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Conserved domains on  [gi|493029422|ref|WP_006099071|]
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NAD(P)-dependent alcohol dehydrogenase [Coleofasciculus chthonoplastes]

Protein Classification

NAD(P)-dependent alcohol dehydrogenase( domain architecture ID 10143012)

NAD(P)-dependent alcohol dehydrogenase catalyzes the reversible conversion of an alcohol to its corresponding aldehyde

CATH:  3.40.50.720|3.90.180.10
EC:  1.1.-.-
Gene Ontology:  GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 3-332 2.28e-166

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


:

Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 466.59  E-value: 2.28e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd05283    1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VGLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSR-------HGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:cd05283   81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKypdgtitQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITVYS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQFDIKPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNSFDFILATA 235
Cdd:cd05283  161 PLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAMKKAAGSLDLIIDTV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 236 NADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNE 315
Cdd:cd05283  241 SASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGINE 320

                        330
                 ....*....|....*..
gi 493029422 316 AMEKLRHGKPRYRLVLK 332
Cdd:cd05283  321 ALERLEKGDVRYRFVLD 337
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 3-332 2.28e-166

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


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 466.59  E-value: 2.28e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd05283    1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VGLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSR-------HGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:cd05283   81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKypdgtitQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITVYS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQFDIKPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNSFDFILATA 235
Cdd:cd05283  161 PLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAMKKAAGSLDLIIDTV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 236 NADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNE 315
Cdd:cd05283  241 SASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGINE 320

                        330
                 ....*....|....*..
gi 493029422 316 AMEKLRHGKPRYRLVLK 332
Cdd:cd05283  321 ALERLEKGDVRYRFVLD 337
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 2-332 9.64e-145

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 411.43  E-value: 9.64e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   2 IKAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQ 81
Cdd:COG1064    1 MKAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  82 RVGLGWFSgSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFD 161
Cdd:COG1064   81 RVGVGWVD-SCGTCEYCRSGRENLCENGRFTGYTTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRRAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 162 IKPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQN--SFDFILATANADL 239
Cdd:COG1064  160 VGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNSSDEDPVEAVREltGADVVIDTVGAPA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 240 DWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNEAMEK 319
Cdd:COG1064  240 TVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIPLEEANEALER 319

                        330
                 ....*....|...
gi 493029422 320 LRHGKPRYRLVLK 332
Cdd:COG1064  320 LRAGKVRGRAVLD 332
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 5-331 4.70e-77

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 240.17  E-value: 4.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   5 YAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVG 84
Cdd:PLN02586  16 WAARDPSGVLSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  85 LGWFSGSCMTCEWCMSGNHNLC---------SNAEGTivSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:PLN02586  96 VGVIVGSCKSCESCDQDLENYCpkmiftynsIGHDGT--KNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQFDI-KPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEA-RELGATHFINSGDVNALESVQNSFDFILA 233
Cdd:PLN02586 174 PMKYYGMtEPGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAiNRLGADSFLVSTDPEKMKAAIGTMDYIID 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 234 TANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQV 313
Cdd:PLN02586 254 TVSAVHALGPLLGLLKVNGKLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRMDEI 333

                        330
                 ....*....|....*...
gi 493029422 314 NEAMEKLRHGKPRYRLVL 331
Cdd:PLN02586 334 NTAMERLAKSDVRYRFVI 351
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 28-133 3.47e-37

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


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 128.88  E-value: 3.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   28 EVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSgSCMTCEWCMSGNHNLCS 107
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNLCP 80

                          90       100
                  ....*....|....*....|....*.
gi 493029422  108 NAEGTIVSRHGGFADKVRADYSWVVP 133
Cdd:pfam08240  81 NGRFLGYDRDGGFAEYVVVPERNLVP 106
Rxyl_3153 TIGR03989
NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within ...
 3-324 2.68e-23

NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within the family pfam00107 of zinc-binding dehydrogenases. The family pfam00107 contains class III alcohol dehydrogenases, including enzymes designated S-(hydroxymethyl)glutathione dehydrogenase and NAD/mycothiol-dependent formaldehyde dehydrogenase. Members of the current family occur only in species that contain the very small protein mycofactocin (TIGR03969), a possible cofactor precursor, and radical SAM protein TIGR03962. We name this family for Rxyl_3153, where the lone member of the family co-clusters with these markers in Rubrobacter xylanophilus. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274905 [Multi-domain]  Cd Length: 369  Bit Score: 98.93  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422    3 KAYAAHEPGgqlQPFEYDPGTLGDE---EVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:TIGR03989   3 KAAVLWGPG---QPWEVEEIELDDPkagEVLVKLVASGLCHSDEHLVTGDLPMPRYPILGGHEGAGVVTKVGPGVTGVKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   80 GQRVGLGwFSGSCMTCEWCMSGNHNLCSN----------AEGTIVSRHGG-----------FADKVRADYSWVVPLPDGI 138
Cdd:TIGR03989  80 GDHVVLS-FIPACGRCRYCSTGLQNLCDLgaalltgsqiSDGTYRFHADGqdvgqmcllgtFSEYTVVPEASVVKIDDDI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  139 NPATAGPLFCGGITVFNPIVQF-DIKPSDrvgVIGIGGLGHIALGFLQ----AWGCEITAFSSSPDKEAEARELGATHFI 213
Cdd:TIGR03989 159 PLDKACLVGCGVPTGWGSAVNIaDVRPGD---TVVVMGIGGVGINAVQgaavAGARKVIAVDPVEFKREQALKFGATHAF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  214 NSGD-----VNALESVQNSFDFILATANADLDWNA-YIAALRPKGRLHFVGVIP---NPLSTPIFPLILGQKSISASPVG 284
Cdd:TIGR03989 236 ASMEeavqlVRELTNGQGADKTIITVGEVDGEHIAeALSATRKGGRVVVTGLGPmadVDVKVNLFELTLLQKELQGTLFG 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 493029422  285 SPATISQMINFAA--RQGV----EPITETFSFEQVNEAMEKLRHGK 324
Cdd:TIGR03989 316 GANPRADIPRLLElyRAGKlkldELITRTYTLDQINEGYQDMLDGK 361
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 31-217 1.08e-06

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 49.31  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422    31 IKVEYCGICHSD--LSMldnewGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVgLGWFSGScmtcewcmsgnhnlcsn 108
Cdd:smart00829   1 IEVRAAGLNFRDvlIAL-----GLYPGEAVLGGECAGVVTRVGPGVTGLAVGDRV-MGLAPGA----------------- 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   109 aegtivsrhggFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF-DIKPSDRvgvigigglghI-------- 179
Cdd:smart00829  58 -----------FATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLaRLRPGES-----------Vlihaaagg 115

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 493029422   180 ----ALGFLQAWGCEITAFSSSPDKEAEARELG--ATHFINSGD 217
Cdd:smart00829 116 vgqaAIQLARHLGAEVFATAGSPEKRDFLRALGipDDHIFSSRD 159
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 3-332 2.28e-166

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


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 466.59  E-value: 2.28e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd05283    1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VGLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSR-------HGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:cd05283   81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKypdgtitQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITVYS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQFDIKPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNSFDFILATA 235
Cdd:cd05283  161 PLKRNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAMKKAAGSLDLIIDTV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 236 NADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNE 315
Cdd:cd05283  241 SASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGINE 320

                        330
                 ....*....|....*..
gi 493029422 316 AMEKLRHGKPRYRLVLK 332
Cdd:cd05283  321 ALERLEKGDVRYRFVLD 337
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 2-332 9.64e-145

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 411.43  E-value: 9.64e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   2 IKAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQ 81
Cdd:COG1064    1 MKAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  82 RVGLGWFSgSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFD 161
Cdd:COG1064   81 RVGVGWVD-SCGTCEYCRSGRENLCENGRFTGYTTDGGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRALRRAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 162 IKPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQN--SFDFILATANADL 239
Cdd:COG1064  160 VGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNSSDEDPVEAVREltGADVVIDTVGAPA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 240 DWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNEAMEK 319
Cdd:COG1064  240 TVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIPLEEANEALER 319

                        330
                 ....*....|...
gi 493029422 320 LRHGKPRYRLVLK 332
Cdd:COG1064  320 LRAGKVRGRAVLD 332
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 3-331 7.09e-108

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


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 317.73  E-value: 7.09e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd08245    1 KAAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VGLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDI 162
Cdd:cd08245   81 VGVGWLVGSCGRCEYCRRGLENLCQKAVNTGYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSALRDAGP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 163 KPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNSFDFILATANADLDWN 242
Cdd:cd08245  161 RPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQAAAGGADVILVTVVSGAAAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 243 AYIAALRPKGRLHFVGVIPNPLSTP-IFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNEAMEKLR 321
Cdd:cd08245  241 AALGGLRRGGRIVLVGLPESPPFSPdIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIETFPLDQANEAYERME 320

                        330
                 ....*....|
gi 493029422 322 HGKPRYRLVL 331
Cdd:cd08245  321 KGDVRFRFVL 330
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 3-332 1.88e-94

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


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 283.75  E-value: 1.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd08296    2 KAVQVTEPGGPLELVERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VGLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDI 162
Cdd:cd08296   82 VGVGWHGGHCGTCDACRRGDFVHCENGKVTGVTRDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNALRNSGA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 163 KPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQN--SFDFILATA-NADl 239
Cdd:cd08296  162 KPGDLVAVQGIGGLGHLAVQYAAKMGFRTVAISRGSDKADLARKLGAHHYIDTSKEDVAEALQElgGAKLILATApNAK- 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 240 DWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNEAMEK 319
Cdd:cd08296  241 AISALVGGLAPRGKLLILGAAGEPVAVSPLQLIMGRKSIHGWPSGTALDSEDTLKFSALHGVRPMVETFPLEKANEAYDR 320

                        330
                 ....*....|...
gi 493029422 320 LRHGKPRYRLVLK 332
Cdd:cd08296  321 MMSGKARFRVVLT 333
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 25-332 8.23e-79

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


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 243.98  E-value: 8.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  25 GDEEVEIKVEYCGICHSDLSMLDNEWGM-TDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSGSCMTCEWCMSGNH 103
Cdd:cd08297   25 GPGEVLVKLEASGVCHTDLHAALGDWPVkPKLPLIGGHEGAGVVVAVGPGVSGLKVGDRVGVKWLYDACGKCEYCRTGDE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 104 NLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVI-GIGGLGHIALG 182
Cdd:cd08297  105 TLCPNQKNSGYTVDGTFAEYAIADARYVTPIPDGLSFEQAAPLLCAGVTVYKALKKAGLKPGDWVVISgAGGGLGHLGVQ 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 183 FLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNSFD-------FILATANAdldwnAYIAA---LRPKG 252
Cdd:cd08297  185 YAKAMGLRVIAIDVGDEKLELAKELGADAFVDFKKSDDVEAVKELTGgggahavVVTAVSAA-----AYEQAldyLRPGG 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 253 RLHFVGVIPN-PLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNEAMEKLRHGKPRYRLVL 331
Cdd:cd08297  260 TLVCVGLPPGgFIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVKPHIQVVPLEDLNEVFEKMEEGKIAGRVVV 339


                 .
gi 493029422 332 K 332
Cdd:cd08297  340 D 340
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 5-331 4.70e-77

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 240.17  E-value: 4.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   5 YAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVG 84
Cdd:PLN02586  16 WAARDPSGVLSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  85 LGWFSGSCMTCEWCMSGNHNLC---------SNAEGTivSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:PLN02586  96 VGVIVGSCKSCESCDQDLENYCpkmiftynsIGHDGT--KNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQFDI-KPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEA-RELGATHFINSGDVNALESVQNSFDFILA 233
Cdd:PLN02586 174 PMKYYGMtEPGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAiNRLGADSFLVSTDPEKMKAAIGTMDYIID 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 234 TANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQV 313
Cdd:PLN02586 254 TVSAVHALGPLLGLLKVNGKLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRMDEI 333

                        330
                 ....*....|....*...
gi 493029422 314 NEAMEKLRHGKPRYRLVL 331
Cdd:PLN02586 334 NTAMERLAKSDVRYRFVI 351
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 5-331 1.18e-75

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 236.62  E-value: 1.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   5 YAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVG 84
Cdd:PLN02514  13 WAARDPSGHLSPYTYTLRKTGPEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  85 LGWFSGSCMTCEWCMSGNHNLCSN---------AEGTIVsrHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:PLN02514  93 VGVIVGCCGECSPCKSDLEQYCNKriwsyndvyTDGKPT--QGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYS 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQFDIKPSD-RVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARE-LGATHFINSGDVNALESVQNSFDFILA 233
Cdd:PLN02514 171 PLSHFGLKQSGlRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEhLGADDYLVSSDAAEMQEAADSLDYIID 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 234 TANADLDWNAYIAALRPKGRLHFVGVIPNPLS--TPIfpLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFE 311
Cdd:PLN02514 251 TVPVFHPLEPYLSLLKLDGKLILMGVINTPLQfvTPM--LMLGRKVITGSFIGSMKETEEMLEFCKEKGLTSMIEVVKMD 328

                        330       340
                 ....*....|....*....|
gi 493029422 312 QVNEAMEKLRHGKPRYRLVL 331
Cdd:PLN02514 329 YVNTAFERLEKNDVRYRFVV 348
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 3-331 2.51e-67

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


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 214.35  E-value: 2.51e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPG----GQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLN 78
Cdd:cd08298    2 KAMVLEKPGpieeNPLRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTRFS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  79 LGQRVGLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIV 158
Cdd:cd08298   82 VGDRVGVPWLGSTCGECRYCRSGRENLCDNARFTGYTVDGGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRALK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 159 QFDIKPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGAtHFINSGDVNALESVQNSFDFilatANAD 238
Cdd:cd08298  162 LAGLKPGQRLGLYGFGASAHLALQIARYQGAEVFAFTRSGEHQELARELGA-DWAGDSDDLPPEPLDAAIIF----APVG 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 239 LDWNAYIAALRPKGRLhFVGVIPNplsTPI----FPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVN 314
Cdd:cd08298  237 ALVPAALRAVKKGGRV-VLAGIHM---SDIpafdYELLWGEKTIRSVANLTRQDGEEFLKLAAEIPIKPEVETYPLEEAN 312

                        330
                 ....*....|....*..
gi 493029422 315 EAMEKLRHGKPRYRLVL 331
Cdd:cd08298  313 EALQDLKEGRIRGAAVL 329
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 4-331 3.45e-65

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 210.27  E-value: 3.45e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   4 AYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRV 83
Cdd:PLN02178   9 GWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  84 GLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSR-------HGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNP 156
Cdd:PLN02178  89 GVGVIIGSCQSCESCNQDLENYCPKVVFTYNSRssdgtrnQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSP 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 157 IVQFDI--KPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARE-LGATHFINSGDVNALESVQNSFDFILA 233
Cdd:PLN02178 169 MKYYGMtkESGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDrLGADSFLVTTDSQKMKEAVGTMDFIID 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 234 TANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQV 313
Cdd:PLN02178 249 TVSAEHALLPLFSLLKVSGKLVALGLPEKPLDLPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSDI 328

                        330
                 ....*....|....*...
gi 493029422 314 NEAMEKLRHGKPRYRLVL 331
Cdd:PLN02178 329 NSAMDRLAKSDVRYRFVI 346
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 3-331 2.79e-59

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


Pssm-ID: 176187 [Multi-domain]  Cd Length: 340  Bit Score: 193.93  E-value: 2.79e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWG---MTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:cd05284    2 KAARLYEYGKPLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGgilPYKLPFTLGHENAGWVEEVGSGVDGLKE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRVGL-GWFSgsCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIV 158
Cdd:cd05284   82 GDPVVVhPPWG--CGTCRYCRRGEENYCENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 159 QF--DIKPSDRVGVIGIGGLGHIALGFLQAW-GCEITAFSSSPDKEAEARELGATHFINSGDvNALESVQNS-------- 227
Cdd:cd05284  160 KAlpYLDPGSTVVVIGVGGLGHIAVQILRALtPATVIAVDRSEEALKLAERLGADHVLNASD-DVVEEVRELtggrgada 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 228 -FDFILATANADLdwnaYIAALRPKGRLHFVGVIPNpLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITE 306
Cdd:cd05284  239 vIDFVGSDETLAL----AAKLLAKGGRYVIVGYGGH-GRLPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVKVEIT 313

                        330       340
                 ....*....|....*....|....*
gi 493029422 307 TFSFEQVNEAMEKLRHGKPRYRLVL 331
Cdd:cd05284  314 KFPLEDANEALDRLREGRVTGRAVL 338
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 3-326 5.08e-59

