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Conserved domains on  [gi|1543036938|ref|WP_125946942|]
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MULTISPECIES: L-idonate 5-dehydrogenase [unclassified Variovorax]

Protein Classification

L-idonate 5-dehydrogenase( domain architecture ID 10169506)

L-idonate 5-dehydrogenase catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 8-347 0e+00

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: 504.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08232     1 CVIHAAGDLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYQHGGFGTVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd08232    81 VAVNPSRPCGTCDYCRAGRPNLCLNMRFLGSAMRFPHVQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKtwVARHSADKGTFDVMLEC 247
Cdd:cd08232   161 AGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADETVNLARDP--LAAYAADKGDFDVVFEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNERALRDGLEVMRPRGVVVQLG-LGGDVSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVVSHTFPMLQ 326
Cdd:cd08232   239 SGAPAALASALRVVRPGGTVVQVGmLGGPVPLPLNALVAKELDLRGSFRFDDEFAEAVRLLAAGRIDVRPLITAVFPLEE 318

                         330       340
                  ....*....|....*....|.
gi 1543036938 327 ARQAFELASDRQKAMKVLIDF 347
Cdd:cd08232   319 AAEAFALAADRTRSVKVQLSF 339
 
Name Accession Description Interval E-value
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 8-347 0e+00

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: 504.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08232     1 CVIHAAGDLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYQHGGFGTVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd08232    81 VAVNPSRPCGTCDYCRAGRPNLCLNMRFLGSAMRFPHVQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKtwVARHSADKGTFDVMLEC 247
Cdd:cd08232   161 AGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADETVNLARDP--LAAYAADKGDFDVVFEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNERALRDGLEVMRPRGVVVQLG-LGGDVSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVVSHTFPMLQ 326
Cdd:cd08232   239 SGAPAALASALRVVRPGGTVVQVGmLGGPVPLPLNALVAKELDLRGSFRFDDEFAEAVRLLAAGRIDVRPLITAVFPLEE 318

                         330       340
                  ....*....|....*....|.
gi 1543036938 327 ARQAFELASDRQKAMKVLIDF 347
Cdd:cd08232   319 AAEAFALAADRTRSVKVQLSF 339
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 8-348 1.18e-118

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: 346.74  E-value: 1.18e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFgtvRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:COG1063     4 LVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYP---FVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:COG1063    81 VVVEPNIPCGECRYCRRGRYNLCENLQFLGI----AGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVER 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQD--KTWVARHSADKGtFDVML 245
Cdd:COG1063   157 AGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPREEdlVEAVRELTGGRG-ADVVI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 246 ECSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVDLSPVVSHTFP 323
Cdd:COG1063   236 EAVGAPAALEQALDLVRPGGTVVLVGVpGGPVPIDLNALVRKELTLRGSRNYtREDFPEALELLASGRIDLEPLITHRFP 315

                         330       340
                  ....*....|....*....|....*.
gi 1543036938 324 MLQARQAFELASDRQ-KAMKVLIDFT 348
Cdd:COG1063   316 LDDAPEAFEAAADRAdGAIKVVLDPD 341
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 1-347 1.99e-115

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 338.58  E-value: 1.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   1 MRLRCMCLVIHAPDDLRLDEQDAgEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAV-APGV 79
Cdd:PRK09880    1 MQVKTQSCVVAGKKDVAVTEQEI-EWNNNGTLVQITRGGICGSDLHYYQEGKVGNFVIKAPMVLGHEVIGKIVHSdSSGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  80 esvRIGDKVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFS 159
Cdd:PRK09880   80 ---KEGQTVAINPSKPCGHCKYCLSHNENQCTTMRFFGSAMYFPHVDGGFTRYKVVDTAQCIPYPEKADEKVMAFAEPLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 160 VGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKtwVARHSADKG 239
Cdd:PRK09880  157 VAIHAAHQAGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQNDD--LDHYKAEKG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 240 TFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGGD-VSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVV 318
Cdd:PRK09880  235 YFDVSFEVSGHPSSINTCLEVTRAKGVMVQVGMGGApPEFPMMTLIVKEISLKGSFRFTEEFNTAVSWLANGVINPLPLL 314

                         330       340
                  ....*....|....*....|....*....
gi 1543036938 319 SHTFPMLQARQAFELASDRQKAMKVLIDF 347
Cdd:PRK09880  315 SAEYPFTDLEEALIFAGDKTQAAKVQLVF 343
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
 18-345 6.76e-57

L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results.E. coli His-90 modulates substrate specificity and is believed part of the active site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 188.53  E-value: 6.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  18 LDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCG 97
Cdd:TIGR00692  13 LTEVPVPEPGPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVGDYVSVETHIVCG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  98 ACKFCLEGLPNQCLDMRFYGsaMRTPhvqGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVsRAGPLLGKRVL 177
Cdd:TIGR00692  93 KCYACRRGQYHVCQNTKIFG--VDTD---GCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTV-LAGPISGKSVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 178 VSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVA-QDKTWVARHSADKGTFDVMLECSGNERALRD 256
Cdd:TIGR00692 167 VTGAGPIGLMAIAVAKASGAYPVIVSDPNEYRLELAKKMGATYVVNPFkEDVVKEVADLTDGEGVDVFLEMSGAPKALEQ 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 257 GLEVMRPRGVVVQLGL-GGDVSIP-QNMVVAKELSICGSFRFH--AEFALAVKLINEGRVDLSPVVSHTFPMLQARQAFE 332
Cdd:TIGR00692 247 GLQAVTPGGRVSLLGLpPGKVTIDfTNKVIFKGLTIYGITGRHmfETWYTVSRLIQSGKLDLDPIITHKFKFDKFEKGFE 326

                         330
                  ....*....|...
gi 1543036938 333 LASDRQKAMKVLI 345
Cdd:TIGR00692 327 LMRSGQTGKVILS 339
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 29-142 2.02e-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: 130.04  E-value: 2.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  29 GQVLVKVGMGGICGSDLHYFhNGGFGTVriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGLPN 108
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIY-KGGNPPV--KLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1543036938 109 QCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVK 142
Cdd:pfam08240  78 LCPNGRFLGY-----DRDGGFAEYVVVPERNLVP 106
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 57-345 1.23e-07

