPVD-LMIkngynqQGFYGE-----IGLGREYFGVISDIGsk 111
Cdd:cd08241    2 KAVVCKELGGPEDLVLEEVPPEPGAPGEVRIRVEAAGVNFPDlLMI------QGKYQVkpplpFVPGSEVAGVVEAVG-- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 112 lESDNRWKIGDEVMGIyyhphIGYGSLQTSILVDPKQdpLVLKPENVTMPEAGGSLFCLASAFEILEKLNSLKkltPNAN 191
Cdd:cd08241   74 -EGVTGFKVGDRVVAL-----TGQGGFAEEVVVPAAA--VFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQ---PGET 142

                        170
                 ....*....|....*....
gi 156849077 192 ILINGGTSSVGLFALQLLK 210
Cdd:cd08241  143 VLVLGAAGGVGLAAVQLAK 161
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 60-208 4.09e-08

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: 54.36  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  60 PIGSSKLVVDVRYVGLNPVDLMIkngynQQGFYGEIGL-----GREYFGVISDIGSKLEsdnRWKIGDEVMGIyyhphIG 134
Cdd:cd08251    4 PPGPGEVRIQVRAFSLNFGDLLC-----VRGLYPTMPPypftpGFEASGVVRAVGPHVT---RLAVGDEVIAG-----TG 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156849077 135 --YGSLQTSILVDpkQDPLVLKPENVTMPEAGGSLFCLASAFEILEKLnslkKLTPNANILINGGTSSVGLFALQL 208
Cdd:cd08251   71 esMGGHATLVTVP--EDQVVRKPASLSFEEACALPVVFLTVIDAFARA----GLAKGEHILIQTATGGTGLMAVQL 140
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 37-235 3.02e-07

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: 51.84  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  37 TKALVFqTKTGPVD--FTYEN-KIKTPIGSSKLVVDVRYVGLNPVDLmikngyNQ-QGFYGE----------IGlGREYF 102
Cdd:cd08290    1 AKALVY-TEHGEPKevLQLESyEIPPPGPPNEVLVKMLAAPINPADI------NQiQGVYPIkppttpeppaVG-GNEGV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 103 GVISDIGSKLESdnrWKIGDEVMgiyyhPHI-GYGSLQTSILVDPKQdplVLK-PENVTMPEAGGSLFCLASAFEILEKL 180
Cdd:cd08290   73 GEVVKVGSGVKS---LKPGDWVI-----PLRpGLGTWRTHAVVPADD---LIKvPNDVDPEQAATLSVNPCTAYRLLEDF 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 156849077 181 NSLKkltPNANILINGGTSSVGLFALQLLKNYYhiVSKVTIVTSGTGPKVIKQHM 235
Cdd:cd08290  142 VKLQ---PGDWVIQNGANSAVGQAVIQLAKLLG--IKTINVVRDRPDLEELKERL 191
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 38-408 4.53e-07

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 51.07  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGPVDFTYENKIKTPIGSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIgLGREYFGVISDigsklESDNR 117
Cdd:cd08243    2 KAIVIEQPGGPEVLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRV-LGIEAVGEVEE-----APGGT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 118 WKIGDEV------MGIYYHphigyGSLQTSILVDPKQ----------DPLVLKPEnvTMPEAGGSLFclasafeilekln 181
Cdd:cd08243   76 FTPGQRVatamggMGRTFD-----GSYAEYTLVPNEQvyaidsdlswAELAALPE--TYYTAWGSLF------------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 182 SLKKLTPNANILINGGTSSVGLFALQLLKNYyhivskvtivtsgtGPKVIKqhmpgfekdfifidylACRGKASKPLLKL 261
Cdd:cd08243  136 RSLGLQPGDTLLIRGGTSSVGLAALKLAKAL--------------GATVTA----------------TTRSPERAALLKE 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 262 LE-DNTYTyfDEENGTESIENYSQGkYDIVLDFIGGyDILSQSQSLIHSGGhYVTTVGDYVADyktDVFEHWdNPsasar 340
Cdd:cd08243  186 LGaDEVVI--DDGAIAEQLRAAPGG-FDKVLELVGT-ATLKDSLRHLRPGG-IVCMTGLLGGQ---WTLEDF-NP----- 251

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156849077 341 kmFGNILWSYNYTHYKFDPNGKTEL-IEKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLI 408
Cdd:cd08243  252 --MDDIPSGVNLTLTGSSSGDVPQTpLQELFDFVAAGHLDIPPSKVFTFDEIVEAHAYMESNRAFGKVV 318
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 62-410 1.12e-05