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


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 193.05  E-value: 5.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG-QLQpfEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQ 81
Cdd:COG1063    2 KALVLHGPGDlRLE--EVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  82 RVgLGWFSGSCMTCEWCMSGNHNLCSNAEGT-IVSRHGGFADKVRADYSWVVPLPDGINPATAG---PLFCGgitvFNPI 157
Cdd:COG1063   80 RV-VVEPNIPCGECRYCRRGRYNLCENLQFLgIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAAlvePLAVA----LHAV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 158 VQFDIKPSDRvgvigigglghI-----------ALGFLQAWGC-EITAFSSSPDKEAEARELGATHFINSGDVNALESVQ 225
Cdd:COG1063  155 ERAGVKPGDT-----------VlvigagpigllAALAARLAGAaRVIVVDRNPERLELARELGADAVVNPREEDLVEAVR 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 226 -----NSFDFIL-ATANADLdWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQ 299
Cdd:COG1063  224 eltggRGADVVIeAVGAPAA-LEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASG 302

                        330       340       350
                 ....*....|....*....|....*....|
gi 493029422 300 GVEP---ITETFSFEQVNEAMEKLRHGKPR 326
Cdd:COG1063  303 RIDLeplITHRFPLDDAPEAFEAAADRADG 332
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 2-333 1.86e-51

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


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 173.59  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   2 IKAYAAHEPGGQLQPFEYDP-GTLGDEEVEIKVEYCGICHSDLSMLDNE-WGMTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:cd08254    1 MKAWRFHKGSKGLLVLEEVPvPEPGPGEVLVKVKAAGVCHSDLHILDGGvPTLTKLPLTLGHEIAGTVVEVGAGVTNFKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRVGLgWFSGSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQ 159
Cdd:cd08254   81 GDRVAV-PAVIPCGACALCRRGRGNLCLNQGMPGLGIDGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 160 FD-IKPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNS--------FDF 230
Cdd:cd08254  160 AGeVKPGETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAGlgggfdviFDF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 231 ILATANADLDWNayiaALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSF 310
Cdd:cd08254  240 VGTQPTFEDAQK----AVKPGGRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVETRPL 315

                        330       340
                 ....*....|....*....|...
gi 493029422 311 EQVNEAMEKLRHGKPRYRLVLKH 333
Cdd:cd08254  316 DEIPEVLERLHKGKVKGRVVLVP 338
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 3-333 5.73e-50

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


Pssm-ID: 176202 [Multi-domain]  Cd Length: 350  Bit Score: 169.72  E-value: 5.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYD-PGTLGDEeVEIKVEYCGICHSDLSMLDNEWGMTD------------YPFVPGHEVVGTIAA 69
Cdd:cd08240    2 KAAAVVEPGKPLEEVEIDtPKPPGTE-VLVKVTACGVCHSDLHIWDGGYDLGGgktmslddrgvkLPLVLGHEIVGEVVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  70 LGDKVTTLNLGQRVGLGWFSGsCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCG 149
Cdd:cd08240   81 VGPDAADVKVGDKVLVYPWIG-CGECPVCLAGDENLCAKGRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 150 GITVFNPIVQFDIKPSDRvgvigigglgHI-----------ALGFLQAWG-CEITAFSSSPDKEAEARELGATHFINSGD 217
Cdd:cd08240  160 GLTAYSAVKKLMPLVADE----------PVviigagglglmALALLKALGpANIIVVDIDEAKLEAAKAAGADVVVNGSD 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 218 VNALESVQ----NSFDFILATANADLDWNAYIAALRPKGRLHFVGVIPN--PLSTPIFPliLGQKSISASPVGSPATISQ 291
Cdd:cd08240  230 PDAAKRIIkaagGGVDAVIDFVNNSATASLAFDILAKGGKLVLVGLFGGeaTLPLPLLP--LRALTIQGSYVGSLEELRE 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 493029422 292 MINFAARQGVEPI-TETFSFEQVNEAMEKLRHGKPRYRLVLKH 333
Cdd:cd08240  308 LVALAKAGKLKPIpLTERPLSDVNDALDDLKAGKVVGRAVLKP 350
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 3-332 1.12e-49

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


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 168.65  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd08259    2 KAAILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPGDR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VGLGWFSGsCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDI 162
Cdd:cd08259   82 VILYYYIP-CGKCEYCLSGEENLCRNRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAVHALKRAGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 163 KPSDRVGVIGIGGLGHI-ALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNalESVQN--SFDFILATANADl 239
Cdd:cd08259  161 KKGDTVLVTGAGGGVGIhAIQLAKALGARVIAVTRSPEKLKILKELGADYVIDGSKFS--EDVKKlgGADVVIELVGSP- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 240 DWNAYIAALRPKGRLHFVG-VIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEP-ITETFSFEQVNEAM 317
Cdd:cd08259  238 TIEESLRSLNKGGRLVLIGnVTPDPAPLRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKPvIDRVVSLEDINEAL 317

                        330
                 ....*....|....*
gi 493029422 318 EKLRHGKPRYRLVLK 332
Cdd:cd08259  318 EDLKSGKVVGRIVLK 332
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
15-324 8.06e-49

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 166.80  E-value: 8.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  15 QPFEYDPGTL---GDEEVEIKVEYCGICHSDLSMLDNEWGMTdYPFVPGHEVVGTIAALGDKVTTLNLGQRVgLGWFSGS 91
Cdd:COG1062    2 GPLEIEEVELdepRPGEVLVRIVAAGLCHSDLHVRDGDLPVP-LPAVLGHEGAGVVEEVGPGVTGVAPGDHV-VLSFIPS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  92 CMTCEWCMSGNHNLC-------------------SNAEGTIVSRH---GGFADKVRADYSWVVPLPDGINPATAGPLFCG 149
Cdd:COG1062   80 CGHCRYCASGRPALCeagaalngkgtlpdgtsrlSSADGEPVGHFfgqSSFAEYAVVPERSVVKVDKDVPLELAALLGCG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 150 GIT----VFNpivQFDIKPSDRvgvigigglghIA--------LGFLQA---WGC-EITAFSSSPDKEAEARELGATHFI 213
Cdd:COG1062  160 VQTgagaVLN---TAKVRPGDT-----------VAvfglggvgLSAVQGariAGAsRIIAVDPVPEKLELARELGATHTV 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 214 NSGDVNALESVQ----NSFDF-ILATANADLdWNAYIAALRPKGRLHFVGVIP--NPLSTPIFPLILGQKSISASPVGS- 285
Cdd:COG1062  226 NPADEDAVEAVReltgGGVDYaFETTGNPAV-IRQALEALRKGGTVVVVGLAPpgAEISLDPFQLLLTGRTIRGSYFGGa 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 493029422 286 -PAT-ISQMINFaARQG---VEP-ITETFSFEQVNEAMEKLRHGK 324
Cdd:COG1062  305 vPRRdIPRLVDL-YRAGrlpLDElITRRYPLDEINEAFDDLRSGE 348
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 2-324 5.03e-48

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 165.02  E-value: 5.03e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   2 IKAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGmTDYPFVPGHEVVGTIAALGDKVTTLNLGQ 81
Cdd:cd08279    1 MRAAVLHEVGKPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLP-APLPAVLGHEGAGVVEEVGPGVTGVKPGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  82 RVGLGWfSGSCMTCEWCMSGNHNLCSNAEGTIV-------SRH-------------GGFADKVRADYSWVVPLPDGINPA 141
Cdd:cd08279   80 HVVLSW-IPACGTCRYCSRGQPNLCDLGAGILGgqlpdgtRRFtadgepvgamcglGTFAEYTVVPEASVVKIDDDIPLD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 142 TAGPLFCGGIT----VFNpivQFDIKPSDRvgvigigglghIA--------LGFLQawGC------EITAFSSSPDKEAE 203
Cdd:cd08279  159 RAALLGCGVTTgvgaVVN---TARVRPGDT-----------VAvigcggvgLNAIQ--GAriagasRIIAVDPVPEKLEL 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 204 ARELGATHFINSGDVNALESVQN-----SFDF-ILATANADLdWNAYIAALRPKGRLHFVGVIP--NPLSTPIFPLILGQ 275
Cdd:cd08279  223 ARRFGATHTVNASEDDAVEAVRDltdgrGADYaFEAVGRAAT-IRQALAMTRKGGTAVVVGMGPpgETVSLPALELFLSE 301

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493029422 276 KSISASPVGS---PATISQMINFaARQGV----EPITETFSFEQVNEAMEKLRHGK 324
Cdd:cd08279  302 KRLQGSLYGSanpRRDIPRLLDL-YRAGRlkldELVTRRYSLDEINEAFADMLAGE 356
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 18-332 1.26e-47

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 163.28  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  18 EYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGmtDYP-FVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSGSCMTCE 96
Cdd:PRK09422  17 EKTLRPLKHGEALVKMEYCGVCHTDLHVANGDFG--DKTgRILGHEGIGIVKEVGPGVTSLKVGDRVSIAWFFEGCGHCE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  97 WCMSGNHNLCSNAEGTIVSRHGGFADK--VRADYSwvVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVIGIG 174
Cdd:PRK09422  95 YCTTGRETLCRSVKNAGYTVDGGMAEQciVTADYA--VKVPEGLDPAQASSITCAGVTTYKAIKVSGIKPGQWIAIYGAG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 175 GLGHIALGFLQ-AWGCEITAFSSSPDKEAEARELGATHFINSGDV-NALESVQNSF---DFILATANADLDWNAYIAALR 249
Cdd:PRK09422 173 GLGNLALQYAKnVFNAKVIAVDINDDKLALAKEVGADLTINSKRVeDVAKIIQEKTggaHAAVVTAVAKAAFNQAVDAVR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 250 PKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITETFSFEQVNEAMEKLRHGKPRYRL 329
Cdd:PRK09422 253 AGGRVVAVGLPPESMDLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQLRPLEDINDIFDEMEQGKIQGRM 332


                 ...
gi 493029422 330 VLK 332
Cdd:PRK09422 333 VID 335
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-295 6.72e-47

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: 159.79  E-value: 6.72e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWGMTD-YPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSGsCMTCEWCMSGNHNLC 106
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGYPPPPkLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLG-CGTCELCRELCPGGG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 107 SNAEGtivsRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF-DIKPSDRvgvigigglghIA-LG-- 182
Cdd:cd05188   80 ILGEG----LDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAgVLKPGDT-----------VLvLGag 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 183 --------FLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNS----FDFILATANADLDWNAYIAALRP 250
Cdd:cd05188  145 gvgllaaqLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTggggADVVIDAVGGPETLAQALRLLRP 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 493029422 251 KGRLHFVGVIPNPLSTPIFPLILG-QKSISASPVGSPATISQMINF 295
Cdd:cd05188  225 GGRIVVVGGTSGGPPLDDLRRLLFkELTIIGSTGGTREDFEEALDL 270
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 3-332 7.23e-45

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: 155.69  E-value: 7.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMT-DYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:COG0604    2 KAIVITEFGGpeVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPpGLPFIPGSDAAGVVVAVGEGVTGFKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRV-GLGwfsgscmtcewcmsgnhnlcsnaegtivsRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIV 158
Cdd:COG0604   82 GDRVaGLG-----------------------------RGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLTAWQALF 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 159 QF-DIKPSDRvgvig-igglgHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQ-----NSFDFI 231
Cdd:COG0604  133 DRgRLKPGETvlvhgaaggvgSAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREEDFAERVRaltggRGVDVV 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 232 LATANADLdWNAYIAALRPKGRLHFVGVIPNP-LSTPIFPLILGQKSISASPVGSP------ATISQMINFAARQGVEP- 303
Cdd:COG0604  213 LDTVGGDT-LARSLRALAPGGRLVSIGAASGApPPLDLAPLLLKGLTLTGFTLFARdpaerrAALAELARLLAAGKLRPv 291

                        330       340
                 ....*....|....*....|....*....
gi 493029422 304 ITETFSFEQVNEAMEKLRHGKPRYRLVLK 332
Cdd:COG0604  292 IDRVFPLEEAAEAHRLLESGKHRGKVVLT 320
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 18-324 1.03e-37

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


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 137.27  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  18 EYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTdYPFVPGHEVVGTIAALGDKVTTLNLGQRVGL--GWFsgsCMTC 95
Cdd:cd08234   16 EVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFGAA-PPLVPGHEFAGVVVAVGSKVTGFKVGDRVAVdpNIY---CGEC 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  96 EWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINP---ATAGPLFCggitVFNPIVQFDIKPSDRVGVig 172
Cdd:cd08234   92 FYCRRGRPNLCENLTAVGVTRNGGFAEYVVVPAKQVYKIPDNLSFeeaALAEPLSC----AVHGLDLLGIKPGDSVLV-- 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 173 igglghIALGF--------LQAWG-CEITAFSSSPDKEAEARELGATHFIN--SGDVNALESVQ-NSFDF-ILATANADL 239
Cdd:cd08234  166 ------FGAGPiglllaqlLKLNGaSRVTVAEPNEEKLELAKKLGATETVDpsREDPEAQKEDNpYGFDVvIEATGVPKT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 240 dWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISAspVGS---PATISQMINFAARQGVEP---ITETFSFEQV 313
Cdd:cd08234  240 -LEQAIEYARRGGTVLVFGVYAPDARVSISPFEIFQKELTI--IGSfinPYTFPRAIALLESGKIDVkglVSHRLPLEEV 316

                        330
                 ....*....|.
gi 493029422 314 NEAMEKLRHGK 324
Cdd:cd08234  317 PEALEGMRSGG 327
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 20-326 2.21e-37

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


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 136.58  E-value: 2.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  20 DPgTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGwFSGSCMTCEWCM 99
Cdd:cd08260   20 DP-EPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVP-FVLGCGTCPYCR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 100 SGNHNLCSNAEGTIVSRHGGFADKV---RADYSwVVPLPDGINPATAGPLFCGGITVFNPIV-QFDIKPSDRVGVI---- 171
Cdd:cd08260   98 AGDSNVCEHQVQPGFTHPGSFAEYVavpRADVN-LVRLPDDVDFVTAAGLGCRFATAFRALVhQARVKPGEWVAVHgcgg 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 172 GIGGLGHIAlgflQAWGCEITAFSSSPDKEAEARELGATHFINSGDV-NALESVQN--------SFDfilATANADLDWN 242
Cdd:cd08260  177 VGLSAVMIA----SALGARVIAVDIDDDKLELARELGAVATVNASEVeDVAAAVRDltgggahvSVD---ALGIPETCRN 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 243 AyIAALRPKGRLHFVGVIPNPLSTPIFP---LILGQKSISASPVGSPATISQMINFAARQGVEP---ITETFSFEQVNEA 316
Cdd:cd08260  250 S-VASLRKRGRHVQVGLTLGEEAGVALPmdrVVARELEIVGSHGMPAHRYDAMLALIASGKLDPeplVGRTISLDEAPDA 328

                        330
                 ....*....|
gi 493029422 317 MEKLRHGKPR 326
Cdd:cd08260  329 LAAMDDYATA 338
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 28-133 3.47e-37

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


Pssm-ID: 400513 [Multi-domain]  Cd Length: 106  Bit Score: 128.88  E-value: 3.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   28 EVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSgSCMTCEWCMSGNHNLCS 107
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNLCP 80

                          90       100
                  ....*....|....*....|....*.
gi 493029422  108 NAEGTIVSRHGGFADKVRADYSWVVP 133
Cdd:pfam08240  81 NGRFLGYDRDGGFAEYVVVPERNLVP 106
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 23-324 3.04e-36

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 133.49  E-value: 3.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRV----GLGwfsgsCMTCEWC 98
Cdd:cd08235   21 EPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDRVfvapHVP-----CGECHYC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  99 MSGNHNLCSNAEGTIVSRHGGFADKVRADySW------VVPLPDGIN---PATAGPLFCggitVFNPIVQFDIKPSDRVG 169
Cdd:cd08235   96 LRGNENMCPNYKKFGNLYDGGFAEYVRVP-AWavkrggVLKLPDNVSfeeAALVEPLAC----CINAQRKAGIKPGDTVL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 170 V--IGIGGLGHIALGflQAWGCE-ITAFSSSPDKEAEARELGATHFINSGDVNALESVQNSFDF------ILATANADLd 240
Cdd:cd08235  171 VigAGPIGLLHAMLA--KASGARkVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEKVRELTDGrgadvvIVATGSPEA- 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 241 WNAYIAALRPKGRLHFVGVIPNPLSTPIFPLIL--GQKSISASPVGSPATIS---QMInFAARQGVEP-ITETFSFEQVN 314
Cdd:cd08235  248 QAQALELVRKGGRILFFGGLPKGSTVNIDPNLIhyREITITGSYAASPEDYKealELI-ASGKIDVKDlITHRFPLEDIE 326