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 52.39  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   57 RIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAvnpsrpcgackfcleGLpnqcldmrfygsamrtphVQGAFRNMLLCE 136
Cdd:smart00829  19 LYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVM---------------GL------------------APGAFATRVVTD 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  137 ATQCVKVADHVPLRLAAlaepfSV---------GLHGVSRAGPllGKRVLV-SGCGPIGvlaiaaarahgaaeITAtdvv 206
Cdd:smart00829  66 ARLVVPIPDGWSFEEAA-----TVpvvfltayyALVDLARLRP--GESVLIhAAAGGVG--------------QAA---- 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  207 depLAIARAMGAD--------------NTINVAQD----------KTWVARHSADKGtFDVMLECSGNErALRDGLEVMR 262
Cdd:smart00829 121 ---IQLARHLGAEvfatagspekrdflRALGIPDDhifssrdlsfADEILRATGGRG-VDVVLNSLSGE-FLDASLRCLA 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  263 PRGVVVQLGLgGDVSIPQNMVVAKELSiCGSF-------------RFHAEFALAVKLINEGRvdLSPVVSHTFPMLQARQ 329
Cdd:smart00829 196 PGGRFVEIGK-RDIRDNSQLAMAPFRP-NVSYhavdldaleegpdRIRELLAEVLELFAEGV--LRPLPVTVFPISDAED 271

                          330
                   ....*....|....*.
gi 1543036938  330 AFELASDRQKAMKVLI 345
Cdd:smart00829 272 AFRYMQQGKHIGKVVL 287
 
Name Accession Description Interval E-value
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 8-347 0e+00

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: 504.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08232     1 CVIHAAGDLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYQHGGFGTVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd08232    81 VAVNPSRPCGTCDYCRAGRPNLCLNMRFLGSAMRFPHVQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKtwVARHSADKGTFDVMLEC 247
Cdd:cd08232   161 AGDLAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADETVNLARDP--LAAYAADKGDFDVVFEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNERALRDGLEVMRPRGVVVQLG-LGGDVSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVVSHTFPMLQ 326
Cdd:cd08232   239 SGAPAALASALRVVRPGGTVVQVGmLGGPVPLPLNALVAKELDLRGSFRFDDEFAEAVRLLAAGRIDVRPLITAVFPLEE 318

                         330       340
                  ....*....|....*....|.
gi 1543036938 327 ARQAFELASDRQKAMKVLIDF 347
Cdd:cd08232   319 AAEAFALAADRTRSVKVQLSF 339
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 8-348 1.18e-118

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: 346.74  E-value: 1.18e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFgtvRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:COG1063     4 LVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYP---FVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:COG1063    81 VVVEPNIPCGECRYCRRGRYNLCENLQFLGI----AGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVER 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQD--KTWVARHSADKGtFDVML 245
Cdd:COG1063   157 AGVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPREEdlVEAVRELTGGRG-ADVVI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 246 ECSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVDLSPVVSHTFP 323
Cdd:COG1063   236 EAVGAPAALEQALDLVRPGGTVVLVGVpGGPVPIDLNALVRKELTLRGSRNYtREDFPEALELLASGRIDLEPLITHRFP 315

                         330       340
                  ....*....|....*....|....*.
gi 1543036938 324 MLQARQAFELASDRQ-KAMKVLIDFT 348
Cdd:COG1063   316 LDDAPEAFEAAADRAdGAIKVVLDPD 341
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 1-347 1.99e-115

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 338.58  E-value: 1.99e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   1 MRLRCMCLVIHAPDDLRLDEQDAgEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAV-APGV 79
Cdd:PRK09880    1 MQVKTQSCVVAGKKDVAVTEQEI-EWNNNGTLVQITRGGICGSDLHYYQEGKVGNFVIKAPMVLGHEVIGKIVHSdSSGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  80 esvRIGDKVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFS 159
Cdd:PRK09880   80 ---KEGQTVAINPSKPCGHCKYCLSHNENQCTTMRFFGSAMYFPHVDGGFTRYKVVDTAQCIPYPEKADEKVMAFAEPLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 160 VGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKtwVARHSADKG 239
Cdd:PRK09880  157 VAIHAAHQAGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQNDD--LDHYKAEKG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 240 TFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGGD-VSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVV 318
Cdd:PRK09880  235 YFDVSFEVSGHPSSINTCLEVTRAKGVMVQVGMGGApPEFPMMTLIVKEISLKGSFRFTEEFNTAVSWLANGVINPLPLL 314

                         330       340
                  ....*....|....*....|....*....
gi 1543036938 319 SHTFPMLQARQAFELASDRQKAMKVLIDF 347
Cdd:PRK09880  315 SAEYPFTDLEEALIFAGDKTQAAKVQLVF 343
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 8-346 1.61e-111

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: 328.68  E-value: 1.61e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd05285     2 AVLHGPGDLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVGDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGsamrTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd05285    82 VAIEPGVPCRTCEFCKSGRYNLCPDMRFAA----TPPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGT----FDV 243
Cdd:cd05285   158 AGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNVRTEDTPESAEKIAELLggkgPDV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 244 MLECSGNERALRDGLEVMRPRGVVVQLGLGGD-VSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVVSHTF 322
Cdd:cd05285   238 VIECTGAESCIQTAIYATRPGGTVVLVGMGKPeVTLPLSAASLREIDIRGVFRYANTYPTAIELLASGKVDVKPLITHRF 317

                         330       340
                  ....*....|....*....|....*
gi 1543036938 323 PMLQARQAFELASD-RQKAMKVLID 346
Cdd:cd05285   318 PLEDAVEAFETAAKgKKGVIKVVIE 342
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 8-345 1.16e-90

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: 275.26  E-value: 1.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGfgtvRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08236     4 LVLTGPGDLRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYLGTG----AYHPPLVLGHEFSGTVEEVGSGVDDLAVGDR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd08236    80 VAVNPLLPCGKCEYCKKGEYSLCSNYDYIGS-----RRDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAAVALHAVRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGTFDVMLEC 247
Cdd:cd08236   155 AGITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTINPKEEDVEKVRELTEGRGADLVIEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQ---NMVVAKELSICGSF------RFHAEFALAVKLINEGRVDLSPV 317
Cdd:cd08236   235 AGSPATIEQALALARPGGKVVLVGIpYGDVTLSEeafEKILRKELTIQGSWnsysapFPGDEWRTALDLLASGKIKVEPL 314

                         330       340
                  ....*....|....*....|....*....
gi 1543036938 318 VSHTFPMLQARQAFE-LASDRQKAMKVLI 345
Cdd:cd08236   315 ITHRLPLEDGPAAFErLADREEFSGKVLL 343
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 8-345 5.76e-84