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: 46.87  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  62 GSSKLVVDVRYVGLNPVDLMIKNG--YNQQgfYGEIGLGREYFGVISDIGSKLESdnrWKIGDEVMGIYYhphigYGSLQ 139
Cdd:cd08273   26 AAGEVVVKVEASGVSFADVQMRRGlyPDQP--PLPFTPGYDLVGRVDALGSGVTG---FEVGDRVAALTR-----VGGNA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 140 TSILVDPKQdpLVLKPENVTMPEAggslFCLAS----AFEILEKLnslKKLTPNANILINGGTSSVGLFALQLLKnyyhi 215
Cdd:cd08273   96 EYINLDAKY--LVPVPEGVDAAEA----VCLVLnyvtAYQMLHRA---AKVLTGQRVLIHGASGGVGQALLELAL----- 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 216 VSKVTIVtsGTGPKviKQHMpgfekdfifidylACRGKASKPLlkllednTYTYFD--EENGTesienysQGKYDIVLDF 293
Cdd:cd08273  162 LAGAEVY--GTASE--RNHA-------------ALRELGATPI-------DYRTKDwlPAMLT-------PGGVDVVFDG 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 294 IGGyDILSQSQSLIHSGGHYVTTVGDyvADYKTDVFEHWDNPSASARKMFGNILWSYNYTHY-------KFDPNGKTELI 366
Cdd:cd08273  211 VGG-ESYEESYAALAPGGTLVCYGGN--SSLLQGRRSLAALGSLLARLAKLKLLPTGRRATFyyvwrdrAEDPKLFRQDL 287

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 156849077 367 EKCAELLGKRYVKCIVDNVYDWKDYKEAFNYMKLQRAQGKLILK 410
Cdd:cd08273  288 TELLDLLAKGKIRPKIAKRLPLSEVAEAHRLLESGKVVGKIVLL 331
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 62-225 4.46e-05

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 45.03  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  62 GSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIgLGREYFGVISDIGSKLEsdnRWKIGDEVMGIYYHP---------- 131
Cdd:PRK13771  24 GKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVI-LGHEVVGTVEEVGENVK---GFKPGDRVASLLYAPdgtceycrsg 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 132 -------HIGY-----GSLQTSILVDPKQdpLVLKPENVtmPEAGGSLF-CLASA-FEILEKLNslkkLTPNANILINGG 197
Cdd:PRK13771 100 eeaycknRLGYgeeldGFFAEYAKVKVTS--LVKVPPNV--SDEGAVIVpCVTGMvYRGLRRAG----VKKGETVLVTGA 171

                        170       180
                 ....*....|....*....|....*...
gi 156849077 198 TSSVGLFALQLLKNYYhivSKVTIVTSG 225
Cdd:PRK13771 172 GGGVGIHAIQVAKALG---AKVIAVTSS 196
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 66-231 7.57e-05

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: 44.44  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  66 LVVDVRYVGLNPVDLMIKNGYNQQGFYGEIgLGREYFGVISDIGSKLEsdnRWKIGDEVmgiYY-----HPhigyGS--- 137
Cdd:cd08252   33 LLVRVEAVSVNPVDTKVRAGGAPVPGQPKI-LGWDASGVVEAVGSEVT---LFKVGDEV---YYagditRP----GSnae 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 138 LQtsiLVDPKqdpLV-LKPENVTMPEAGG----SLfclaSAFEILEKLNSLKKLTPNAN--ILINGGTSSVGLFALQLLK 210
Cdd:cd08252  102 YQ---LVDER---IVgHKPKSLSFAEAAAlpltSL----TAWEALFDRLGISEDAENEGktLLIIGGAGGVGSIAIQLAK 171

                        170       180
                 ....*....|....*....|.
gi 156849077 211 NYyhivskvtivtsgTGPKVI 231
Cdd:cd08252  172 QL-------------TGLTVI 179
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 38-208 1.71e-04

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: 43.34  E-value: 1.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFqTKTGPVDFTYENKIKTP-IGSSKLVVDVRYVGLNPVDLMIKNG-YNQQGFYGEIGlGREYFGVISDIGsklESD 115
Cdd:cd08253    2 RAIRY-HEFGAPDVLRLGDLPVPtPGPGEVLVRVHASGVNPVDTYIRAGaYPGLPPLPYVP-GSDGAGVVEAVG---EGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 116 NRWKIGDEV---MGIYYHPHigyGSLQTSILVDpkQDPLVLKPENVTmPEAGGslfCLAS-AFEILEKLNSLKKLTPNAN 191
Cdd:cd08253   77 DGLKVGDRVwltNLGWGRRQ---GTAAEYVVVP--ADQLVPLPDGVS-FEQGA---ALGIpALTAYRALFHRAGAKAGET 147