                        330
                 ....*....|
gi 493029422 315 EAMEKLRHGK 324
Cdd:cd08235  327 EAFELAADGK 336
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 23-327 1.49e-35

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


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 131.58  E-value: 1.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDLSMLDNEWGMTdYPFVPGHEVVGTIAALGDKVTTLNLGQRVG----LgwfsgSCMTCEWC 98
Cdd:cd08236   21 EPGPGEVLVKVKACGICGSDIPRYLGTGAYH-PPLVLGHEFSGTVEEVGSGVDDLAVGDRVAvnplL-----PCGKCEYC 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  99 MSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAG---PLFCGGITVFnpivQFDIKPSDRVGVIGIGG 175
Cdd:cd08236   95 KKGEYSLCSNYDYIGSRRDGAFAEYVSVPARNLIKIPDHVDYEEAAmiePAAVALHAVR----LAGITLGDTVVVIGAGT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 176 LGHIALGFLQAWGCE-ITAFSSSPDKEAEARELGATHFINSGDVNA---LESVQNS-FDFILATANADLDWNAYIAALRP 250
Cdd:cd08236  171 IGLLAIQWLKILGAKrVIAVDIDDEKLAVARELGADDTINPKEEDVekvRELTEGRgADLVIEAAGSPATIEQALALARP 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 251 KGRLHFVGVIPNPLSTPIFPL--ILGQK--------SISASPVGS--PATIsQMINFAARQGVEPITETFSFEQVNEAME 318
Cdd:cd08236  251 GGKVVLVGIPYGDVTLSEEAFekILRKEltiqgswnSYSAPFPGDewRTAL-DLLASGKIKVEPLITHRLPLEDGPAAFE 329


                 ....*....
gi 493029422 319 KLRHGKPRY 327
Cdd:cd08236  330 RLADREEFS 338
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 2-324 2.83e-35

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


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 131.47  E-value: 2.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   2 IKAYAAHEPGG--QLQPFEYDPgtLGDEEVEIKVEYCGICHSDLSMLDNeWGMTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:cd08278    3 TTAAVVREPGGpfVLEDVELDD--PRPDEVLVRIVATGICHTDLVVRDG-GLPTPLPAVLGHEGAGVVEAVGSAVTGLKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRVGLGWfsGSCMTCEWCMSGNHNLCSN----------AEGTI-VSRHGG------------FADKVRADYSWVVPLPD 136
Cdd:cd08278   80 GDHVVLSF--ASCGECANCLSGHPAYCENffplnfsgrrPDGSTpLSLDDGtpvhghffgqssFATYAVVHERNVVKVDK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 137 GINPATAGPLFCG-----GiTVFNpivQFDIKPSDRvgvigigglghIAL------GF-----LQAWGCE-ITAFSSSPD 199
Cdd:cd08278  158 DVPLELLAPLGCGiqtgaG-AVLN---VLKPRPGSS-----------IAVfgagavGLaavmaAKIAGCTtIIAVDIVDS 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 200 KEAEARELGATHFINSGDVNALESVQNSF----DFIL-ATANADLDWNAyIAALRPKGRLHFVGVIP--NPLSTPIFPLI 272
Cdd:cd08278  223 RLELAKELGATHVINPKEEDLVAAIREITgggvDYALdTTGVPAVIEQA-VDALAPRGTLALVGAPPpgAEVTLDVNDLL 301

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 493029422 273 LGQKSISASPVGS--PAT-ISQMINFaARQG---VEPITETFSFEQVNEAMEKLRHGK 324
Cdd:cd08278  302 VSGKTIRGVIEGDsvPQEfIPRLIEL-YRQGkfpFDKLVTFYPFEDINQAIADSESGK 358
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 28-330 1.57e-32

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


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 124.02  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWGMTDyPFVPGHEVVGTIAALGDKVT---TLNLGQRVgLGWFSGSCMTCEWCMSGNHN 104
Cdd:cd08263   27 EILIRVAACGVCHSDLHVLKGELPFPP-PFVLGHEISGEVVEVGPNVEnpyGLSVGDRV-VGSFIMPCGKCRYCARGKEN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 105 LCSNA-----------EGT--IVSRH---------GGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF-D 161
Cdd:cd08263  105 LCEDFfaynrlkgtlyDGTtrLFRLDggpvymysmGGLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALKHAaD 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 162 IKPSDRVGVIGIGGLGHIALGFLQAWGC-EITAFSSSPDKEAEARELGATHFINSGDVNALESVQN-----SFDFILATA 235
Cdd:cd08263  185 VRPGETVAVIGVGGVGSSAIQLAKAFGAsPIIAVDVRDEKLAKAKELGATHTVNAAKEDAVAAIREitggrGVDVVVEAL 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 236 NADLDWNAYIAALRPKGRLHFVGVIPNPLST--PIFPLILGQKSISASPVGSPAT-ISQMINFAARQGVEP---ITETFS 309
Cdd:cd08263  265 GKPETFKLALDVVRDGGRAVVVGLAPGGATAeiPITRLVRRGIKIIGSYGARPRQdLPELVGLAASGKLDPealVTHKYK 344

                        330       340
                 ....*....|....*....|.
gi 493029422 310 FEQVNEAMEKLRHGKPRYRLV 330
Cdd:cd08263  345 LEEINEAYENLRKGLIHGRAI 365
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 25-316 5.75e-31

L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as a threonine dehydrogenase. L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)-dependent oxidation. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Zinc-dependent ADHs are medium chain dehydrogenase/reductase type proteins (MDRs) and have a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. In addition to alcohol dehydrogenases, this group includes quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176201 [Multi-domain]  Cd Length: 339  Bit Score: 119.35  E-value: 5.75e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  25 GDEEVEIKVEYCGICHSDLSMLDNEWGMTDYP-FVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSGsCMTCEWCMSGNH 103
Cdd:cd08239   23 GPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQgVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHYVG-CGACRNCRRGWM 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 104 NLCSNAEGTI-VSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVIGIGGLGHIALG 182
Cdd:cd08239  102 QLCTSKRAAYgWNRDGGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLGALM 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 183 FLQAWGCE-ITAFSSSPDKEAEARELGATHFINSGDVNALESVQNS----FDFILATANADLDWNAYIAALRPKGRLHFV 257
Cdd:cd08239  182 LARALGAEdVIGVDPSPERLELAKALGADFVINSGQDDVQEIRELTsgagADVAIECSGNTAARRLALEAVRPWGRLVLV 261

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493029422 258 GVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEP---ITETFSFEQVNEA 316
Cdd:cd08239  262 GEGGELTIEVSNDLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVdrlVTHRFGLDQAPEA 323
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 20-281 4.79e-29

(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent medium chain alcohol dehydrogenase, catalyzes the NAD(+)-dependent oxidation of (2R,3R)-2,3-butanediol and meso-butanediol to acetoin. BDH functions as a homodimer. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit.


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 114.17  E-value: 4.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  20 DPGTLGDEEVEIKVEYCGICHSDL---------SMLDNEWGMT--DYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGwF 88
Cdd:cd08233   18 PEPPVKPGEVKIKVAWCGICGSDLheyldgpifIPTEGHPHLTgeTAPVTLGHEFSGVVVEVGSGVTGFKVGDRVVVE-P 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  89 SGSCMTCEWCMSGNHNLCSNAeGTI--VSRHGGFADKVRADYSWVVPLPDGINPATAG---PLfcggiTV-FNPIVQFDI 162
Cdd:cd08233   97 TIKCGTCGACKRGLYNLCDSL-GFIglGGGGGGFAEYVVVPAYHVHKLPDNVPLEEAAlvePL-----AVaWHAVRRSGF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 163 KPSDRvgvigigglghiALGF------------LQAWGC-EITAFSSSPDKEAEARELGATHFINSGDVNALESVQ---- 225
Cdd:cd08233  171 KPGDT------------ALVLgagpiglltilaLKAAGAsKIIVSEPSEARRELAEELGATIVLDPTEVDVVAEVRkltg 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493029422 226 -NSFDFILATANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISAS 281
Cdd:cd08233  239 gGGVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGS 295
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 23-331 1.94e-27

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


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 109.59  E-value: 1.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSgSCMTCEWCMSGN 102
Cdd:cd08261   21 VPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGEGVAGLKVGDRVVVDPYI-SCGECYACRKGR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 103 HNLCSNAEGTIVSRHGGFADK--VRADYswvVPLPDGINPATAG---PLFCGgitvFNPIVQFDIKPSDRVGVIGIGGlg 177
Cdd:cd08261  100 PNCCENLQVLGVHRDGGFAEYivVPADA---LLVPEGLSLDQAAlvePLAIG----AHAVRRAGVTAGDTVLVVGAGP-- 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 178 hIALG---FLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQ-----NSFDFIL-ATANADLdWNAYIAAL 248
Cdd:cd08261  171 -IGLGviqVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLReltdgEGADVVIdATGNPAS-MEEAVELV 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 249 RPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEP---ITETFSFEQVNEAMEKLRHGKP 325
Cdd:cd08261  249 AHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPealITHRFPFEDVPEAFDLWEAPPG 328


                 ....*.
gi 493029422 326 RYRLVL 331
Cdd:cd08261  329 GVIKVL 334
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 3-331 2.59e-27

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: 108.80  E-value: 2.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYD---PgTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDY---PFVPGHEVVGTIAALGDKVTT 76
Cdd:cd05289    2 KAVRIHEYGGPEVLELADvptP-EPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPltlPLIPGHDVAGVVVAVGPGVTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  77 LNLGQRVglgwfsgscmtceWCMSGnhnlcsnaegtiVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNP 156
Cdd:cd05289   81 FKVGDEV-------------FGMTP------------FTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQA 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 157 IVQF-DIKPSDRvgvig-igglgHIALGFLQAWGCEITAfSSSPDKEAEARELGATHFINSGDVNALESVQ-NSFDFILA 233
Cdd:cd05289  136 LFELgGLKAGQTvlihgaaggvgSFAVQLAKARGARVIA-TASAANADFLRSLGADEVIDYTKGDFERAAApGGVDAVLD 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 234 TANADlDWNAYIAALRPKGRLhfVGVIPnplsTPIFPLILGQKSISASPV---GSPATISQMINFAARQGVEP-ITETFS 309
Cdd:cd05289  215 TVGGE-TLARSLALVKPGGRL--VSIAG----PPPAEQAAKRRGVRAGFVfvePDGEQLAELAELVEAGKLRPvVDRVFP 287

                        330       340
                 ....*....|....*....|..
gi 493029422 310 FEQVNEAMEKLRHGKPRYRLVL 331
Cdd:cd05289  288 LEDAAEAHERLESGHARGKVVL 309
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 25-334 2.72e-27

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 109.36  E-value: 2.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  25 GDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVgLGWFSGSCMTCEWCMSGNHN 104
Cdd:PRK13771  24 GKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPGDRV-ASLLYAPDGTCEYCRSGEEA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 105 LCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVIGIGGLGHI-ALGF 183
Cdd:PRK13771 103 YCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGLRRAGVKKGETVLVTGAGGGVGIhAIQV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 184 LQAWGCEITAFSSSPDKeAEARELGATHFIN----SGDVNALESVqnsfDFILATANADlDWNAYIAALRPKGRLHFVG- 258
Cdd:PRK13771 183 AKALGAKVIAVTSSESK-AKIVSKYADYVIVgskfSEEVKKIGGA----DIVIETVGTP-TLEESLRSLNMGGKIIQIGn 256

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493029422 259 VIPNP-LSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEP-ITETFSFEQVNEAMEKLRHGKPRYRLVLKHS 334
Cdd:PRK13771 257 VDPSPtYSLRLGYIILKDIEIIGHISATKRDVEEALKLVAEGKIKPvIGAEVSLSEIDKALEELKDKSRIGKILVKPS 334
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
178-298 3.58e-27

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 103.46  E-value: 3.58e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  178 HIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQ-----NSFDFILATANADLDWNAYIAALRPKG 252
Cdd:pfam00107   4 LAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKeltggKGVDVVFDCVGSPATLEQALKLLRPGG 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 493029422  253 RLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINFAAR 298
Cdd:pfam00107  84 RVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 3-279 3.98e-27

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: 108.17  E-value: 3.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPG-GQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQ 81
Cdd:cd08258    2 KALVKTGPGpGNVELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  82 RVGLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGInPATAG----PLFCggitVFNPI 157
Cdd:cd08258   82 RVVSETTFSTCGRCPYCRRGDYNLCPHRKGIGTQADGGFAEYVLVPEESLHELPENL-SLEAAaltePLAV----AVHAV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 158 VQ-FDIKPSDRVGVIGIGglghiALGFLQAWGC-----EITAFSSSPDKE--AEARELGATHfINSGDVNALESVQ---- 225
Cdd:cd08258  157 AErSGIRPGDTVVVFGPG-----PIGLLAAQVAklqgaTVVVVGTEKDEVrlDVAKELGADA-VNGGEEDLAELVNeitd 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 226 -NSFDFILATANADLDWNAYIAALRPKGRLHFVGvIPNPLSTPIFPLILGQKSIS 279
Cdd:cd08258  231 gDGADVVIECSGAVPALEQALELLRKGGRIVQVG-IFGPLAASIDVERIIQKELS 284
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 6-331 1.64e-26

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


Pssm-ID: 176241 [Multi-domain]  Cd Length: 371  Bit Score: 107.85  E-value: 1.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   6 AAHEPGGQLQPF-----EYDPGTLGdeEVEIKVEYCGICHSDLSMLDNEwGMTDYPFVPGHEVVGTIAALGDKVTTLNLG 80
Cdd:cd08281   10 GAPTPYADSRPLvieevELDPPGPG--EVLVKIAAAGLCHSDLSVINGD-RPRPLPMALGHEAAGVVVEVGEGVTDLEVG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  81 QRVGLGwFSGSCMTCEWCMSGNHNLC-----SNAEGTIVS-------------RHGG---FADKVRADYSWVVPLPDGIN 139
Cdd:cd08281   87 DHVVLV-FVPSCGHCRPCAEGRPALCepgaaANGAGTLLSggrrlrlrggeinHHLGvsaFAEYAVVSRRSVVKIDKDVP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 140 PATAGPLFCGGIT----VFNPIvqfDIKPSDRVGVIGIGGLGHIA-LGFLQAWGCEITAFSSSPDKEAEARELGATHFIN 214
Cdd:cd08281  166 LEIAALFGCAVLTgvgaVVNTA---GVRPGQSVAVVGLGGVGLSAlLGAVAAGASQVVAVDLNEDKLALARELGATATVN 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 215 SGDVNALESVQN------SFDFILATANADLDwNAYiAALRPKGRLHFVGvIPNP---LSTPIFPLILGQKSISASPVGS 285
Cdd:cd08281  243 AGDPNAVEQVREltgggvDYAFEMAGSVPALE-TAY-EITRRGGTTVTAG-LPDPearLSVPALSLVAEERTLKGSYMGS 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493029422 286 --PA-TISQMINFaARQGVEPI----TETFSFEQVNEAMEKLRHGKPRYRLVL 331
Cdd:cd08281  320 cvPRrDIPRYLAL-YLSGRLPVdkllTHRLPLDEINEGFDRLAAGEAVRQVIL 371
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 18-318 1.68e-26

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 107.32  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  18 EYDPGTLGDEEVEIKVEYCGICHSDLS-MLDNEWGMTD--YPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGwFSGSCMT 94
Cdd:cd08232   13 ERPAPEPGPGEVRVRVAAGGICGSDLHyYQHGGFGTVRlrEPMVLGHEVSGVVEAVGPGVTGLAPGQRVAVN-PSRPCGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  95 CEWCMSGNHNLCSN-----AEGTIVSRHGGFADKVRADYSWVVPLPDGINPAT----------------AGPLFcgGITV 153
Cdd:cd08232   92 CDYCRAGRPNLCLNmrflgSAMRFPHVQGGFREYLVVDASQCVPLPDGLSLRRaalaeplavalhavnrAGDLA--GKRV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 154 F----NPIvqfdikpsdrvgvigiggLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGD--VNALESVQNS 227
Cdd:cd08232  170 LvtgaGPI------------------GALVVAAARRAGAAEIVATDLADAPLAVARAMGADETVNLARdpLAAYAADKGD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 228 FDFILATANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLIlgQKSISAspVGSP------ATISQMINfAARQGV 301
Cdd:cd08232  232 FDVVFEASGAPAALASALRVVRPGGTVVQVGMLGGPVPLPLNALV--AKELDL--RGSFrfddefAEAVRLLA-AGRIDV 306