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: 257.84  E-value: 5.76e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnGGFGTvriKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08234     4 LVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYE-GEFGA---APPLVPGHEFAGVVVAVGSKVTGFKVGDR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd08234    80 VAVDPNIYCGECFYCRRGRPNLCENLTAVGV-----TRNGGFAEYVVVPAKQVYKIPDNLSFEEAALAEPLSCAVHGLDL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTwVARHSADKGTFDVMLEC 247
Cdd:cd08234   155 LGIKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPSREDP-EAQKEDNPYGFDVVIEA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNERALRDGLEVMRPRGVVVQLGLGGD---VSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVVSHTFPM 324
Cdd:cd08234   234 TGVPKTLEQAIEYARRGGTVLVFGVYAPdarVSISPFEIFQKELTIIGSFINPYTFPRAIALLESGKIDVKGLVSHRLPL 313

                         330       340
                  ....*....|....*....|.
gi 1543036938 325 LQARQAFELASDRqKAMKVLI 345
Cdd:cd08234   314 EEVPEALEGMRSG-GALKVVV 333
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 8-347 2.13e-81

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: 251.34  E-value: 2.13e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnGGFGTVRIkePMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08261     4 LVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYH-GRNPFASY--PRILGHELSGEVVEVGEGVAGLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNmLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd08261    81 VVVDPYISCGECYACRKGRPNCCENLQVLGV-----HRDGGFAE-YIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGvLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTW--VARHSADKGtFDVML 245
Cdd:cd08261   155 AGVTAGDTVLVVGAGPIG-LGVIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAarLRELTDGEG-ADVVI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 246 ECSGNERALRDGLEVMRPRGVVVQLGLG-GDVSIPQNMVVAKELSICGSfR--FHAEFALAVKLINEGRVDLSPVVSHTF 322
Cdd:cd08261   233 DATGNPASMEEAVELVAHGGRVVLVGLSkGPVTFPDPEFHKKELTILGS-RnaTREDFPDVIDLLESGKVDPEALITHRF 311

                         330       340
                  ....*....|....*....|....*.
gi 1543036938 323 PMLQARQAFE-LASDRQKAMKVLIDF 347
Cdd:cd08261   312 PFEDVPEAFDlWEAPPGGVIKVLIEF 337
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 8-345 1.60e-74

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: 234.03  E-value: 1.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGtvrIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08235     4 AVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIRGGHTD---LKPPRILGHEIAGEIVEVGDGVTGFKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAF-------RNMLLCEATqcVKVADHVPLRLAALAEPFSV 160
Cdd:cd08235    81 VFVAPHVPCGECHYCLRGNENMCPNYKKFGN-----LYDGGFaeyvrvpAWAVKRGGV--LKLPDNVSFEEAALVEPLAC 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 161 GLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQD--KTWVARHSADK 238
Cdd:cd08235   154 CINAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEdlVEKVRELTDGR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 239 GtFDVMLECSGNERALRDGLEVMRPRGVVV---QLGLGGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVDL 314
Cdd:cd08235   234 G-ADVVIVATGSPEAQAQALELVRKGGRILffgGLPKGSTVNIDPNLIHYREITITGSYAAsPEDYKEALELIASGKIDV 312

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1543036938 315 SPVVSHTFPMLQARQAFELASDrQKAMKVLI 345
Cdd:cd08235   313 KDLITHRFPLEDIEEAFELAAD-GKSLKIVI 342
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 9-346 3.94e-73

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 230.00  E-value: 3.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   9 VIHAPD-DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnGGFGtvRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:COG1064     5 VLTEPGgPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAE-GEWP--VPKLPLVPGHEIVGRVVAVGPGVTGFKVGDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAA-LAEPFSVGLHGVS 166
Cdd:COG1064    82 VGVGWVDSCGTCEYCRSGRENLCENGRFTGY-----TTDGGYAEYVVVPARFLVKLPDGLDPAEAApLLCAGITAYRALR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 167 RAGPLLGKRVLVSGCGPIGVLaIAAARAHGAAEITATDVVDEPLAIARAMGADNTINvAQDKTWVARHsADKGTFDVMLE 246
Cdd:COG1064   157 RAGVGPGDRVAVIGAGGLGHL-AVQIAKALGAEVIAVDRSPEKLELARELGADHVVN-SSDEDPVEAV-RELTGADVVID 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 247 CSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVDlspVVSHTFPM 324
Cdd:COG1064   234 TVGAPATVNAALALLRRGGRLVLVGLpGGPIPLPPFDLILKERSIRGSLIGtRADLQEMLDLAAEGKIK---PEVETIPL 310

                         330       340
                  ....*....|....*....|..
gi 1543036938 325 LQARQAFELASDRQKAMKVLID 346
Cdd:COG1064   311 EEANEALERLRAGKVRGRAVLD 332
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 8-346 8.96e-72

(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: 227.04  E-value: 8.96e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLH-YFHNGGFGTV-------RIKEPMVLGHEVAGTVVAVAPGV 79
Cdd:cd08233     4 ARYHGRKDIRVEEVPEPPVKPGEVKIKVAWCGICGSDLHeYLDGPIFIPTeghphltGETAPVTLGHEFSGVVVEVGSGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  80 ESVRIGDKVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRTphvqGAFRNMLLCEATQCVKVADHVPLRLAALAEPFS 159
Cdd:cd08233    84 TGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFIGLGGGG----GGFAEYVVVPAYHVHKLPDNVPLEEAALVEPLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 160 VGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTwVA--RHSAD 237
Cdd:cd08233   160 VAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVLDPTEVDV-VAevRKLTG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 238 KGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVDLS 315
Cdd:cd08233   239 GGGVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIwEKPISFNPNDLVLKEKTLTGSICYtREDFEEVIDLLASGKIDAE 318

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1543036938 316 PVVSHTFPMLQA-RQAF-ELASDRQKAMKVLID 346
Cdd:cd08233   319 PLITSRIPLEDIvEKGFeELINDKEQHVKILVS 351
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 16-345 1.58e-65