                        170
                 ....*....|....*..
gi 156849077 192 ILINGGTSSVGLFALQL 208
Cdd:cd08253  148 VLVHGGSGAVGHAAVQL 164
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 38-210 3.33e-04

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


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 42.30  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVfQTKTGPVDFTYENKIKTPIGSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIgLGREYFGVISDIGSKLEsdnR 117
Cdd:cd08258    2 KALV-KTGPGPGNVELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVV-LGHEFSGTIVEVGPDVE---G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 118 WKIGDEVM----------------GIYYH-PH---IGY---GSLQTSILVDPKQdpLVLKPENVTMPEAGGSLFCLASAF 174
Cdd:cd08258   77 WKVGDRVVsettfstcgrcpycrrGDYNLcPHrkgIGTqadGGFAEYVLVPEES--LHELPENLSLEAAALTEPLAVAVH 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 156849077 175 EILEKlnslKKLTPNANILINgGTSSVGLFALQLLK 210
Cdd:cd08258  155 AVAER----SGIRPGDTVVVF-GPGPIGLLAAQVAK 185
PRK10754 PRK10754
NADPH:quinone reductase;
38-210 8.37e-04

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 41.26  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQTKTGP-----VDFTyenkiKTPIGSSKLVVDVRYVGLNPVDLMIKNG-YNQQGFYGeiGLGREYFGVISDIGSK 111
Cdd:PRK10754   3 KRIEFHKHGGPevlqaVEFT-----PADPAENEVQVENKAIGINYIDTYIRSGlYPPPSLPS--GLGTEAAGVVSKVGSG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 112 LESdnrWKIGDEVmgIYYHPHIG-YGSLQtsilvDPKQDPLVLKPENVTMPEAGGSLFCLASAFEILEKLNSLKkltPNA 190
Cdd:PRK10754  76 VKH---IKVGDRV--VYAQSALGaYSSVH-----NVPADKAAILPDAISFEQAAASFLKGLTVYYLLRKTYEIK---PDE 142

                        170       180
                 ....*....|....*....|
gi 156849077 191 NILINGGTSSVGLFALQLLK 210
Cdd:PRK10754 143 QFLFHAAAGGVGLIACQWAK 162
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 38-210 2.34e-03

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 39.64  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  38 KALVFQtKTGpVDFTYENKIKTP-IGSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEigLGREYFGVISDIGSKLESdn 116
Cdd:cd08264    2 KALVFE-KSG-IENLKVEDVKDPkPGPGEVLIRVKMAGVNPVDYNVINAVKVKPMPHI--PGAEFAGVVEEVGDHVKG-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077 117 rWKIGDEV---------------------------MGIyyhphIGYGSLQTSILVDPKQdpLVLKPENVTMpEAGGSLFC 169
Cdd:cd08264   76 -VKKGDRVvvynrvfdgtcdmclsgnemlcrnggiIGV-----VSNGGYAEYIVVPEKN--LFKIPDSISD-ELAASLPV 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 156849077 170 LAsafeiLEKLNSLK--KLTPNANILINGGTSSVGLFALQLLK 210
Cdd:cd08264  147 AA-----LTAYHALKtaGLGPGETVVVFGASGNTGIFAVQLAK 184
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 62-212 2.69e-03

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: 39.55  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156849077  62 GSSKLVVDVRYVGLNPVDLMIKNGYNQQGFYGEIGLGREYFGVISDIGsklESDNRWKIGDEVMGIYYHPHIGYGSLQTS 141
Cdd:cd08250   29 GPGEVLVKNRFVGINASDINFTAGRYDPGVKPPFDCGFEGVGEVVAVG---EGVTDFKVGDAVATMSFGAFAEYQVVPAR 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156849077 142 ILVdpkqdPL-VLKPENVTMPEAGgslfclASAFEILEKLNSLKKltpNANILIN---GGTssvGLFALQLLKNY 212
Cdd:cd08250  106 HAV-----PVpELKPEVLPLLVSG------LTASIALEEVGEMKS---GETVLVTaaaGGT---GQFAVQLAKLA 163
 
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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