                        330
                 ....*....|....*...
gi 493029422 302 EP-ITETFSFEQVNEAME 318
Cdd:cd08232  307 RPlITAVFPLEEAAEAFA 324
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 3-332 1.74e-23

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 98.50  E-value: 1.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLG 80
Cdd:cd08271    2 KAWVLPKPGAalQLTLEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  81 QRVglgwfsgscmtcewcmSGNHNLcsnaegtivSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFnpiVQF 160
Cdd:cd08271   82 DRV----------------AYHASL---------ARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAY---QAL 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 161 DIKPSDRVGVIGIGGLG-----HIALGFLQAWGCEITAfSSSPDKEAEARELGATHFINSGDVNALESVQNS-----FDF 230
Cdd:cd08271  134 FKKLRIEAGRTILITGGaggvgSFAVQLAKRAGLRVIT-TCSKRNFEYVKSLGADHVIDYNDEDVCERIKEItggrgVDA 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 231 ILATANADLDwNAYIAALRPKGrlHFVGVIPNPLSTPIFPLilgQKSISASPV--------GSPATISQ-------MINF 295
Cdd:cd08271  213 VLDTVGGETA-AALAPTLAFNG--HLVCIQGRPDASPDPPF---TRALSVHEValgaahdhGDPAAWQDlryageeLLEL 286

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 493029422 296 AARQGVEP-ITETFSFEQVNEAMEKLRHGKPRYRLVLK 332
Cdd:cd08271  287 LAAGKLEPlVIEVLPFEQLPEALRALKDRHTRGKIVVT 324
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 11-319 2.23e-23

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


Pssm-ID: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 98.09  E-value: 2.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  11 GGQLQPF-EYDPGTLGDEEVEIKVEYCGICHSDLSMLDNewgmtDYPF--VPGHEVVGTIAALGDKvtTLnLGQRVGlGW 87
Cdd:cd08242    8 GGLDLRVeDLPKPEPPPGEALVRVLLAGICNTDLEIYKG-----YYPFpgVPGHEFVGIVEEGPEA--EL-VGKRVV-GE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  88 FSGSCMTCEWCMSGNHNLCSNAE--GtIVSRHGGFAD--KVRADYSWVVPLPDGINPAT-AGPLfcggITVFNPIVQFDI 162
Cdd:cd08242   79 INIACGRCEYCRRGLYTHCPNRTvlG-IVDRDGAFAEylTLPLENLHVVPDLVPDEQAVfAEPL----AAALEILEQVPI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 163 KPSDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALEsvqnSFDFIL-ATANADlDW 241
Cdd:cd08242  154 TPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLGVETVLPDEAESEGG----GFDVVVeATGSPS-GL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 242 NAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGS-PATIsqminFAARQG---VEP-ITETFSFEQVNEA 316
Cdd:cd08242  229 ELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVGSRCGPfAPAL-----RLLRKGlvdVDPlITAVYPLEEALEA 303


                 ...
gi 493029422 317 MEK 319
Cdd:cd08242  304 FER 306
Rxyl_3153 TIGR03989
NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within ...
 3-324 2.68e-23

NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within the family pfam00107 of zinc-binding dehydrogenases. The family pfam00107 contains class III alcohol dehydrogenases, including enzymes designated S-(hydroxymethyl)glutathione dehydrogenase and NAD/mycothiol-dependent formaldehyde dehydrogenase. Members of the current family occur only in species that contain the very small protein mycofactocin (TIGR03969), a possible cofactor precursor, and radical SAM protein TIGR03962. We name this family for Rxyl_3153, where the lone member of the family co-clusters with these markers in Rubrobacter xylanophilus. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274905 [Multi-domain]  Cd Length: 369  Bit Score: 98.93  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422    3 KAYAAHEPGgqlQPFEYDPGTLGDE---EVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:TIGR03989   3 KAAVLWGPG---QPWEVEEIELDDPkagEVLVKLVASGLCHSDEHLVTGDLPMPRYPILGGHEGAGVVTKVGPGVTGVKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   80 GQRVGLGwFSGSCMTCEWCMSGNHNLCSN----------AEGTIVSRHGG-----------FADKVRADYSWVVPLPDGI 138
Cdd:TIGR03989  80 GDHVVLS-FIPACGRCRYCSTGLQNLCDLgaalltgsqiSDGTYRFHADGqdvgqmcllgtFSEYTVVPEASVVKIDDDI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  139 NPATAGPLFCGGITVFNPIVQF-DIKPSDrvgVIGIGGLGHIALGFLQ----AWGCEITAFSSSPDKEAEARELGATHFI 213
Cdd:TIGR03989 159 PLDKACLVGCGVPTGWGSAVNIaDVRPGD---TVVVMGIGGVGINAVQgaavAGARKVIAVDPVEFKREQALKFGATHAF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  214 NSGD-----VNALESVQNSFDFILATANADLDWNA-YIAALRPKGRLHFVGVIP---NPLSTPIFPLILGQKSISASPVG 284
Cdd:TIGR03989 236 ASMEeavqlVRELTNGQGADKTIITVGEVDGEHIAeALSATRKGGRVVVTGLGPmadVDVKVNLFELTLLQKELQGTLFG 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 493029422  285 SPATISQMINFAA--RQGV----EPITETFSFEQVNEAMEKLRHGK 324
Cdd:TIGR03989 316 GANPRADIPRLLElyRAGKlkldELITRTYTLDQINEGYQDMLDGK 361
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 28-332 4.29e-23

Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 98.28  E-value: 4.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWgMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLgWFSGSCMTCEWCMSGNHNLCS 107
Cdd:cd05279   27 EVRIKVVATGVCHTDLHVIDGKL-PTPLPVILGHEGAGIVESIGPGVTTLKPGDKVIP-LFGPQCGKCKQCLNPRPNLCS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 108 NA------------------EGTIVSRHGG---FADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQ-FDIKP- 164
Cdd:cd05279  105 KSrgtngrglmsdgtsrftcKGKPIHHFLGtstFAEYTVVSEISLAKIDPDAPLEKVCLIGCGFSTGYGAAVNtAKVTPg 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 165 SDRVGVIGIGGLGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGD-----VNAL-ESVQNSFDFIL-ATANA 237
Cdd:cd05279  185 STCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECINPRDqdkpiVEVLtEMTDGGVDYAFeVIGSA 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 238 DLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLIL-GQKSISASPVGSPATISQMINFAA--RQGVEP----ITETFSF 310
Cdd:cd05279  265 DTLKQALDATRLGGGTSVVVGVPPSGTEATLDPNDLlTGRTIKGTVFGGWKSKDSVPKLVAlyRQKKFPldelITHVLPF 344

                        330       340
                 ....*....|....*....|..
gi 493029422 311 EQVNEAMEKLRHGKPrYRLVLK 332
Cdd:cd05279  345 EEINDGFDLMRSGES-IRTILT 365
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 3-332 4.37e-23

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: 97.57  E-value: 4.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG-------QLQPfeyDPGTLGdeEVEIKVEYCGICHSDLSMLDNEWGMT-DYPFVPGHEVVGTIAALGDKV 74
Cdd:cd08241    2 KAVVCKELGGpedlvleEVPP---EPGAPG--EVRIRVEAAGVNFPDLLMIQGKYQVKpPLPFVPGSEVAGVVEAVGEGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  75 TTLNLGQRVgLGWfsgscmtcewcmsgnhnlcsnaegtivSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVf 154
Cdd:cd08241   77 TGFKVGDRV-VAL---------------------------TGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTA- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 155 npivqfdikpsdrvgvigigglgHIAL---GFLQ-----------------------AWGCEITAFSSSPDKEAEARELG 208
Cdd:cd08241  128 -----------------------YHALvrrARLQpgetvlvlgaaggvglaavqlakALGARVIAAASSEEKLALARALG 184

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 209 ATHFINSGDVNALESVQnsfdfiLATANADLD----------WNAYIAALRPKGRLHFVGV----IPN-PLSTPIFplil 273
Cdd:cd08241  185 ADHVIDYRDPDLRERVK------ALTGGRGVDvvydpvggdvFEASLRSLAWGGRLLVIGFasgeIPQiPANLLLL---- 254

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493029422 274 gqKSISAspVG---------SPATISQMIN-----FAARQGVEPITETFSFEQVNEAMEKLRHGKPRYRLVLK 332
Cdd:cd08241  255 --KNISV--VGvywgayarrEPELLRANLAelfdlLAEGKIRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 23-324 9.01e-23

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


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 96.94  E-value: 9.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDLSMLDNEWGMT-DYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLgwFSG-SCMTCEWCMS 100
Cdd:cd08266   24 EPGPDEVLVRVKAAALNHLDLWVRRGMPGIKlPLPHILGSDGAGVVEAVGPGVTNVKPGQRVVI--YPGiSCGRCEYCLA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 101 GNHNLCsnAEGTIVSRH--GGFADKVRADYSWVVPLPDGIN--PATAGPL-FcggITVFNPIV-QFDIKPSDRVGVIGIG 174
Cdd:cd08266  102 GRENLC--AQYGILGEHvdGGYAEYVAVPARNLLPIPDNLSfeEAAAAPLtF---LTAWHMLVtRARLRPGETVLVHGAG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 175 G-LGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFIN------SGDVNAL---ESVQNSFDFILATAnadldWNAY 244
Cdd:cd08266  177 SgVGSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDyrkedfVREVRELtgkRGVDVVVEHVGAAT-----WEKS 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 245 IAALRPKGRLHFV----GVIPNplsTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEP-ITETFSFEQVNEAMEK 319
Cdd:cd08266  252 LKSLARGGRLVTCgattGYEAP---IDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKPvIDSVFPLEEAAEAHRR 328


                 ....*
gi 493029422 320 LRHGK 324
Cdd:cd08266  329 LESRE 333
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 18-332 9.53e-23

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 96.79  E-value: 9.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  18 EYDPGTLGDEEVEIKVEYCGICHSDLSMLDN----EWGMTDyPFVPGHEVVGTIAALGDKVTTLNLGQRV----GLgwfs 89
Cdd:cd05285   14 ERPIPEPGPGEVLVRVRAVGICGSDVHYYKHgrigDFVVKE-PMVLGHESAGTVVAVGSGVTHLKVGDRVaiepGV---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  90 gSCMTCEWCMSGNHNLCSNAE--GTIVSrHGGFADKVRADYSWVVPLPDGINPATAG---PLFCGgitvfnpiVQF---- 160
Cdd:cd05285   89 -PCRTCEFCKSGRYNLCPDMRfaATPPV-DGTLCRYVNHPADFCHKLPDNVSLEEGAlvePLSVG--------VHAcrra 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 161 DIKPSDRvgvigigglghiAL-------GFL-----QAWGC-EITAFSSSPDKEAEARELGATHFINSGDVNALESVQN- 226
Cdd:cd05285  159 GVRPGDT------------VLvfgagpiGLLtaavaKAFGAtKVVVTDIDPSRLEFAKELGATHTVNVRTEDTPESAEKi 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 227 -------SFDFILATANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSIsaspVGS-------PATI--- 289
Cdd:cd05285  227 aellggkGPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDI----RGVfryantyPTAIell 302

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 493029422 290 -SQMINfaarqgVEP-ITETFSFEQVNEAMEKLRHGKPryrLVLK 332
Cdd:cd05285  303 aSGKVD------VKPlITHRFPLEDAVEAFETAAKGKK---GVIK 338
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 3-278 1.73e-22

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


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 95.58  E-value: 1.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGichsdLSMLDNEW--GM--TDYPFVPGHEVVGTIAALGDKVTT 76
Cdd:cd05286    1 KAVRIHKTGGpeVLEYEDVPVPEPGPGEVLVRNTAIG-----VNFIDTYFrsGLypLPLPFVLGVEGAGVVEAVGPGVTG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  77 LNLGQRVGlgwfsgscmtceWCMSGnhnlcsnaegtivsrhGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNP 156
Cdd:cd05286   76 FKVGDRVA------------YAGPP----------------GAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAHYL 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 157 IVQ-FDIKPSDRvgvigigGLGHIALG----FLQAW----GCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQN- 226
Cdd:cd05286  128 LREtYPVKPGDT-------VLVHAAAGgvglLLTQWakalGATVIGTVSSEEKAELARAAGADHVINYRDEDFVERVREi 200

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493029422 227 --------SFDFI-LATANADLDwnayiaALRPKGRlhFV------GVIPnplstPIFPLILGQKSI 278
Cdd:cd05286  201 tggrgvdvVYDGVgKDTFEGSLD------SLRPRGT--LVsfgnasGPVP-----PFDLLRLSKGSL 254
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 4-324 2.51e-22

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 95.79  E-value: 2.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   4 AYAA--HEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQ 81
Cdd:cd08231    1 ARAAvlTGPGKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTDVAGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  82 RVGLG----WFSG-SCMTCEWCMSGNHNLCSNaeGTIVSR---------HGGFADK--VRADySWVVPLPDGINPATAGP 145
Cdd:cd08231   81 PLKVGdrvtWSVGaPCGRCYRCLVGDPTKCEN--RKKYGHeascddphlSGGYAEHiyLPPG-TAIVRVPDNVPDEVAAP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 146 LFCGGITVFNPIvqfdikpsDRVGVIGIGGLGHI---------ALGFLQAWGCE-ITAFSSSPDKEAEARELGATHFINs 215
Cdd:cd08231  158 ANCALATVLAAL--------DRAGPVGAGDTVVVqgagplglyAVAAAKLAGARrVIVIDGSPERLELAREFGADATID- 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 216 GDVNALESVQNSFDFILATANADL--DW-------NAYIAALRPKGRLHFVGVIPNPLSTPIFP--LILGQKSISASPVG 284
Cdd:cd08231  229 IDELPDPQRRAIVRDITGGRGADVviEAsghpaavPEGLELLRRGGTYVLVGSVAPAGTVPLDPerIVRKNLTIIGVHNY 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 493029422 285 SPATISQMINFAAR-QGVEP----ITETFSFEQVNEAMEKLRHGK 324
Cdd:cd08231  309 DPSHLYRAVRFLERtQDRFPfaelVTHRYPLEDINEALELAESGT 353
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 23-331 4.01e-22

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: 94.59  E-value: 4.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDLSMLDNEWGMTD---YPFVPGHEVVGTIAALGDKVTTLNLGQRVgLGWFSgscmtcewcm 99
Cdd:cd08267   23 TPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLgrpFPPIPGMDFAGEVVAVGSGVTRFKVGDEV-FGRLP---------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 100 sgnhnlcsnaegtiVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF-DIKPSDRvgvig-igglg 177
Cdd:cd08267   92 --------------PKGGGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAgKVKPGQRvlingasggvg 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 178 HIALGFLQAWGCEITAfSSSPDKEAEARELGATHFIN--SGDVNALESVQNSFDFILATANaDLDWNAYIAALRPKGRLH 255
Cdd:cd08267  158 TFAVQIAKALGAHVTG-VCSTRNAELVRSLGADEVIDytTEDFVALTAGGEKYDVIFDAVG-NSPFSLYRASLALKPGGR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 256 FVGVIPNP-------LSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVEP-ITETFSFEQVNEAMEKLRHGKPRY 327
Cdd:cd08267  236 YVSVGGGPsglllvlLLLPLTLGGGGRRLKFFLAKPNAEDLEQLAELVEEGKLKPvIDSVYPLEDAPEAYRRLKSGRARG 315


                 ....
gi 493029422 328 RLVL 331
Cdd:cd08267  316 KVVI 319
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 3-325 1.21e-21

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: 93.75  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWG-MTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:cd08276    2 KAWRLSGGGGldNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPpPVKDPLIPLSDGAGEVVAVGEGVTRFKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRV----GLGWFSGSCMTCEWcmsgnhnlcSNAEGtiVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:cd08276   82 GDRVvptfFPNWLDGPPTAEDE---------ASALG--GPIDGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWN 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQ-FDIKPSDRVgvigigglghIALG----------FLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVN----- 219
Cdd:cd08276  151 ALFGlGPLKPGDTV----------LVQGtggvslfalqFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPdwgee 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 220 ALESVQNS-FDFILATANAD-LDwnAYIAALRPKGRLHFVGVI-PNPLSTPIFPLILGQKSISASPVGSPATISQMINFA 296
Cdd:cd08276  221 VLKLTGGRgVDHVVEVGGPGtLA--QSIKAVAPGGVISLIGFLsGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAI 298