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: 210.94  E-value: 1.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRP 95
Cdd:cd05281    13 AELVEVPVPKPGPGEVLIKVLAASICGTDVHIYEWDEWAQSRIKPPLIFGHEFAGEVVEVGEGVTRVKVGDYVSAETHIV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  96 CGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSrAGPLLGKR 175
Cdd:cd05281    93 CGKCYQCRTGNYHVCQNTKILGV-----DTDGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVL-AGDVSGKS 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 176 VLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGTFDVMLECSGNERALR 255
Cdd:cd05281   167 VLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGADVVINPREEDVVEVKSVTDGTGVDVVLEMSGNPKAIE 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 256 DGLEVMRPRGVVVQLGL-GGDVSIP-QNMVVAKELSICG--SFRFHAEFALAVKLINEGRVDLSPVVSHTFPMLQARQAF 331
Cdd:cd05281   247 QGLKALTPGGRVSILGLpPGPVDIDlNNLVIFKGLTVQGitGRKMFETWYQVSALLKSGKVDLSPVITHKLPLEDFEEAF 326

                         330
                  ....*....|....
gi 1543036938 332 ELASDRQKAMKVLI 345
Cdd:cd05281   327 ELMRSGKCGKVVLY 340
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 14-344 2.03e-65

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 211.17  E-value: 2.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  14 DDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPS 93
Cdd:PLN02702   27 NTLKIQPFKLPPLGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  94 RPCGACKFCLEGLPNQCLDMRFYGsamrTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSRAGPLLG 173
Cdd:PLN02702  107 ISCWRCNLCKEGRYNLCPEMKFFA----TPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRANIGPE 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 174 KRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQ-----DKTWVARHSADKGTFDVMLECS 248
Cdd:PLN02702  183 TNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVLVSTniedvESEVEEIQKAMGGGIDVSFDCV 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 249 GNERALRDGLEVMRPRGVVVQLGLG-GDVSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVVSHTFPMLQ- 326
Cdd:PLN02702  263 GFNKTMSTALEATRAGGKVCLVGMGhNEMTVPLTPAAAREVDVVGVFRYRNTWPLCLEFLRSGKIDVKPLITHRFGFSQk 342

                         330
                  ....*....|....*....
gi 1543036938 327 -ARQAFELASDRQKAMKVL 344
Cdd:PLN02702  343 eVEEAFETSARGGNAIKVM 361
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 30-307 7.70e-62

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: 199.08  E-value: 7.70e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  30 QVLVKVGMGGICGSDLHYFHNGGFGtvRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGlpnq 109
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPP--PPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCREL---- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 110 CLDMRFYGsamrtPHVQGAFRNMLLCEATQCVKVADHVPLRLAALA-EPFSVGLHGVSRAGPL-LGKRVLVSGCGPIGVL 187
Cdd:cd05188    75 CPGGGILG-----EGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLpEPLATAYHALRRAGVLkPGDTVLVLGAGGVGLL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 188 aIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGTFDVMLECSGNERALRDGLEVMRPRGVV 267
Cdd:cd05188   150 -AAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGGGADVVIDAVGGPETLAQALRLLRPGGRI 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1543036938 268 VQLGL--GGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLI 307
Cdd:cd05188   229 VVVGGtsGGPPLDDLRRLLFKELTIIGSTGGtREDFEEALDLL 271
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 25-348 3.16e-60

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 196.97  E-value: 3.16e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  25 EIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLE 104
Cdd:PRK05396   22 EPGPNDVLIKVKKTAICGTDVHIYNWDEWAQKTIPVPMVVGHEFVGEVVEVGSEVTGFKVGDRVSGEGHIVCGHCRNCRA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 105 GLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVsRAGPLLGKRVLVSGCGPI 184
Cdd:PRK05396  102 GRRHLCRNTKGVGV-----NRPGAFAEYLVIPAFNVWKIPDDIPDDLAAIFDPFGNAVHTA-LSFDLVGEDVLITGAGPI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 185 GVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDK-TWVARHSADKGTFDVMLECSGNERALRDGLEVMRP 263
Cdd:PRK05396  176 GIMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAKEDlRDVMAELGMTEGFDVGLEMSGAPSAFRQMLDNMNH 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 264 RGVVVQLGL-GGDVSIPQNMVVAKELSICGSF-R--FHAEFALAVKLinEGRVDLSPVVSHTFPMLQARQAFELASdRQK 339
Cdd:PRK05396  256 GGRIAMLGIpPGDMAIDWNKVIFKGLTIKGIYgRemFETWYKMSALL--QSGLDLSPIITHRFPIDDFQKGFEAMR-SGQ 332


                  ....*....
gi 1543036938 340 AMKVLIDFT 348
Cdd:PRK05396  333 SGKVILDWD 341
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 11-310 1.41e-58

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: 191.76  E-value: 1.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  11 HAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGtvrIKEPMVLGHEVAGTVVAVAPGVESVRIGDKV-A 89
Cdd:cd08258     9 PGPGNVELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDP---VETPVVLGHEFSGTIVEVGPDVEGWKVGDRVvS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  90 VNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGV-SRA 168
Cdd:cd08258    86 ETTFSTCGRCPYCRRGDYNLCPHRKGIGT-----QADGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAVHAVaERS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 169 GPLLGKRVLVSGCGPIGVLAIAAARAH-GAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGTFDVMLEC 247
Cdd:cd08258   161 GIRPGDTVVVFGPGPIGLLAAQVAKLQgATVVVVGTEKDEVRLDVAKELGADAVNGGEEDLAELVNEITDGDGADVVIEC 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1543036938 248 SGNERALRDGLEVMRPRGVVVQLGLGG--DVSIPQNMVVAKELSICGSFRFHAE-FALAVKLINEG 310
Cdd:cd08258   241 SGAVPALEQALELLRKGGRIVQVGIFGplAASIDVERIIQKELSVIGSRSSTPAsWETALRLLASG 306
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 5-346 1.68e-58

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: 193.24  E-value: 1.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   5 CMCLVIHAPD-DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnGGFGtvRIKEPMVLGHEVAGTVVAVAPGV---- 79
Cdd:cd08231     1 ARAAVLTGPGkPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVA-GRRP--RVPLPIILGHEGVGRVVALGGGVttdv 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  80 --ESVRIGDKVAVNPSRPCGACKFCLEGLPNQCLDMRFYG--SAMRTPHVQGAF-RNMLLCEATQCVKVADHVPLRLAAL 154
Cdd:cd08231    78 agEPLKVGDRVTWSVGAPCGRCYRCLVGDPTKCENRKKYGheASCDDPHLSGGYaEHIYLPPGTAIVRVPDNVPDEVAAP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 155 A-EPFSVGLHGVSRAGP-LLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVA 232
Cdd:cd08231   158 AnCALATVLAALDRAGPvGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADATIDIDELPDPQR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 233 RHSADKGT----FDVMLECSGNERALRDGLEVMRPRGVVVQLGL---GGDVSIPQNMVVAKELSICGSFRFHAE-FALAV 304
Cdd:cd08231   238 RAIVRDITggrgADVVIEASGHPAAVPEGLELLRRGGTYVLVGSvapAGTVPLDPERIVRKNLTIIGVHNYDPShLYRAV 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1543036938 305 KLI--NEGRVDLSPVVSHTFPMLQARQAFELASDRqKAMKVLID 346
Cdd:cd08231   318 RFLerTQDRFPFAELVTHRYPLEDINEALELAESG-TALKVVID 360
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
 18-345 6.76e-57