                        330       340       350
                 ....*....|....*....|....*....|
gi 493029422 297 ARQGVEP-ITETFSFEQVNEAMEKLRHGKP 325
Cdd:cd08276  299 EAHRIRPvIDRVFPFEEAKEAYRYLESGSH 328
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 3-332 2.57e-21

Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 93.17  E-value: 2.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDnEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd08277    4 KAAVAWEAGKPLVIEEIEVAPPKANEVRIKMLATSVCHTDILAIE-GFKATLFPVILGHEGAGIVESVGEGVTNLKPGDK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VgLGWFSGSCMTCEWCMSGNHNLCSN---------AEGTivSRHGGFADKVRA-------------DYSWVVPLPDGINP 140
Cdd:cd08277   83 V-IPLFIGQCGECSNCRSGKTNLCQKyranesglmPDGT--SRFTCKGKKIYHflgtstfsqytvvDENYVAKIDPAAPL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 141 ATAGPLFCGGITVFNPIVQ-FDIKPSDRVGVIGIGglghiALGFLQAWGC------EITAFSSSPDKEAEARELGATHFI 213
Cdd:cd08277  160 EHVCLLGCGFSTGYGAAWNtAKVEPGSTVAVFGLG-----AVGLSAIMGAkiagasRIIGVDINEDKFEKAKEFGATDFI 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 214 NSGDvnALESVQ--------NSFDFIL-ATANADLDWNAYIAALRPKGRLHFVGVIPNP-LSTPIFPLILGqKSISASPV 283
Cdd:cd08277  235 NPKD--SDKPVSeviremtgGGVDYSFeCTGNADLMNEALESTKLGWGVSVVVGVPPGAeLSIRPFQLILG-RTWKGSFF 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 284 GSPATISQMINFAARQGVEP------ITETFSFEQVNEAMEKLRHGKpRYRLVLK 332
Cdd:cd08277  312 GGFKSRSDVPKLVSKYMNKKfdldelITHVLPFEEINKGFDLMKSGE-CIRTVIT 365
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 12-324 4.77e-21

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


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 91.65  E-value: 4.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  12 GQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPF---VPGHEVVGTIAALGDKVTTLNLGQRVgLGWF 88
Cdd:cd08269    5 GRFEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFVYPAepgGPGHEGWGRVVALGPGVRGLAVGDRV-AGLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  89 SGscmtcewcmsgnhnlcsnaegtivsrhgGFADKVRADYSWVVPLPDGIN--PATAGPLFCggitVFNPIVQFDIKPSD 166
Cdd:cd08269   84 GG----------------------------AFAEYDLADADHAVPLPSLLDgqAFPGEPLGC----ALNVFRRGWIRAGK 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 167 RVGVIGIGGLGHIALGFLQAWGCE-ITAFSSSPDKEAEARELGATHFINSGDVNALESVQ-----NSFDFILATANADLD 240
Cdd:cd08269  132 TVAVIGAGFIGLLFLQLAAAAGARrVIAIDRRPARLALARELGATEVVTDDSEAIVERVReltggAGADVVIEAVGHQWP 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 241 WNAYIAALRPKGRLHFVGVIPNPLSTPIFPLIL--GQKSISASPvGSPATISQMINFAAR---QGV----EPITETFSFE 311
Cdd:cd08269  212 LDLAGELVAERGRLVIFGYHQDGPRPVPFQTWNwkGIDLINAVE-RDPRIGLEGMREAVKliaDGRldlgSLLTHEFPLE 290

                        330
                 ....*....|...
gi 493029422 312 QVNEAMEKLRHGK 324
Cdd:cd08269  291 ELGDAFEAARRRP 303
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 3-324 1.25e-20

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


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 90.76  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLD-NEW--GMTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:cd05281    2 KAIVKTKAGPGAELVEVPVPKPGPGEVLIKVLAASICGTDVHIYEwDEWaqSRIKPPLIFGHEFAGEVVEVGEGVTRVKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRVglgwfSG----SCMTCEWCMSGNHNLCSNAEGTIVSRHGGFAD--KVRADYSWVV-------------PLPDGINP 140
Cdd:cd05281   82 GDYV-----SAethiVCGKCYQCRTGNYHVCQNTKILGVDTDGCFAEyvVVPEENLWKNdkdippeiasiqePLGNAVHT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 141 ATAGPLF--------CGGITVFnpivqfdikpsdrvgvigigglghiALGFLQAWGCE-ITAFSSSPDKEAEARELGATH 211
Cdd:cd05281  157 VLAGDVSgksvlitgCGPIGLM-------------------------AIAVAKAAGASlVIASDPNPYRLELAKKMGADV 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 212 FINSG--DVNALESVQNSF--DFILATANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLIL----------GQKS 277
Cdd:cd05281  212 VINPReeDVVEVKSVTDGTgvDVVLEMSGNPKAIEQGLKALTPGGRVSILGLPPGPVDIDLNNLVIfkgltvqgitGRKM 291

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 493029422 278 ISaspvgspaTISQMINFAARQGVEP---ITETFSFEQVNEAMEKLRHGK 324
Cdd:cd05281  292 FE--------TWYQVSALLKSGKVDLspvITHKLPLEDFEEAFELMRSGK 333
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 8-333 3.58e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 89.58  E-value: 3.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   8 HEPGGQ--LQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWG-MTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVG 84
Cdd:cd08268    7 HQFGGPevLRIEELPVPAPGAGEVLIRVEAIGLNRADAMFRRGAYIePPPLPARLGYEAAGVVEAVGAGVTGFAVGDRVS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  85 LgwfsgscmtCEWCMSGnhnlcsnaegtivsRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF-DIK 163
Cdd:cd08268   87 V---------IPAADLG--------------QYGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELaGLR 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 164 PSDRVGVIGIGGLghIALGFLQ---AWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVqnsfDFILATANADL- 239
Cdd:cd08268  144 PGDSVLITAASSS--VGLAAIQianAAGATVIATTRTSEKRDALLALGAAHVIVTDEEDLVAEV----LRITGGKGVDVv 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 240 -------DWNAYIAALRPKGRLHFVGvIPNPLSTPiFPLILG-QKSIS------ASPVGSPATISQM---INFAARQGV- 301
Cdd:cd08268  218 fdpvggpQFAKLADALAPGGTLVVYG-ALSGEPTP-FPLKAAlKKSLTfrgyslDEITLDPEARRRAiafILDGLASGAl 295

                        330       340       350
                 ....*....|....*....|....*....|...
gi 493029422 302 -EPITETFSFEQVNEAMEKLRHGKPRYRLVLKH 333
Cdd:cd08268  296 kPVVDRVFPFDDIVEAHRYLESGQQIGKIVVTP 328
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 18-323 4.93e-19

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: 86.25  E-value: 4.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  18 EYDPGTLGDEEVEIKVEYCGICHSDLSMLdNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGL--GWFSGscmTC 95
Cdd:cd08264   18 DVKDPKPGPGEVLIRVKMAGVNPVDYNVI-NAVKVKPMPHIPGAEFAGVVEEVGDHVKGVKKGDRVVVynRVFDG---TC 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  96 EWCMSGNHNLCSNaeGTIVS--RHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVIGI 173
Cdd:cd08264   94 DMCLSGNEMLCRN--GGIIGvvSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKTAGLGPGETVVVFGA 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 174 GGLGHI-ALGFLQAWGCEITAFSSSPDkeaeARELGATHFINSgdVNALESVQN---SFDFILATANADLdWNAYIAALR 249
Cdd:cd08264  172 SGNTGIfAVQLAKMMGAEVIAVSRKDW----LKEFGADEVVDY--DEVEEKVKEitkMADVVINSLGSSF-WDLSLSVLG 244

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 250 PKGRLHFVGVIP-NPLSTPIFPLILGQKSISASPVGSPATISQMINFAARQGVePITETFSFEQVNEAMEKLRHG 323
Cdd:cd08264  245 RGGRLVTFGTLTgGEVKLDLSDLYSKQISIIGSTGGTRKELLELVKIAKDLKV-KVWKTFKLEEAKEALKELFSK 318
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 20-259 7.26e-18

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 83.08  E-value: 7.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  20 DPGTLGDEEVEIKVEYCGICHSDLSMLDNEwGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVgLGWFSGSCMTCEWCM 99
Cdd:cd08284   19 IPQIQDPTDAIVKVTAAAICGSDLHIYRGH-IPSTPGFVLGHEFVGEVVEVGPEVRTLKVGDRV-VSPFTIACGECFYCR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 100 SGNHNLC--SNAEGTIVSR--HGGFADKVR---ADYSwVVPLPDGINPATAgpLFCGGI--TVFNPIVQFDIKPSDRVGV 170
Cdd:cd08284   97 RGQSGRCakGGLFGYAGSPnlDGAQAEYVRvpfADGT-LLKLPDGLSDEAA--LLLGDIlpTGYFGAKRAQVRPGDTVAV 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 171 IGIGGLGHIALGFLQAWGCE-ITAFSSSPDKEAEARELGAtHFINSGDVNALESVQN-----SFDFILATANADLDWNAY 244
Cdd:cd08284  174 IGCGPVGLCAVLSAQVLGAArVFAVDPVPERLERAAALGA-EPINFEDAEPVERVREategrGADVVLEAVGGAAALDLA 252

                        250
                 ....*....|....*
gi 493029422 245 IAALRPKGRLHFVGV 259
Cdd:cd08284  253 FDLVRPGGVISSVGV 267
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 3-332 7.70e-18

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: 83.02  E-value: 7.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLdneWGMTD----YPFVPGHEVVGTIAALGDKVTT 76
Cdd:cd08275    1 RAVVLTGFGGldKLKVEKEALPEPSSGEVRVRVEACGLNFADLMAR---QGLYDsapkPPFVPGFECAGTVEAVGEGVKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  77 LNLGQRVglgwfsgscmtcewcmsgnhnLCsnaegtiVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNP 156
Cdd:cd08275   78 FKVGDRV---------------------MG-------LTRFGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYA 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 157 IVQF-DIKPSDRvgvigigGLGHIALGflqawGC------------EITAF-SSSPDKEAEARELGATHFINSGDVNALE 222
Cdd:cd08275  130 LFELgNLRPGQS-------VLVHSAAG-----GVglaagqlcktvpNVTVVgTASASKHEALKENGVTHVIDYRTQDYVE 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 223 SVQNS----FDFILaTANADLDWNAYIAALRPKGRL--------------HFVGVIPNPLSTP-IFP--LILGQKSISA- 280
Cdd:cd08275  198 EVKKIspegVDIVL-DALGGEDTRKSYDLLKPMGRLvvygaanlvtgekrSWFKLAKKWWNRPkVDPmkLISENKSVLGf 276

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493029422 281 --------SPVGSP--ATISQMINfaarQGV--EPITETFSFEQVNEAMEKLRHGKPRYRLVLK 332
Cdd:cd08275  277 nlgwlfeeRELLTEvmDKLLKLYE----EGKikPKIDSVFPFEEVGEAMRRLQSRKNIGKVVLT 336
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 23-143 1.88e-17

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 81.80  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDLSMLD-NEW--GMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVglgwfSGS----CMTC 95
Cdd:PRK05396  22 EPGPNDVLIKVKKTAICGTDVHIYNwDEWaqKTIPVPMVVGHEFVGEVVEVGSEVTGFKVGDRV-----SGEghivCGHC 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 493029422  96 EWCMSGNHNLCSNAEGTIVSRHGGFADKVRADYSWVVPLPDGINPATA 143
Cdd:PRK05396  97 RNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAFNVWKIPDDIPDDLA 144
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 23-333 8.69e-17

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: 79.93  E-value: 8.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDLSMLDNEWgMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVglgwfsgscmtCEWCMSGN 102
Cdd:cd08249   23 KPGPDEVLVKVKAVALNPVDWKHQDYGF-IPSYPAILGCDFAGTVVEVGSGVTRFKVGDRV-----------AGFVHGGN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 103 HNlcsnaegtiVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVIGIGGLGHI--- 179
Cdd:cd08249   91 PN---------DPRNGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAALALFQKLGLPLPPPKPSPASKGKPVliw 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 180 ---------ALGFLQAWGCEI--TAfssSPDKEAEARELGATHFI--NSGDVNA--LESVQNSFDFILATANADLDWNAY 244
Cdd:cd08249  162 ggsssvgtlAIQLAKLAGYKVitTA---SPKNFDLVKSLGADAVFdyHDPDVVEdiRAATGGKLRYALDCISTPESAQLC 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 245 IAALRPKGRLHFVGVIPNPLSTPIFplilgqKSISASPV-GSPATISQMINFAARQGVEPITETF--------------- 308
Cdd:cd08249  239 AEALGRSGGGKLVSLLPVPEETEPR------KGVKVKFVlGYTVFGEIPEDREFGEVFWKYLPELleegklkphpvrvve 312

                        330       340
                 ....*....|....*....|....*..
gi 493029422 309 -SFEQVNEAMEKLRHGKPR-YRLVLKH 333
Cdd:cd08249  313 gGLEGVQEGLDLLRKGKVSgEKLVVRL 339
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 3-333 1.01e-16

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


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 79.51  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPF--EYDPGTLGDEEVEIKVEYCGICHSD-LSMLDNEWGMTDYPFVPGHEVVGTIAALGDKvtTLNL 79
Cdd:cd05280    2 KALVVEEQDGGVSLFlrTLPLDDLPEGDVLIRVHYSSLNYKDaLAATGNGGVTRNYPHTPGIDAAGTVVSSDDP--RFRE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRV-----GLGwfsgscmtcewcmsgnhnlcsnaegtiVSRHGGFADKVRADYSWVVPLPDGINP------ATAGplFC 148
Cdd:cd05280   80 GDEVlvtgyDLG---------------------------MNTDGGFAEYVRVPADWVVPLPEGLSLreamilGTAG--FT 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 149 GGITVFnPIVQFDIKPSDrvgvig--igglghIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVN-----AL 221
Cdd:cd05280  131 AALSVH-RLEDNGQTPEDgpvlvtgatggvgsIAVAILAKLGYTVVALTGKEEQADYLKSLGASEVLDREDLLdeskkPL 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 222 ESVQnsFDFILATANADLDWNAyIAALRPKGRLHFVG-VIPNPLSTPIFPLIL-GQKSISASPVGSPATISQMI------ 293
Cdd:cd05280  210 LKAR--WAGAIDTVGGDVLANL-LKQTKYGGVVASCGnAAGPELTTTVLPFILrGVSLLGIDSVNCPMELRKQVwqklat 286

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 493029422 294 NFAARQgVEPITETFSFEQVNEAMEKLRHGKPRYRLVLKH 333
Cdd:cd05280  287 EWKPDL-LEIVVREISLEELPEAIDRLLAGKHRGRTVVKI 325
PLN02740 PLN02740
Alcohol dehydrogenase-like
 3-324 1.10e-16

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 79.84  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGgqlQPF-----EYDPGtlGDEEVEIKVEYCGICHSDLSMLDNEWGMTD-YPFVPGHEVVGTIAALGDKVTT 76
Cdd:PLN02740  12 KAAVAWGPG---EPLvmeeiRVDPP--QKMEVRIKILYTSICHTDLSAWKGENEAQRaYPRILGHEAAGIVESVGEGVED 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  77 LNLGQRVgLGWFSGSCMTCEWCMSGNHNLCS----NAEGTIVSRHGG--------------------FADKVRADYSWVV 132
Cdd:PLN02740  87 LKAGDHV-IPIFNGECGDCRYCKRDKTNLCEtyrvDPFKSVMVNDGKtrfstkgdgqpiyhflntstFTEYTVLDSACVV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 133 PlpdgINPATagP------LFCGGIT----VFNPIvqfDIKPSDRVGVIGIGglghiALGFLQAWGC------EITAFSS 196
Cdd:PLN02740 166 K----IDPNA--PlkkmslLSCGVSTgvgaAWNTA---NVQAGSSVAIFGLG-----AVGLAVAEGArargasKIIGVDI 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 197 SPDKEAEARELGATHFINSGDVN----------ALESVQNSFDfilATANADLDWNAYIAALRPKGRLHFVGVIPNPLST 266
Cdd:PLN02740 232 NPEKFEKGKEMGITDFINPKDSDkpvheriremTGGGVDYSFE---CAGNVEVLREAFLSTHDGWGLTVLLGIHPTPKML 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 267 PIFPLILGQ-KSISASPVGSPATISQMINFAAR--QGV----EPITETFSFEQVNEAMEKLRHGK 324
Cdd:PLN02740 309 PLHPMELFDgRSITGSVFGDFKGKSQLPNLAKQcmQGVvnldGFITHELPFEKINEAFQLLEDGK 373
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 3-325 5.01e-16

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


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 77.70  E-value: 5.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG-QLQPFEyDPGTLGDEEVEIKVEYCGICHSDLSMLdneWGMTD---YPFVPGHEVVGTIAALGDKVTTLN 78
Cdd:cd05278    2 KALVYLGPGKiGLEEVP-DPKIQGPHDAIVRVTATSICGSDLHIY---RGGVPgakHGMILGHEFVGEVVEVGSDVKRLK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  79 LGQRVGLGwFSGSCMTCEWCMSGNHNLCSNAEGTIVS---RHGGFADKVR---ADYSwVVPLPDGINPATAgpLFCGGI- 151
Cdd:cd05278   78 PGDRVSVP-CITFCGRCRFCRRGYHAHCENGLWGWKLgnrIDGGQAEYVRvpyADMN-LAKIPDGLPDEDA--LMLSDIl 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 152 -TVFNPIVQFDIKPSDrvgvigigglgHIAL------GFLQAWGC------EITAFSSSPDKEAEARELGATHFINSGDV 218
Cdd:cd05278  154 pTGFHGAELAGIKPGS-----------TVAVigagpvGLCAVAGArllgaaRIIAVDSNPERLDLAKEAGATDIINPKNG 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 219 NALESVQN-----SFDFILATANADLDWNAYIAALRPKGRLHFVGVIPNPLstPIFPLIL---GQKSISASPVGSPATIS 290
Cdd:cd05278  223 DIVEQILEltggrGVDCVIEAVGFEETFEQAVKVVRPGGTIANVGVYGKPD--PLPLLGEwfgKNLTFKTGLVPVRARMP 300

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 493029422 291 QMINFAARQGVEP---ITETFSFEQVNEAMEKLRHGKP 325
Cdd:cd05278  301 ELLDLIEEGKIDPsklITHRFPLDDILKAYRLFDNKPD 338
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 23-331 5.88e-16

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: 77.24  E-value: 5.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDlsmldneW--------GMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVglgwfsgscmt 94
Cdd:cd08253   24 TPGPGEVLVRVHASGVNPVD-------TyiragaypGLPPLPYVPGSDGAGVVEAVGEGVDGLKVGDRV----------- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  95 ceWCMSGNHNlcsnaegtivSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFD-IKPSDRVGVIGI 173
Cdd:cd08253   86 --WLTNLGWG----------RRQGTAAEYVVVPADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAgAKAGETVLVHGG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 174 GGLGHIALGFLQAW-GCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNS-----FDFILATAnADLDWNAYIAA 247
Cdd:cd08253  154 SGAVGHAAVQLARWaGARVIATASSAEGAELVRQAGADAVFNYRAEDLADRILAAtagqgVDVIIEVL-ANVNLAKDLDV 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 248 LRPKGRLHFVGVIPNPLSTPIFPLILgqKSISASPVG----SPATISQM---INFAARQGV--EPITETFSFEQVNEAME 318
Cdd:cd08253  233 LAPGGRIVVYGSGGLRGTIPINPLMA--KEASIRGVLlytaTPEERAAAaeaIAAGLADGAlrPVIAREYPLEEAAAAHE 310

                        330
                 ....*....|...
gi 493029422 319 KLRHGKPRYRLVL 331
Cdd:cd08253  311 AVESGGAIGKVVL 323
PRK10083 PRK10083
putative oxidoreductase; Provisional
 28-318 1.24e-15

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 76.70  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSgSCMTCEWCMSGNHNLCS 107
Cdd:PRK10083  26 EVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGERVAVDPVI-SCGHCYPCSIGKPNVCT 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 108 NAEGTIVSRHGGFADK--VRADYSWVVplPDGINPATAGPLFCGGITVfNPIVQFDIKPSDrvgVIGIGGLGHIALGFLQ 185
Cdd:PRK10083 105 SLVVLGVHRDGGFSEYavVPAKNAHRI--PDAIADQYAVMVEPFTIAA-NVTGRTGPTEQD---VALIYGAGPVGLTIVQ 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 186 A----WGceITAFSSS---PDKEAEARELGATHFINsgdvNALESVQNSFD---------FILATANADLDWNAYIAAlr 249
Cdd:PRK10083 179 VlkgvYN--VKAVIVAdriDERLALAKESGADWVIN----NAQEPLGEALEekgikptliIDAACHPSILEEAVTLAS-- 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493029422 250 PKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSpATISQMINFAARQGVEP---ITETFSFEQVNEAME 318
Cdd:PRK10083 251 PAARIVLMGFSSEPSEIVQQGITGKELSIFSSRLNA-NKFPVVIDWLSKGLIDPeklITHTFDFQHVADAIE 321
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 23-333 5.02e-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: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 75.03  E-value: 5.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  23 TLGDEEVEIKVEYCGICHSDL----------------SMLDNEWGM----TDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:cd08274   25 TPAPGEVLIRVGACGVNNTDIntregwystevdgatdSTGAGEAGWwggtLSFPRIQGADIVGRVVAVGEGVDTARIGER 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  83 VglgwfsgscmTCEWCMSGNHNLCSNAEGTIVS-RHGGFAD--KVRADYSWVV--PLPDginpATAGPLFCGGITVFNPI 157
Cdd:cd08274  105 V----------LVDPSIRDPPEDDPADIDYIGSeRDGGFAEytVVPAENAYPVnsPLSD----VELATFPCSYSTAENML 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 158 VQFDIKPSDRVGVIGIGGLGHIALgfLQ---AWGCEITAFSSsPDKEAEARELGATHFINSGDVNALESV---QNSFDFI 231
Cdd:cd08274  171 ERAGVGAGETVLVTGASGGVGSAL--VQlakRRGAIVIAVAG-AAKEEAVRALGADTVILRDAPLLADAKalgGEPVDVV 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 232 LATANADLdWNAYIAALRPKGRLHFVGVIPNPL-STPIFPLILGQKSISASPVGSPATISQMINFAARQGVEPITE-TFS 309
Cdd:cd08274  248 ADVVGGPL-FPDLLRLLRPGGRYVTAGAIAGPVvELDLRTLYLKDLTLFGSTLGTREVFRRLVRYIEEGEIRPVVAkTFP 326

                        330       340
                 ....*....|....*....|....*...
gi 493029422 310 FEQVNEA----MEKLRHGKpryrLVLKH 333
Cdd:cd08274  327 LSEIREAqaefLEKRHVGK----LVLVP 350
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 3-324 1.32e-13

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: 70.55  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDLsmLDNEwGMtdYP------FVPGHEVVGTIAALGDKV 74
Cdd:cd05276    2 KAIVIKEPGGpeVLELGEVPKPAPGPGEVLIRVAAAGVNRADL--LQRQ-GL--YPpppgasDILGLEVAGVVVAVGPGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  75 TTLNLGQRVgLGWFSGscmtcewcmsgnhnlcsnaegtivsrhGGFADKVRADYSWVVPLPDGINPATAGPL---FCggi 151
Cdd:cd05276   77 TGWKVGDRV-CALLAG---------------------------GGYAEYVVVPAGQLLPVPEGLSLVEAAALpevFF--- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 152 TVFNPIVQF-DIKPSDRVGVigigglgH--------IALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALE 222
Cdd:cd05276  126 TAWQNLFQLgGLKAGETVLI-------HggasgvgtAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTEDFAE 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 223 SVQ-----NSFDFILATANADlDWNAYIAALRPKGRLHFVGVIPNP-LSTPIFPLILGQKSISAS-----PVGSPATISQ 291
Cdd:cd05276  199 EVKeatggRGVDVILDMVGGD-YLARNLRALAPDGRLVLIGLLGGAkAELDLAPLLRKRLTLTGStlrsrSLEEKAALAA 277

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 493029422 292 MIN------FAARQGVEPITETFSFEQVNEA---MEKLRH-GK 324
Cdd:cd05276  278 AFRehvwplFASGRIRPVIDKVFPLEEAAEAhrrMESNEHiGK 320
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 3-332 1.69e-13

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 70.28  E-value: 1.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422    3 KAYAAHEPGGQLQPF--EYDPGTLGDEEVEIKVEYCGICHSD-LSMLDNEWGMTDYPFVPGHEVVGTIAA-------LGD 72
Cdd:TIGR02823   1 KALVVEKEDGKVSAQveTLDLSDLPEGDVLIKVAYSSLNYKDaLAITGKGGVVRSYPMIPGIDAAGTVVSsedprfrEGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   73 KVttLNLGQRVGlgwfsgscmtcewcmsgnhnlcsnaegtiVSRHGGFADKVRADYSWVVPLPDGINPA------TAGpl 146
Cdd:TIGR02823  81 EV--IVTGYGLG-----------------------------VSHDGGYSQYARVPADWLVPLPEGLSLReamalgTAG-- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  147 FCGGITVFNpIVQFDIKPSDRVGVIGIGG--LGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFIN----SGDVNA 220
Cdd:TIGR02823 128 FTAALSVMA-LERNGLTPEDGPVLVTGATggVGSLAVAILSKLGYEVVASTGKAEEEDYLKELGASEVIDredlSPPGKP 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  221 LESVQnsFDF--------ILATANADLDWNAYIAAlrpkgrlhfVGVIPNP-LSTPIFPLIL-GQKSISASPVGSPATI- 289
Cdd:TIGR02823 207 LEKER--WAGavdtvgghTLANVLAQLKYGGAVAA---------CGLAGGPdLPTTVLPFILrGVSLLGIDSVYCPMALr 275

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 493029422  290 -------SQMINFAarqGVEPITETFSFEQVNEAMEKLRHGKPRYRLVLK 332
Cdd:TIGR02823 276 eaawqrlATDLKPR---NLESITREITLEELPEALEQILAGQHRGRTVVD 322
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 15-318 2.97e-13

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 69.71  E-value: 2.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  15 QPFEYDpgtlgDEEVEIKVEYCGICHSDLSMLDN-EWGMTD--YPFVPGHEVVGTIAALGDKvtTLNLGQRVGLGwFSGS 91
Cdd:PRK09880  21 QEIEWN-----NNGTLVQITRGGICGSDLHYYQEgKVGNFVikAPMVLGHEVIGKIVHSDSS--GLKEGQTVAIN-PSKP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  92 CMTCEWCMSGNHNLCSNAE---GTIVSRH--GGFADKVRADYSWVVPLPDGINP---ATAGPLFCG-----------GIT 152
Cdd:PRK09880  93 CGHCKYCLSHNENQCTTMRffgSAMYFPHvdGGFTRYKVVDTAQCIPYPEKADEkvmAFAEPLAVAihaahqagdlqGKR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 153 VF----NPIvqfdikpsdrvgvigigglGHIALGFLQAWGC-EITAFSSSPDKEAEARELGATHFINSGDVNALESVQNS 227
Cdd:PRK09880 173 VFvsgvGPI-------------------GCLIVAAVKTLGAaEIVCADVSPRSLSLAREMGADKLVNPQNDDLDHYKAEK 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 228 --FDFILATANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILgqKSISAspVGSPATISQM---INFAARQGVE 302
Cdd:PRK09880 234 gyFDVSFEVSGHPSSINTCLEVTRAKGVMVQVGMGGAPPEFPMMTLIV--KEISL--KGSFRFTEEFntaVSWLANGVIN 309

                        330
                 ....*....|....*....
gi 493029422 303 P---ITETFSFEQVNEAME 318
Cdd:PRK09880 310 PlplLSAEYPFTDLEEALI 328
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-143 3.15e-13

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 69.21  E-value: 3.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWGMTDY-PFVPGHEVVGTIAALGDKVTTLNLGQRVGlgwfsgsCMTcewcmsgnhnlc 106
Cdd:cd08273   29 EVVVKVEASGVSFADVQMRRGLYPDQPPlPFTPGYDLVGRVDALGSGVTGFEVGDRVA-------ALT------------ 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 493029422 107 snaegtivsRHGGFADKVRADYSWVVPLPDGINPATA 143
Cdd:cd08273   90 ---------RVGGNAEYINLDAKYLVPVPEGVDAAEA 117
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
26-273 3.46e-13

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 69.48  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  26 DEEVEIKVEYCGICHSDLSMLDNEwGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSgSCMTCEWCMSGNHNL 105
Cdd:PRK10309  25 QDDVLVKVASSGLCGSDIPRIFKN-GAHYYPITLGHEFSGYVEAVGSGVDDLHPGDAVACVPLL-PCFTCPECLRGFYSL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 106 CSNAEGTIVSRHGGFADKVRADYSWVVPLPDG--------INPATAGP---LFCGGITVFNPIVqfdikpsdrvgvIGIG 174
Cdd:PRK10309 103 CAKYDFIGSRRDGGNAEYIVVKRKNLFALPTDmpiedgafIEPITVGLhafHLAQGCEGKNVII------------IGAG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 175 GLGHIALGFLQAWGCE-ITAFSSSPDKEAEARELGATHFINSGDVNALESVQ----NSFD-FILATANADLDWNAYIAAL 248
Cdd:PRK10309 171 TIGLLAIQCAVALGAKsVTAIDINSEKLALAKSLGAMQTFNSREMSAPQIQSvlreLRFDqLILETAGVPQTVELAIEIA 250

                        250       260
                 ....*....|....*....|....*..
gi 493029422 249 RPKGRLHFVGVIPNPLSTP--IFPLIL 273
Cdd:PRK10309 251 GPRAQLALVGTLHHDLHLTsaTFGKIL 277
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 3-316 4.33e-13

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 69.26  E-value: 4.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG-QLQPFEyDPGTLGDEEVEIKVEYCGICHSDLsmldneW---GMTDY--PFVPGHEVVGTIAALGDKVTT 76
Cdd:cd08287    2 RATVIHGPGDiRVEEVP-DPVIEEPTDAVIRVVATCVCGSDL------WpyrGVSPTraPAPIGHEFVGVVEEVGSEVTS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  77 LNLGQRVgLGWFSGSCMTCEWCMSGNHNLCSNAEGTIVSRHGGFADKVR---ADYSwVVPLPDgiNPATAGPLFCGGITV 153
Cdd:cd08287   75 VKPGDFV-IAPFAISDGTCPFCRAGFTTSCVHGGFWGAFVDGGQGEYVRvplADGT-LVKVPG--SPSDDEDLLPSLLAL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 154 -------FNPIVQFDIKPSDRVGVIGIGglghiALGFL-----QAWGCE-ITAFSSSPDKEAEARELGATHFINSGDVNA 220
Cdd:cd08287  151 sdvmgtgHHAAVSAGVRPGSTVVVVGDG-----AVGLCavlaaKRLGAErIIAMSRHEDRQALAREFGATDIVAERGEEA 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 221 LESVQNSFDFILATA-----NADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPLILGQKSISASPVGSPATISQMINF 295
Cdd:cd08287  226 VARVRELTGGVGADAvlecvGTQESMEQAIAIARPGGRVGYVGVPHGGVELDVRELFFRNVGLAGGPAPVRRYLPELLDD 305

                        330       340
                 ....*....|....*....|....
gi 493029422 296 AARQGVEP---ITETFSFEQVNEA 316
Cdd:cd08287  306 VLAGRINPgrvFDLTLPLDEVAEG 329
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 3-318 7.63e-13

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: 68.02  E-value: 7.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAAlgDKVTTLNLG 80
Cdd:cd08243    2 KAIVIEQPGGpeVLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEE--APGGTFTPG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  81 QRV-----GLGWfsgscmtcewcmsgnhnlcsnaegtivSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFN 155
Cdd:cd08243   80 QRVatamgGMGR---------------------------TFDGSYAEYTLVPNEQVYAIDSDLSWAELAALPETYYTAWG 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 156 PIVQ-FDIKPSDRVGVIGIGGLGHIA-LGFLQAWGCEITAFSSSPDKEAEARELGATH-FINSGDVNA-LESVQNSFDFI 231
Cdd:cd08243  133 SLFRsLGLQPGDTLLIRGGTSSVGLAaLKLAKALGATVTATTRSPERAALLKELGADEvVIDDGAIAEqLRAAPGGFDKV 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 232 LatanaDLDWNAYI----AALRPKGRLHFVGVIPNPLSTPIFPLIlgqKSIsASPVGSPAT-----------ISQMINFA 296
Cdd:cd08243  213 L-----ELVGTATLkdslRHLRPGGIVCMTGLLGGQWTLEDFNPM---DDI-PSGVNLTLTgsssgdvpqtpLQELFDFV 283