L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme of threonine catabolism. Closely related proteins include sorbitol dehydrogenase, xylitol dehydrogenase, and benzyl alcohol dehydrogenase. Eukaryotic examples of this enzyme have been demonstrated experimentally but do not appear in database search results.E. coli His-90 modulates substrate specificity and is believed part of the active site. [Energy metabolism, Amino acids and amines]


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 188.53  E-value: 6.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  18 LDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCG 97
Cdd:TIGR00692  13 LTEVPVPEPGPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVGDYVSVETHIVCG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  98 ACKFCLEGLPNQCLDMRFYGsaMRTPhvqGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVsRAGPLLGKRVL 177
Cdd:TIGR00692  93 KCYACRRGQYHVCQNTKIFG--VDTD---GCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTV-LAGPISGKSVL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 178 VSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVA-QDKTWVARHSADKGTFDVMLECSGNERALRD 256
Cdd:TIGR00692 167 VTGAGPIGLMAIAVAKASGAYPVIVSDPNEYRLELAKKMGATYVVNPFkEDVVKEVADLTDGEGVDVFLEMSGAPKALEQ 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 257 GLEVMRPRGVVVQLGL-GGDVSIP-QNMVVAKELSICGSFRFH--AEFALAVKLINEGRVDLSPVVSHTFPMLQARQAFE 332
Cdd:TIGR00692 247 GLQAVTPGGRVSLLGLpPGKVTIDfTNKVIFKGLTIYGITGRHmfETWYTVSRLIQSGKLDLDPIITHKFKFDKFEKGFE 326

                         330
                  ....*....|...
gi 1543036938 333 LASDRQKAMKVLI 345
Cdd:TIGR00692 327 LMRSGQTGKVILS 339
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 8-345 7.44e-57

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: 188.77  E-value: 7.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHN-----GGFGTVR-IKEPMVLGHEVAGTVVAVAPGVES 81
Cdd:cd08256     4 VVCHGPQDYRLEEVPVPRPGPGEILVKVEACGICAGDIKCYHGapsfwGDENQPPyVKPPMIPGHEFVGRVVELGEGAEE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  82 --VRIGDKVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRtphVQGAFRNMLLCEATQCV-KVADHVPLRLAALAEPF 158
Cdd:cd08256    84 rgVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHDLYGFQNN---VNGGMAEYMRFPKEAIVhKVPDDIPPEDAILIEPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 159 SVGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADK 238
Cdd:cd08256   161 ACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALARKFGADVVLNPPEVDVVEKIKELTG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 239 G-TFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGGD-VSIPQNMVV-AKELSICGSFRFHAEFALAVKLINEGRVDLS 315
Cdd:cd08256   241 GyGCDIYIEATGHPSAVEQGLNMIRKLGRFVEFSVFGDpVTVDWSIIGdRKELDVLGSHLGPYCYPIAIDLIASGRLPTD 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1543036938 316 PVVSHTFPMLQARQAFELASDRQKAMKVLI 345
Cdd:cd08256   321 GIVTHQFPLEDFEEAFELMARGDDSIKVVL 350
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 27-347 6.31e-56

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: 185.99  E-value: 6.31e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  27 GPGQVLVKVGMGGICGSDLHYFHNGGFGTVriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGL 106
Cdd:cd08239    23 GPGEVLLRVKASGLCGSDLHYYYHGHRAPA--YQGVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHYVGCGACRNCRRGW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 107 PNQCLDMRFYGSAMRtphvQGAFRNMLLCEATQCVKVADHVPLRLAA-LAEPFSVGLHGVSRAGPLLGKRVLVSGCGPIG 185
Cdd:cd08239   101 MQLCTSKRAAYGWNR----DGGHAEYMLVPEKTLIPLPDDLSFADGAlLLCGIGTAYHALRRVGVSGRDTVLVVGAGPVG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 186 VLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGTFDVMLECSGNERALRDGLEVMRPRG 265
Cdd:cd08239   177 LGALMLARALGAEDVIGVDPSPERLELAKALGADFVINSGQDDVQEIRELTSGAGADVAIECSGNTAARRLALEAVRPWG 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 266 VVVQLGLGGDVSI-PQNMVVAKELSICGSFRFHA-EFALAVKLINEGRVDLSPVVSHTFPMLQARQAFELAsDRQKAMKV 343
Cdd:cd08239   257 RLVLVGEGGELTIeVSNDLIRKQRTLIGSWYFSVpDMEECAEFLARHKLEVDRLVTHRFGLDQAPEAYALF-AQGESGKV 335


                  ....
gi 1543036938 344 LIDF 347
Cdd:cd08239   336 VFVF 339
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 9-334 8.96e-53

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: 177.44  E-value: 8.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   9 VIHAPDDLRLDEQD--AGEIGPGQVLVKVGMGGICGSDLHYFHNGGfgTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGD 86
Cdd:cd08254     5 RFHKGSKGLLVLEEvpVPEPGPGEVLVKVKAAGVCHSDLHILDGGV--PTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  87 KVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMrtphvQGAFRNMLLCEATQCVKVADHVPL-RLAALAEPFSVGLHGV 165
Cdd:cd08254    83 RVAVPAVIPCGACALCRRGRGNLCLNQGMPGLGI-----DGGFAEYIVVPARALVPVPDGVPFaQAAVATDAVLTPYHAV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 166 SRAGPLL-GKRVLVSGCGPIGvLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGTFDVM 244
Cdd:cd08254   158 VRAGEVKpGETVLVIGLGGLG-LNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAGLGGGFDVI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 245 LECSGNERALRDGLEVMRPRGVVVQLGLGGD-VSIPQNMVVAKELSICGSF-RFHAEFALAVKLINEGRVDLspvVSHTF 322
Cdd:cd08254   237 FDFVGTQPTFEDAQKAVKPGGRIVVVGLGRDkLTVDLSDLIARELRIIGSFgGTPEDLPEVLDLIAKGKLDP---QVETR 313