                        330       340
                 ....*....|....*....|....*.
gi 493029422 297 ARQGVE-PITETFSFEQVNEA---ME 318
Cdd:cd08243  284 AAGHLDiPPSKVFTFDEIVEAhayME 309
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 12-323 8.89e-13

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


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 68.07  E-value: 8.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  12 GQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGM-TDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWFSG 90
Cdd:cd05282   12 LVLELVSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSrPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRVLPLGGEG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  91 ScmtceWcmsgnhnlcsnaegtivsrhggfADKVRADYSWVVPLPDG----------INPATAGplfcGGITVFNPIVQF 160
Cdd:cd05282   92 T-----W-----------------------QEYVVAPADDLIPVPDSisdeqaamlyINPLTAW----LMLTEYLKLPPG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 161 DikpsdrvgvigigglgHI-------ALG-----FLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVN---ALESVQ 225
Cdd:cd05282  140 D----------------WViqnaansAVGrmliqLAKLLGFKTINVVRRDEQVEELKALGADEVIDSSPEDlaqRVKEAT 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 226 NS------FDFILATANADLdwnayIAALRPKGrlHFV--------GVIPNPLSTpIFPLI------LGQKSISASPVGS 285
Cdd:cd05282  204 GGagarlaLDAVGGESATRL-----ARSLRPGG--TLVnygllsgePVPFPRSVF-IFKDItvrgfwLRQWLHSATKEAK 275

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 493029422 286 PATISQMIN-FAARQGVEPITETFSFEQVNEAMEKLRHG 323
Cdd:cd05282  276 QETFAEVIKlVEAGVLTTPVGAKFPLEDFEEAVAAAEQP 314
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 3-324 3.79e-12

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. 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. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 66.48  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSD---LSMLDNEwGMtdYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:cd08300    4 KAAVAWEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDaytLSGADPE-GL--FPVILGHEGAGIVESVGEGVTSVKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRVgLGWFSGSCMTCEWCMSGNHNLCSN----------AEGTivSRhggFADK-----------------VRADYSwVV 132
Cdd:cd08300   81 GDHV-IPLYTPECGECKFCKSGKTNLCQKiratqgkglmPDGT--SR---FSCKgkpiyhfmgtstfseytVVAEIS-VA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 133 PLPDGINPATAGPLFCGGIT----VFNPIvqfDIKPSDRVGVIGIGglghiALGFLQAWGC------EITAFSSSPDKEA 202
Cdd:cd08300  154 KINPEAPLDKVCLLGCGVTTgygaVLNTA---KVEPGSTVAVFGLG-----AVGLAVIQGAkaagasRIIGIDINPDKFE 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 203 EARELGATHFINSGDVNalESVQN------------SFDfilATANADLDWNAYIAALRPKGRLHFVGVIP--NPLSTPI 268
Cdd:cd08300  226 LAKKFGATDCVNPKDHD--KPIQQvlvemtdggvdyTFE---CIGNVKVMRAALEACHKGWGTSVIIGVAAagQEISTRP 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493029422 269 FPLILGQ----------KSISASPvgspatisQMINFAARQGV---EPITETFSFEQVNEAMEKLRHGK 324
Cdd:cd08300  301 FQLVTGRvwkgtafggwKSRSQVP--------KLVEDYMKGKIkvdEFITHTMPLDEINEAFDLMHAGK 361
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 28-331 5.98e-12

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: 65.28  E-value: 5.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWGMTDYPFvpGHEVVGTIAALGDKVTTLNLGQRVglgwfsgscmtceWCMSgnhnlcs 107
Cdd:cd05195    2 EVEVEVKAAGLNFRDVLVALGLLPGDETPL--GLECSGIVTRVGSGVTGLKVGDRV-------------MGLA------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 108 naegtivsrHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF-DIKPSDRvgvigigglghI------- 179
Cdd:cd05195   60 ---------PGAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAYYALVDLaRLQKGES-----------Vlihaaag 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 180 -----ALGFLQAWGCEITAFSSSPDKEAEARELG--ATHFINSGDVNALESVQNS-----FDFILATANADLDwNAYIAA 247
Cdd:cd05195  120 gvgqaAIQLAQHLGAEVFATVGSEEKREFLRELGgpVDHIFSSRDLSFADGILRAtggrgVDVVLNSLSGELL-RASWRC 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 248 LRPKGRlhFVGV------IPNPLSTPIFplilgQKSISASPV-------GSPATISQM----INFAARQGVEPIT-ETFS 309
Cdd:cd05195  199 LAPFGR--FVEIgkrdilSNSKLGMRPF-----LRNVSFSSVdldqlarERPELLRELlrevLELLEAGVLKPLPpTVVP 271

                        330       340
                 ....*....|....*....|..
gi 493029422 310 FEQVNEAMEKLRHGKPRYRLVL 331
Cdd:cd05195  272 SASEIDAFRLMQSGKHIGKVVL 293
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 26-225 7.21e-12

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


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 65.61  E-value: 7.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  26 DEEVEIKVEYCGICHSDLSMLDNEW-------GMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVG---LGWfsgsCMTC 95
Cdd:cd08265   51 PDEILIRVKACGICGSDIHLYETDKdgyilypGLTEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTaeeMMW----CGMC 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  96 EWCMSGNHNLCSNAEGTIVSRHGGFAD--KVRADYSW----VVPLPDGINPATAG----PLFCGGITVFnpIVQFDIKPS 165
Cdd:cd08265  127 RACRSGSPNHCKNLKELGFSADGAFAEyiAVNARYAWeineLREIYSEDKAFEAGalvePTSVAYNGLF--IRGGGFRPG 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493029422 166 DRVGVIGIGGLGHIALGFLQAWGC-EITAFSSSPDKEAEARELGATHFINSGDVNALESVQ 225
Cdd:cd08265  205 AYVVVYGAGPIGLAAIALAKAAGAsKVIAFEISEERRNLAKEMGADYVFNPTKMRDCLSGE 265
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 2-224 8.19e-12

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


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 65.51  E-value: 8.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   2 IKAYAAHEPGG-QLQpfEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNE---WGMTDY------PFVPGHEVVGTIAALG 71
Cdd:cd08256    1 MRAVVCHGPQDyRLE--EVPVPRPGPGEILVKVEACGICAGDIKCYHGApsfWGDENQppyvkpPMIPGHEFVGRVVELG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  72 DKVTT--LNLGQRVglgwFSGS---CMTCEWCMSGNHNLCS--NAEGTIVSRHGGFADKVRADYSWVV-PLPDGINPATA 143
Cdd:cd08256   79 EGAEErgVKVGDRV----ISEQivpCWNCRFCNRGQYWMCQkhDLYGFQNNVNGGMAEYMRFPKEAIVhKVPDDIPPEDA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 144 ---GPLFCGGITVFNPIVQFDikpsdrvGVIGIGGLGHIALGFLQAWGC----EITAFSSSPDKEAEARELGATHFINSG 216
Cdd:cd08256  155 iliEPLACALHAVDRANIKFD-------DVVVLAGAGPLGLGMIGAARLknpkKLIVLDLKDERLALARKFGADVVLNPP 227


                 ....*...
gi 493029422 217 DVNALESV 224
Cdd:cd08256  228 EVDVVEKI 235
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 28-324 8.26e-12

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


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 65.41  E-value: 8.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWGMTdYPFVPGHEVVGTIAALGDKVTTLNLGQRVgLGWFSGSCMTCEWCMSGNHNLC- 106
Cdd:cd08299   34 EVRIKIVATGICRSDDHVVSGKLVTP-FPVILGHEAAGIVESVGEGVTTVKPGDKV-IPLFVPQCGKCRACLNPESNLCl 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 107 ----SNAEGTIVSRHGGFADKVRADYSW----------VVplpDGINPA---TAGPLF------CGGITVFNPIVQF-DI 162
Cdd:cd08299  112 kndlGKPQGLMQDGTSRFTCKGKPIHHFlgtstfseytVV---DEIAVAkidAAAPLEkvcligCGFSTGYGAAVNTaKV 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 163 KPSDRVGVIGIGglghiALGFLQAWGCE------ITAFSSSPDKEAEARELGATHFINSGDVN----------ALESVQN 226
Cdd:cd08299  189 TPGSTCAVFGLG-----GVGLSAIMGCKaagasrIIAVDINKDKFAKAKELGATECINPQDYKkpiqevltemTDGGVDF 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 227 SFDFIlatANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFP--LILGqKSISASPVG---SPATISQMI-NFAARQ- 299
Cdd:cd08299  264 SFEVI---GRLDTMKAALASCHEGYGVSVIVGVPPSSQNLSINPmlLLTG-RTWKGAVFGgwkSKDSVPKLVaDYMAKKf 339

                        330       340
                 ....*....|....*....|....*.
gi 493029422 300 GVEP-ITETFSFEQVNEAMEKLRHGK 324
Cdd:cd08299  340 NLDPlITHTLPFEKINEGFDLLRSGK 365
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 3-324 3.25e-11

Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 63.47  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQL--QPFEYDPGTLGdeEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLG 80
Cdd:cd08301    4 KAAVAWEAGKPLviEEVEVAPPQAM--EVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  81 QRVgLGWFSGSCMTCEWCMSGNHNLCS---NAEGTIVSRHGG---FADKVRADYSWV------------VPLPDGINPAT 142
Cdd:cd08301   82 DHV-LPVFTGECKECRHCKSEKSNMCDllrINTDRGVMINDGksrFSINGKPIYHFVgtstfseytvvhVGCVAKINPEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 143 ----AGPLFCGGITVFNPIVQF-DIKPSDRVGvigigglghI----ALGFLQAWGCEITAFSS------SPDKEAEAREL 207
Cdd:cd08301  161 pldkVCLLSCGVSTGLGAAWNVaKVKKGSTVA---------IfglgAVGLAVAEGARIRGASRiigvdlNPSKFEQAKKF 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 208 GATHFINSGDVNalESVQN------------SFDfilATANADLDWNAYIAALRPKGRLHFVGVIPNPLSTPIFPL-ILG 274
Cdd:cd08301  232 GVTEFVNPKDHD--KPVQEviaemtgggvdySFE---CTGNIDAMISAFECVHDGWGVTVLLGVPHKDAVFSTHPMnLLN 306

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493029422 275 QKSISASPVGSPATISQMINFAARQ-----GVEP-ITETFSFEQVNEAMEKLRHGK 324
Cdd:cd08301  307 GRTLKGTLFGGYKPKTDLPNLVEKYmkkelELEKfITHELPFSEINKAFDLLLKGE 362
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 20-143 4.83e-11

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


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 63.10  E-value: 4.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  20 DPgTLGDEEVEIKVEYCGICHSDLS-------MLDNEWGMTDY----PFVPGHEVVGTIAALG-DKVTTLNLGQRVglgw 87
Cdd:cd08262   18 DP-EPGPGQVLVKVLACGICGSDLHatahpeaMVDDAGGPSLMdlgaDIVLGHEFCGEVVDYGpGTERKLKVGTRV---- 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  88 fSG----SCMTCEWCMSGNHNlcsnaeGTIvsrhGGFADKVRADYSWVVPLPDGINPATA 143
Cdd:cd08262   93 -TSlpllLCGQGASCGIGLSP------EAP----GGYAEYMLLSEALLLRVPDGLSMEDA 141
PLN02827 PLN02827
Alcohol dehydrogenase-like
 3-106 6.50e-11

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 62.61  E-value: 6.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEwgmTDYPFVPGHEVVGTIAALGDKVTTLNLGQR 82
Cdd:PLN02827  14 RAAVAWGAGEALVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWESQ---ALFPRIFGHEASGIVESIGEGVTEFEKGDH 90

                         90       100
                 ....*....|....*....|....
gi 493029422  83 VgLGWFSGSCMTCEWCMSGNHNLC 106
Cdd:PLN02827  91 V-LTVFTGECGSCRHCISGKSNMC 113
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 13-138 1.13e-10

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 62.10  E-value: 1.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  13 QLQPFEYDPgtLGDEEVEIKVEYCGICHSDLSMLdNEWGMTDY----PFVPGHEVVGTIAALGDKVTTLNLGQRVGLGwf 88
Cdd:PLN02702  30 KIQPFKLPP--LGPHDVRVRMKAVGICGSDVHYL-KTMRCADFvvkePMVIGHECAGIIEEVGSEVKHLVVGDRVALE-- 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493029422  89 SG-SCMTCEWCMSGNHNLCSNAE--GTiVSRHGGFADKVRADYSWVVPLPDGI 138
Cdd:PLN02702 105 PGiSCWRCNLCKEGRYNLCPEMKffAT-PPVHGSLANQVVHPADLCFKLPENV 156
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 22-226 1.27e-10

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: 61.29  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  22 GTLGDEEVEIKVEYCGICHSDLSMLDNEW-GMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLgwFSGSCMtcewcms 100
Cdd:cd08251    3 APPGPGEVRIQVRAFSLNFGDLLCVRGLYpTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIA--GTGESM------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 101 gnhnlcsnaegtivsrhGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVIGIGGLGH-I 179
Cdd:cd08251   74 -----------------GGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAGLAKGEHILIQTATGGTGlM 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 493029422 180 ALGFLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQN 226
Cdd:cd08251  137 AVQLARLKGAEIYATASSDDKLEYLKQLGVPHVINYVEEDFEEEIMR 183
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 31-224 8.73e-10

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


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 59.19  E-value: 8.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  31 IKVEYCGICHSDLSMLDNewgmtDYPFVP-----GHEVVGTIAALGDKVTTLNLGQRVGLGWFSgSCMTCEWCMSGNHNL 105
Cdd:cd08286   30 VKMLKTTICGTDLHILKG-----DVPTVTpgrilGHEGVGVVEEVGSAVTNFKVGDRVLISCIS-SCGTCGYCRKGLYSH 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 106 CSNAeGTIVSRH--GGFADKVR---ADYSwVVPLPDGINPATAgpLFCGGI--TVFNPIVQF-DIKPSDRVGVIGIGGlg 177
Cdd:cd08286  104 CESG-GWILGNLidGTQAEYVRiphADNS-LYKLPEGVDEEAA--VMLSDIlpTGYECGVLNgKVKPGDTVAIVGAGP-- 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493029422 178 hIALGFLqawgceITAFSSSPDKE----------AEARELGATHFINSGDVNALESV 224
Cdd:cd08286  178 -VGLAAL------LTAQLYSPSKIimvdlddnrlEVAKKLGATHTVNSAKGDAIEQV 227
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 56-327 3.22e-09

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


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 56.90  E-value: 3.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  56 PFVPGHEVVGTIAALGDKVTTLNLGQRVglgwfsgscmtcewCMSGNHnlcsnaegtivsrhggfADKVRADYSWVVPLP 135
Cdd:cd08255   21 PLPPGYSSVGRVVEVGSGVTGFKPGDRV--------------FCFGPH-----------------AERVVVPANLLVPLP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 136 DGINPATA--GPLfcgGITVFNPIVQFDIKPSDRVGVIGIGGLGHIALGFLQAWGC-EITAFSSSPDKEAEARELGATHF 212
Cdd:cd08255   70 DGLPPERAalTAL---AATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGArEVVGVDPDAARRELAEALGPADP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 213 INSGDvnALESVQNSFDFILATANADLDWNAYIAALRPKGRLHFVGvipnplSTPIFPLILGQ------KSISASPVGSP 286
Cdd:cd08255  147 VAADT--ADEIGGRGADVVIEASGSPSALETALRLLRDRGRVVLVG------WYGLKPLLLGEefhfkrLPIRSSQVYGI 218

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493029422 287 A------TISQMINFA------ARQGVEP-ITETFSFEQVNEAMEKLRHGKPRY 327
Cdd:cd08255  219 GrydrprRWTEARNLEealdllAEGRLEAlITHRVPFEDAPEAYRLLFEDPPEC 272
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 21-326 1.45e-08