                         330
                  ....*....|..
gi 1543036938 323 PMLQARQAFELA 334
Cdd:cd08254   314 PLDEIPEVLERL 325
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 9-332 6.83e-52

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: 175.81  E-value: 6.83e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   9 VIHAPD-DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnggfGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08279     5 VLHEVGkPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVT----GDLPAPLPAVLGHEGAGVVEEVGPGVTGVKPGDH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQC------LDMRFYGSAMRTpHVQG----------AFRNMLLCEATQCVKVADHVPLRL 151
Cdd:cd08279    81 VVLSWIPACGTCRYCSRGQPNLCdlgagiLGGQLPDGTRRF-TADGepvgamcglgTFAEYTVVPEASVVKIDDDIPLDR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 152 AAL---AEPFSVGlHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDK 228
Cdd:cd08279   160 AALlgcGVTTGVG-AVVNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGATHTVNASEDD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 229 TWVA-RHSADKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGGD---VSIPQNMVVAKELSICGSF----RFHAEF 300
Cdd:cd08279   239 AVEAvRDLTDGRGADYAFEAVGRAATIRQALAMTRKGGTAVVVGMGPPgetVSLPALELFLSEKRLQGSLygsaNPRRDI 318

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1543036938 301 ALAVKLINEGRVDLSPVVSHTFPMLQARQAFE 332
Cdd:cd08279   319 PRLLDLYRAGRLKLDELVTRRYSLDEINEAFA 350
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 8-332 1.99e-51

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: 174.29  E-value: 1.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDD-LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGD 86
Cdd:cd05284     4 ARLYEYGKpLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGILPYKLPFTLGHENAGWVEEVGSGVDGLKEGD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  87 KVAVNPSRPCGACKFCLEGLPNQCLDMRFYGsamRTPHvqGAFRNMLLCEATQCVKVADHV-PLRLAALAEpfsVGL--- 162
Cdd:cd05284    84 PVVVHPPWGCGTCRYCRRGEENYCENARFPG---IGTD--GGFAEYLLVPSRRLVKLPRGLdPVEAAPLAD---AGLtay 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 163 HGVSRAGPLL--GKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGT 240
Cdd:cd05284   156 HAVKKALPYLdpGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERLGADHVLNASDDVVEEVRELTGGRG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 241 FDVMLECSGNERALRDGLEVMRPRGVVVQLGLGGDVSIPQNMVVAKELSICGSF---RfhAEFALAVKLINEGRVdlSPV 317
Cdd:cd05284   236 ADAVIDFVGSDETLALAAKLLAKGGRYVIVGYGGHGRLPTSDLVPTEISVIGSLwgtR--AELVEVVALAESGKV--KVE 311

                         330
                  ....*....|....*
gi 1543036938 318 VShTFPMLQARQAFE 332
Cdd:cd05284   312 IT-KFPLEDANEALD 325
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
15-333 3.15e-51

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 174.12  E-value: 3.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  15 DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnggfGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSR 94
Cdd:COG1062     3 PLEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVRD----GDLPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  95 PCGACKFCLEGLPNQC---LDMRFYGSAMR-TPHV-------------QGAFRNMLLCEATQCVKVADHVPLRLAALaep 157
Cdd:COG1062    79 SCGHCRYCASGRPALCeagAALNGKGTLPDgTSRLssadgepvghffgQSSFAEYAVVPERSVVKVDKDVPLELAAL--- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 158 fsVG---LHGV----SRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTW 230
Cdd:COG1062   156 --LGcgvQTGAgavlNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHTVNPADEDAV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 231 VARHSADKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGG---DVSIPQNMVVAKELSICGSF----RFHAEFALA 303
Cdd:COG1062   234 EAVRELTGGGVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPpgaEISLDPFQLLLTGRTIRGSYfggaVPRRDIPRL 313

                         330       340       350
                  ....*....|....*....|....*....|
gi 1543036938 304 VKLINEGRVDLSPVVSHTFPMLQARQAFEL 333
Cdd:COG1062   314 VDLYRAGRLPLDELITRRYPLDEINEAFDD 343
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 14-346 5.15e-51

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: 173.26  E-value: 5.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  14 DDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHN--------GGFGTVRIKEPMVLGHEVAGTVVAVAPGVES-VRI 84
Cdd:cd08262     9 GPLVVRDVPDPEPGPGQVLVKVLACGICGSDLHATAHpeamvddaGGPSLMDLGADIVLGHEFCGEVVDYGPGTERkLKV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  85 GDKVAVNPSRPCGACKFCLEGLpnqcldmrfygsamrTPHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHG 164
Cdd:cd08262    89 GTRVTSLPLLLCGQGASCGIGL---------------SPEAPGGYAEYMLLSEALLLRVPDGLSMEDAALTEPLAVGLHA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 165 VSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQD------KTWVARHSADK 238
Cdd:cd08262   154 VRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGADIVVDPAADspfaawAAELARAGGPK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 239 GtfDVMLECSGNERALRDGLEVMRPRGVVVQLGL--GGDVSIPQnMVVAKELSICGSFRFH-AEFALAVKLINEGRVDLS 315
Cdd:cd08262   234 P--AVIFECVGAPGLIQQIIEGAPPGGRIVVVGVcmESDNIEPA-LAIRKELTLQFSLGYTpEEFADALDALAEGKVDVA 310

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1543036938 316 PVVSHTFPMLQARQAFELASDRQKAMKVLID 346
Cdd:cd08262   311 PMVTGTVGLDGVPDAFEALRDPEHHCKILVD 341
PRK10083 PRK10083
putative oxidoreductase; Provisional
 8-347 7.87e-50

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 169.92  E-value: 7.87e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFH-NGGFgtvrIKEPMVLGHEVAGTVVAVAPGVESVRIGD 86
Cdd:PRK10083    4 IVIEKPNSLAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRgHNPF----AKYPRVIGHEFFGVIDAVGEGVDAARIGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  87 KVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVS 166
Cdd:PRK10083   80 RVAVDPVISCGHCYPCSIGKPNVCTSLVVLGV-----HRDGGFSEYAVVPAKNAHRIPDAIADQYAVMVEPFTIAANVTG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 167 RAGPLLGKRVLVSGCGPIG-VLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKtwVARHSADKGTFDVML 245
Cdd:PRK10083  155 RTGPTEQDVALIYGAGPVGlTIVQVLKGVYNVKAVIVADRIDERLALAKESGADWVINNAQEP--LGEALEEKGIKPTLI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 246 -ECSGNERALRDGLEVMRPRGVVVQLGLGGDVS-IPQNMVVAKELSICGSFRFHAEFALAVKLINEGRVDLSPVVSHTFP 323
Cdd:PRK10083  233 iDAACHPSILEEAVTLASPAARIVLMGFSSEPSeIVQQGITGKELSIFSSRLNANKFPVVIDWLSKGLIDPEKLITHTFD 312