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


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 55.32  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  21 PGTLGDEEVEIKVeyCG------------ICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGWF 88
Cdd:cd08285    9 IGKVGWIEKPIPV--CGpndaivrptavaPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGDRVIVPAI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  89 SgSCMTCEWCMSGNHNLCSNAEGTIvsRHGGFADKVRADYSWV-------VPLPDGINPATAGPL-------FCG----G 150
Cdd:cd08285   87 T-PDWRSVAAQRGYPSQSGGMLGGW--KFSNFKDGVFAEYFHVndadanlAPLPDGLTDEQAVMLpdmmstgFHGaelaN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 151 ITVFNPIVQFDIKPsdrvgvigigglghiaLGFLQAWGCE------ITAFSSSPDKEAEARELGATHFINSGDVNALESV 224
Cdd:cd08285  164 IKLGDTVAVFGIGP----------------VGLMAVAGARlrgagrIIAVGSRPNRVELAKEYGATDIVDYKNGDVVEQI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 225 QNSFD------FILATANADLdWNAYIAALRPKGRLHFVGVIPNPLSTPIfPLI-----LGQKSISAS--PVGSpATISQ 291
Cdd:cd08285  228 LKLTGgkgvdaVIIAGGGQDT-FEQALKVLKPGGTISNVNYYGEDDYLPI-PREewgvgMGHKTINGGlcPGGR-LRMER 304

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 493029422 292 MINFAARQGVEP----ITETFSFEQVNEAMEkLRHGKPR 326
Cdd:cd08285  305 LASLIEYGRVDPskllTHHFFGFDDIEEALM-LMKDKPD 342
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
 2-330 3.19e-08

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


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 54.08  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   2 IKAYAAHEPGGQLQP--FEYDPGTLGDEEVEIKVEYcgichSDLSMLDnewGMT---------DYPFVPGHEVVGTIA-- 68
Cdd:cd08288    1 FKALVLEKDDGGTSAelRELDESDLPEGDVTVEVHY-----STLNYKD---GLAitgkggivrTFPLVPGIDLAGTVVes 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  69 -----ALGDKVTtLNlGQRVGlgwfsgscmtcewcmsgnhnlcsnaegtiVSRHGGFADKVRADYSWVVPLPDGINPATA 143
Cdd:cd08288   73 ssprfKPGDRVV-LT-GWGVG-----------------------------ERHWGGYAQRARVKADWLVPLPEGLSARQA 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 144 GPLFCGGITVF---NPIVQFDIKPSDRVGVIGIGG--LGHIALGFLQAWGCEITAFSSSPDKEAEARELGATHFIN---- 214
Cdd:cd08288  122 MAIGTAGFTAMlcvMALEDHGVTPGDGPVLVTGAAggVGSVAVALLARLGYEVVASTGRPEEADYLRSLGASEIIDrael 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 215 SGDVNALES------VQNSFDFILATANADLDWNAYIAAlrpkgrlhfVGVIPNP-LSTPIFPLIL-GQKSISASPVGSP 286
Cdd:cd08288  202 SEPGRPLQKerwagaVDTVGGHTLANVLAQTRYGGAVAA---------CGLAGGAdLPTTVMPFILrGVTLLGIDSVMAP 272

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 493029422 287 --------ATISQMINFAArqgVEPITETFSFEQVNEAMEKLRHGKPRYRLV 330
Cdd:cd08288  273 ierrraawARLARDLDPAL---LEALTREIPLADVPDAAEAILAGQVRGRVV 321
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 7-209 5.18e-08

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


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 53.53  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   7 AHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDlSMLDNEWG----MTDYPFVPGHEVVGTIAALGDKVTTLNLG 80
Cdd:cd08244    6 LHEFGPpeVLVPEDVPDPVPGPGQVRIAVAAAGVHFVD-TQLRSGWGpgpfPPELPYVPGGEVAGVVDAVGPGVDPAWLG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  81 QRVglgwfsgscmtcewcmsgnhnlcsnaEGTIVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF 160
Cdd:cd08244   85 RRV--------------------------VAHTGRAGGGYAELAVADVDSLHPVPDGLDLEAAVAVVHDGRTALGLLDLA 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493029422 161 DIKPSDRVGVIGIGGlghiALGFL-----QAWGCEITAFSSSPDKEAEARELGA 209
Cdd:cd08244  139 TLTPGDVVLVTAAAG----GLGSLlvqlaKAAGATVVGAAGGPAKTALVRALGA 188
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
 24-152 6.55e-08

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 53.49  E-value: 6.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  24 LGDEEVEIKVEYCGICHSD-LSMLDNEWGMTDYPFVPGHEVVGTIA-------ALGDKV--TTLNLGqrvglgwfsgscm 93
Cdd:cd08289   25 LPEGDVLIRVAYSSVNYKDgLASIPGGKIVKRYPFIPGIDLAGTVVesndprfKPGDEVivTSYDLG------------- 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 493029422  94 tcewcmsgnhnlcsnaegtiVSRHGGFADKVRADYSWVVPLPDGINPATAGPLFCGGIT 152
Cdd:cd08289   92 --------------------VSHHGGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFT 130
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 20-143 7.53e-08

2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 52.99  E-value: 7.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  20 DPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTD-YPFVPGHEVVGTIAALGDK-VTTLNLGQRVglgwfsgSCMTCEW 97
Cdd:cd08291   24 EVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKaLPVPPGFEGSGTVVAAGGGpLAQSLIGKRV-------AFLAGSY 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493029422  98 cmsgnhnlcsnaegtivsrhGGFADKVRADYSWVVPLPDG----------INPATA 143
Cdd:cd08291   97 --------------------GTYAEYAVADAQQCLPLPDGvsfeqgassfVNPLTA 132
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 20-138 1.03e-07

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 52.92  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  20 DPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLGwFSGSCMTCEWCM 99
Cdd:cd08283   19 DPKIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGDRVVVP-FTIACGECFYCK 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493029422 100 SGNHNLCSNA------EGTIVSRHGGF--------------ADKVR---ADYSwVVPLPDGI 138
Cdd:cd08283   98 RGLYSQCDNTnpsaemAKLYGHAGAGIfgyshltggyaggqAEYVRvpfADVG-PFKIPDDL 158
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 31-217 1.08e-06

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 49.31  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422    31 IKVEYCGICHSD--LSMldnewGMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVgLGWFSGScmtcewcmsgnhnlcsn 108
Cdd:smart00829   1 IEVRAAGLNFRDvlIAL-----GLYPGEAVLGGECAGVVTRVGPGVTGLAVGDRV-MGLAPGA----------------- 57

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   109 aegtivsrhggFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQF-DIKPSDRvgvigigglghI-------- 179
Cdd:smart00829  58 -----------FATRVVTDARLVVPIPDGWSFEEAATVPVVFLTAYYALVDLaRLRPGES-----------Vlihaaagg 115

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 493029422   180 ----ALGFLQAWGCEITAFSSSPDKEAEARELG--ATHFINSGD 217
Cdd:smart00829 116 vgqaAIQLARHLGAEVFATAGSPEKRDFLRALGipDDHIFSSRD 159
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 6-143 4.28e-06

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


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 47.71  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   6 AAHEPGGQ----LQPFEYDPGTLGDEEVEIKVEYCGICHSDLsmldneWGMT-DYPFVP------GHEVVGTIAALGDKV 74
Cdd:cd08292    4 AVHTQFGDpadvLEIGEVPKPTPGAGEVLVRTTLSPIHNHDL------WTIRgTYGYKPelpaigGSEAVGVVDAVGEGV 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493029422  75 TTLNLGQRVglgwfsgscmtcewcmsgnhnlcsnaegTIVSRHGGFADKVRADYSWVVPLPDGI----------NPATA 143
Cdd:cd08292   78 KGLQVGQRV----------------------------AVAPVHGTWAEYFVAPADGLVPLPDGIsdevaaqliaMPLSA 128
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 3-279 5.02e-06

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: 47.52  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGGQLQP-----FEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTL 77
Cdd:cd08252    2 KAIGFTQPLPITDPdslidIELPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVTLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  78 NLGQRVglgWFSGScMTcewcMSGnhnlcSNAEGTIVsrhggfadkvraDYSWVVPLPDGINPATAGPLFCGGITVFNPI 157
Cdd:cd08252   82 KVGDEV---YYAGD-IT----RPG-----SNAEYQLV------------DERIVGHKPKSLSFAEAAALPLTSLTAWEAL 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 158 VqfdikpsDRVGVIGIGGLGH--------------IALGFLQAWGC-EITAFSSSPDKEAEARELGATHFINSGD----- 217
Cdd:cd08252  137 F-------DRLGISEDAENEGktlliiggaggvgsIAIQLAKQLTGlTVIATASRPESIAWVKELGADHVINHHQdlaeq 209

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 218 VNALESVQnsFDFILATANADLDWNAYIAALRPKGRlhfVGVIPNPLStpifPLILG---QKSIS 279
Cdd:cd08252  210 LEALGIEP--VDYIFCLTDTDQHWDAMAELIAPQGH---ICLIVDPQE----PLDLGplkSKSAS 265
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 188-256 1.40e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 42.82  E-value: 1.40e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493029422 188 GCEITAFSSSPDKEAEARELGATHFINSGDVNALESVQNSFDfiLATANADLDW-NAYIAAL-------RPKGRLHF 256
Cdd:PRK10258  64 GSQVTALDLSPPMLAQARQKDAADHYLAGDIESLPLATATFD--LAWSNLAVQWcGNLSTALrelyrvvRPGGVVAF 138
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
207-331 1.51e-04

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 41.16  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  207 LGATHFINSGDVNALESVQ-NSFDFILATANADLdWNAYIAALRPKGRlhFVGVIPNPLSTPIFPLILGQKS-------I 278
Cdd:pfam13602   1 LGADEVIDYRTTDFVQATGgEGVDVVLDTVGGEA-FEASLRVLPGGGR--LVTIGGPPLSAGLLLPARKRGGrgvkylfL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 493029422  279 SASPVGSPATISQMINFAARQGVEP-ITETFSFEQVNEAMEKLRHGKPRYRLVL 331
Cdd:pfam13602  78 FVRPNLGADILQELADLIEEGKLRPvIDRVFPLEEAAEAHRYLESGRARGKIVL 131
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 25-332 2.90e-04

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: 42.24  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  25 GDEEVEIKVEYCGICHSDLSMLDNEW-GMTDYPFVPGHEVVGTIAALGDKVTTLNLGQRVGLgwfsgscmtcewcMSGnh 103
Cdd:cd08250   29 GPGEVLVKNRFVGINASDINFTAGRYdPGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVAT-------------MSF-- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 104 nlcsnaegtivsrhGGFADKVRADYSWVVPLPDgINPATAgPLFCGGITVFNPIVQF-DIKPSDRVGVIGIGGLG-HIAL 181
Cdd:cd08250   94 --------------GAFAEYQVVPARHAVPVPE-LKPEVL-PLLVSGLTASIALEEVgEMKSGETVLVTAAAGGTgQFAV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 182 GFLQAWGCEITAFSSSPDKEAEARELGATHFIN--SGDVNAL--ESVQNSFDFILATANADLdWNAYIAALRPKGRLHFV 257
Cdd:cd08250  158 QLAKLAGCHVIGTCSSDEKAEFLKSLGCDRPINykTEDLGEVlkKEYPKGVDVVYESVGGEM-FDTCVDNLALKGRLIVI 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 258 GVI--------PNPLSTPIFPLILGQKsiSASPVG---------SPATISQMINFAAR----QGVEPiTETFSFEQVNEA 316
Cdd:cd08250  237 GFIsgyqsgtgPSPVKGATLPPKLLAK--SASVRGfflphyaklIPQHLDRLLQLYQRgklvCEVDP-TRFRGLESVADA 313

                        330
                 ....*....|....*.
gi 493029422 317 MEKLRHGKPRYRLVLK 332
Cdd:cd08250  314 VDYLYSGKNIGKVVVE 329
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 3-214 2.95e-04

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 42.16  E-value: 2.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   3 KAYAAHEPGG--QLQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNE-WGMTDYPFVPGHEVVGTIAALGDKVTTLNL 79
Cdd:cd08272    2 KALVLESFGGpeVFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGaAARPPLPAILGCDVAGVVEAVGEGVTRFRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  80 GQRVglgwfsgscmtceWCMSGnhnlcsnaegtIVSRHGG-FADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIV 158
Cdd:cd08272   82 GDEV-------------YGCAG-----------GLGGLQGsLAEYAVVDARLLALKPANLSMREAAALPLVGITAWEGLV 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 159 qfdikpsDRVGVIGIGGLG---------HIALGFLQAWGCEITAfSSSPDKEAEARELGATHFIN 214
Cdd:cd08272  138 -------DRAAVQAGQTVLihggaggvgHVAVQLAKAAGARVYA-TASSEKAAFARSLGADPIIY 194
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 28-138 4.18e-04

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. 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-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 41.82  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  28 EVEIKVEYCGICHSDLSMLDNEWGM----TDYpFVPGHEVVGTIAALGDKvTTLNLGQRVgLGWFSGSCMTCEWCMSGNH 103
Cdd:cd08230   27 EVLVRTLEVGVCGTDREIVAGEYGTappgEDF-LVLGHEALGVVEEVGDG-SGLSPGDLV-VPTVRRPPGKCLNCRIGRP 103

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 493029422 104 NLCSNAEGT---IVSRHGGFADKVRADYSWVVPLPDGI 138
Cdd:cd08230  104 DFCETGEYTergIKGLHGFMREYFVDDPEYLVKVPPSL 141
PRK10754 PRK10754
NADPH:quinone reductase;
1-224 2.41e-03

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 39.33  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422   1 MIKAYAAHEPGGQ--LQPFEYDPGTLGDEEVEIKVEYCGICHSDLSMLDNEWGMTDYPFVPGHEVVGTIAALGDKVTTLN 78
Cdd:PRK10754   1 MAKRIEFHKHGGPevLQAVEFTPADPAENEVQVENKAIGINYIDTYIRSGLYPPPSLPSGLGTEAAGVVSKVGSGVKHIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  79 LGQRVGLgwfsgscmtcewcmsgnhnlCSNAEGTIVSRHGGFADKVradyswvVPLPDGINPATAGPLFCGGITVFNPIV 158
Cdd:PRK10754  81 VGDRVVY--------------------AQSALGAYSSVHNVPADKA-------AILPDAISFEQAAASFLKGLTVYYLLR 133

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 159 Q-FDIKPSDrvgvigiGGLGHIALG--------FLQAWGCEITAFSSSPDKEAEARELGATHFINSGDVNALESV 224
Cdd:PRK10754 134 KtYEIKPDE-------QFLFHAAAGgvgliacqWAKALGAKLIGTVGSAQKAQRAKKAGAWQVINYREENIVERV 201
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 118-331 3.40e-03

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 38.89  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 118 GGFADKVRADYSWVVPLPDGINPATAGPLFCGGITVFNPIVQFDIKPSDRVGVI-GIGGLGHIALGFLQAWGCEITAFSS 196
Cdd:cd08270   86 GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALRRGGPLLGRRVLVTgASGGVGRFAVQLAALAGAHVVAVVG 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 197 SPDKEAEARELGATHFInsgdVNALESVQNSFDFILATANADLdWNAYIAALRPKGRLHFVGVIPNPLSTpiFPL----- 271
Cdd:cd08270  166 SPARAEGLRELGAAEVV----VGGSELSGAPVDLVVDSVGGPQ-LARALELLAPGGTVVSVGSSSGEPAV--FNPaafvg 238

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493029422 272 ILGQKSIS--ASPVGSPAT--ISQMINFAARQGVEP-ITETFSFEQVNEAMEKLRHGKPRYRLVL 331
Cdd:cd08270  239 GGGGRRLYtfFLYDGEPLAadLARLLGLVAAGRLDPrIGWRGSWTEIDEAAEALLARRFRGKAVL 303
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 183-262 7.53e-03

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 36.15  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422 183 FLQAWGCEITAFSSSPDKEAEARELGAT---HFINsGDVNALESVQNSFDFILAT------ANADLDWNAYIAALRPKGR 253
Cdd:COG2227   41 ALARRGADVTGVDISPEALEIARERAAElnvDFVQ-GDLEDLPLEDGSFDLVICSevlehlPDPAALLRELARLLKPGGL 119


                 ....*....
gi 493029422 254 LHFvgVIPN 262
Cdd:COG2227  120 LLL--STPN 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 178-252 9.76e-03

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 35.23  E-value: 9.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493029422  178 HIALGFLQAWGCEITAFSSSPDKEAEARELGATHFINS----GDVNALESVQNSFDFILATA----NADLDWNAYIA--- 246
Cdd:pfam13649  10 RLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVefvqGDAEDLPFPDGSFDLVVSSGvlhhLPDPDLEAALReia 89


                  ....*..
gi 493029422  247 -ALRPKG 252
Cdd:pfam13649  90 rVLKPGG 96
 
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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