                         330       340
                  ....*....|....*....|....*
gi 1543036938 324 MLQARQAFELA-SDRQKAMKVLIDF 347
Cdd:PRK10083  313 FQHVADAIELFeKDQRHCCKVLLTF 337
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 8-347 2.16e-49

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: 168.97  E-value: 2.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEI-GPGQVLVKVGMGGICGSDLHYFHNGGFGTVrikePMVLGHEVAGTVVAVAPGVESVRIGD 86
Cdd:cd08284     4 VVFKGPGDVRVEEVPIPQIqDPTDAIVKVTAAAICGSDLHIYRGHIPSTP----GFVLGHEFVGEVVEVGPEVRTLKVGD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  87 KVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMrTPHVQGAfrnmllceATQCVKV--ADHVPLRLAA---------LA 155
Cdd:cd08284    80 RVVSPFTIACGECFYCRRGQSGRCAKGGLFGYAG-SPNLDGA--------QAEYVRVpfADGTLLKLPDglsdeaallLG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 156 EPFSVGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADnTINVAQD--KTWVAR 233
Cdd:cd08284   151 DILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAALGAE-PINFEDAepVERVRE 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 234 HSADKGtFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGGDVSIPQNMVVA--KELsicgSFRF-----HAEFALAVKL 306
Cdd:cd08284   230 ATEGRG-ADVVLEAVGGAAALDLAFDLVRPGGVISSVGVHTAEEFPFPGLDAynKNL----TLRFgrcpvRSLFPELLPL 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1543036938 307 INEGRVDLSPVVSHTFPMLQARQAFELAsDRQKAMKVLIDF 347
Cdd:cd08284   305 LESGRLDLEFLIDHRMPLEEAPEAYRLF-DKRKVLKVVLDP 344
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 16-346 7.30e-47

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: 162.10  E-value: 7.30e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHyFHNGGFGtvRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRP 95
Cdd:cd08259    13 LQIEEVPDPEPGPGEVLIKVKAAGVCYRDLL-FWKGFFP--RGKYPLILGHEIVGTVEEVGEGVERFKPGDRVILYYYIP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  96 CGACKFCLEGLPNQCLDMRFYGSAmrtphVQGAFRNMLLCEATQCVKVADHVPLRLAALAE-PFSVGLHGVSRAGPLLGK 174
Cdd:cd08259    90 CGKCEYCLSGEENLCRNRAEYGEE-----VDGGFAEYVKVPERSLVKLPDNVSDESAALAAcVVGTAVHALKRAGVKKGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 175 RVLVSGC-GPIGVLAIAAARAHGAAEITATDvVDEPLAIARAMGADNTINVAQDKTWVARhsadKGTFDVMLECSGNeRA 253
Cdd:cd08259   165 TVLVTGAgGGVGIHAIQLAKALGARVIAVTR-SPEKLKILKELGADYVIDGSKFSEDVKK----LGGADVVIELVGS-PT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 254 LRDGLEVMRPRGVVVQLG-LGGD-VSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVdlSPVVSHTFPMLQARQA 330
Cdd:cd08259   239 IEESLRSLNKGGRLVLIGnVTPDpAPLRPGLLILKEIRIIGSISAtKADVEEALKLVKEGKI--KPVIDRVVSLEDINEA 316

                         330
                  ....*....|....*.
gi 1543036938 331 FELASDRQKAMKVLID 346
Cdd:cd08259   317 LEDLKSGKVVGRIVLK 332
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 8-347 5.15e-46

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: 160.13  E-value: 5.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEI-GPGQVLVKVGMGGICGSDLHYFHNGGFGtvrIKEPMVLGHEVAGTVVAVAPGVESVRIGD 86
Cdd:cd05278     4 LVYLGPGKIGLEEVPDPKIqGPHDAIVRVTATSICGSDLHIYRGGVPG---AKHGMILGHEFVGEVVEVGSDVKRLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  87 KVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAM-RTPHVQGAFrnMLLCEATQ-CVKVADHVPLRLA-ALAEPFSVGLH 163
Cdd:cd05278    81 RVSVPCITFCGRCRFCRRGYHAHCENGLWGWKLGnRIDGGQAEY--VRVPYADMnLAKIPDGLPDEDAlMLSDILPTGFH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 164 GVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDkTWVARHSADKGT--F 241
Cdd:cd05278   159 GAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKNG-DIVEQILELTGGrgV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 242 DVMLECSGNERALRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSI-CGSFRFHAEFALAVKLINEGRVDLSPVV 318
Cdd:cd05278   238 DCVIEAVGFEETFEQAVKVVRPGGTIANVGVygKPDPLPLLGEWFGKNLTFkTGLVPVRARMPELLDLIEEGKIDPSKLI 317

                         330       340       350
                  ....*....|....*....|....*....|
gi 1543036938 319 SHTFPMLQARQAFELASDRQK-AMKVLIDF 347
Cdd:cd05278   318 THRFPLDDILKAYRLFDNKPDgCIKVVIRP 347
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
8-320 1.35e-41

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 148.44  E-value: 1.35e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEI-GPGQVLVKVGMGGICGSDL-HYFHNGGFgtvriKEPMVLGHEVAGTVVAVAPGVESVRIG 85
Cdd:PRK10309    4 VVNDTDGIVRVAESPIPEIkHQDDVLVKVASSGLCGSDIpRIFKNGAH-----YYPITLGHEFSGYVEAVGSGVDDLHPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  86 DKVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGV 165
Cdd:PRK10309   79 DAVACVPLLPCFTCPECLRGFYSLCAKYDFIGS-----RRDGGNAEYIVVKRKNLFALPTDMPIEDGAFIEPITVGLHAF 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 166 SRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSADKGTFD-VM 244
Cdd:PRK10309  154 HLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAMQTFNSREMSAPQIQSVLRELRFDqLI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 245 LECSGNERALRDGLEVMRPRGVVVQLG-LGGDVSIPQ---NMVVAKELSICGSFRFHA------EFALAVKLINEGRVDL 314
Cdd:PRK10309  234 LETAGVPQTVELAIEIAGPRAQLALVGtLHHDLHLTSatfGKILRKELTVIGSWMNYSspwpgqEWETASRLLTERKLSL 313


                  ....*.
gi 1543036938 315 SPVVSH 320
Cdd:PRK10309  314 EPLIAH 319
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 8-346 1.71e-41

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: 147.39  E-value: 1.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHyFHNGGFGTvrikePMVLGHEVAGTVVAVApgvESVRIGDK 87
Cdd:cd08242     4 LVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLE-IYKGYYPF-----PGVPGHEFVGIVEEGP---EAELVGKR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRtphvQGAFRNMLLCEATQCVKVADHVPLRLAALAEPFSVGLHGVSR 167
Cdd:cd08242    75 VVGEINIACGRCEYCRRGLYTHCPNRTVLGIVDR----DGAFAEYLTLPLENLHVVPDLVPDEQAVFAEPLAAALEILEQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 168 AGPLLGKRVLVSGCGPIGVLAIAAARAhgaaeiTATDVV-----DEPLAIARAMGADNTINVaqDKTWVARHsadkgtFD 242
Cdd:cd08242   151 VPITPGDKVAVLGDGKLGLLIAQVLAL------TGPDVVlvgrhSEKLALARRLGVETVLPD--EAESEGGG------FD 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 243 VMLECSGNERALRDGLEVMRPRGVVV-QLGLGGDVSIPQNMVVAKELSI----CGSFrfhaefALAVKLINEGRVDLSPV 317
Cdd:cd08242   217 VVVEATGSPSGLELALRLVRPRGTVVlKSTYAGPASFDLTKAVVNEITLvgsrCGPF------APALRLLRKGLVDVDPL 290

                         330       340
                  ....*....|....*....|....*....
gi 1543036938 318 VSHTFPMLQARQAFELASDRQkAMKVLID 346
Cdd:cd08242   291 ITAVYPLEEALEAFERAAEPG-ALKVLLR 318
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 16-332 3.48e-41

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: 147.36  E-value: 3.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGtvrIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRP 95
Cdd:cd08260    13 LEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPD---VTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVPFVLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  96 CGACKFCLEGLPNQCLDMRFYGSamrTPHvqGAF-RNMLLCEA-TQCVKVADHVPLRLAA-LAEPFSVGLHGVSRAGPLL 172
Cdd:cd08260    90 CGTCPYCRAGDSNVCEHQVQPGF---THP--GSFaEYVAVPRAdVNLVRLPDDVDFVTAAgLGCRFATAFRALVHQARVK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 173 -GKRVLVSGCGPIGvLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVAR-HSADKGTFDVMLECSGN 250
Cdd:cd08260   165 pGEWVAVHGCGGVG-LSAVMIASALGARVIAVDIDDDKLELARELGAVATVNASEVEDVAAAvRDLTGGGAHVSVDALGI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 251 ERALRDGLEVMRPRGVVVQLGL----GGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVDLSPVVSHTFPML 325
Cdd:cd08260   244 PETCRNSVASLRKRGRHVQVGLtlgeEAGVALPMDRVVARELEIVGSHGMpAHRYDAMLALIASGKLDPEPLVGRTISLD 323


                  ....*..
gi 1543036938 326 QARQAFE 332
Cdd:cd08260   324 EAPDALA 330
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 10-345 5.84e-41

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: 145.96  E-value: 5.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  10 IHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVA 89
Cdd:cd08269     1 LTGPGRFEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  90 VNPSrpcgackfcleglpnqcldmrfygsamrtphvqGAFRNMLLCEATQCVKVADHVPLRlAALAEPFSVGLHGVSRAG 169
Cdd:cd08269    81 GLSG---------------------------------GAFAEYDLADADHAVPLPSLLDGQ-AFPGEPLGCALNVFRRGW 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 170 PLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTIN--VAQDKTWVARHSADKGtFDVMLEC 247
Cdd:cd08269   127 IRAGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALARELGATEVVTddSEAIVERVRELTGGAG-ADVVIEA 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNERALRDGLEVMRPRGVVVQLGLGGDVSIPQNM--VVAKELSICGS-FRFHAE----FALAVKLINEGRVDLSPVVSH 320
Cdd:cd08269   206 VGHQWPLDLAGELVAERGRLVIFGYHQDGPRPVPFqtWNWKGIDLINAvERDPRIglegMREAVKLIADGRLDLGSLLTH 285

                         330       340
                  ....*....|....*....|....*.
gi 1543036938 321 TFPMLQARQAFELASDRQKA-MKVLI 345
Cdd:cd08269   286 EFPLEELGDAFEAARRRPDGfIKGVI 311
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 9-332 2.66e-38

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: 139.38  E-value: 2.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   9 VIHAPDD-LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTvriKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08245     4 VVHAAGGpLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGS---KYPLVPGHEIVGEVVEVGAGVEGRKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVN-PSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAAlaeP-FSVGLHGV 165
Cdd:cd08245    81 VGVGwLVGSCGRCEYCRRGLENLCQKAVNTGY-----TTQGGYAEYMVADAEYTVLLPDGLPLAQAA---PlLCAGITVY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 166 S---RAGPLLGKRVLVSGCGPIGVLaIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVarhsADKGTFD 242
Cdd:cd08245   153 SalrDAGPRPGERVAVLGIGGLGHL-AVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQ----AAAGGAD 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 243 VMLECSGNERALRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSICGSFRF-HAEFALAVKLINEGRVdlSPVVs 319
Cdd:cd08245   228 VILVTVVSGAAAEAALGGLRRGGRIVLVGLpeSPPFSPDIFPLIMKRQSIAGSTHGgRADLQEALDFAAEGKV--KPMI- 304

                         330
                  ....*....|...
gi 1543036938 320 HTFPMLQARQAFE 332
Cdd:cd08245   305 ETFPLDQANEAYE 317
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 29-142 2.02e-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: 130.04  E-value: 2.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  29 GQVLVKVGMGGICGSDLHYFhNGGFGTVriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGLPN 108
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIY-KGGNPPV--KLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1543036938 109 QCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVK 142
Cdd:pfam08240  78 LCPNGRFLGY-----DRDGGFAEYVVVPERNLVP 106
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 7-347 3.31e-37

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: 136.51  E-value: 3.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   7 CLVIHAPDD--LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHyFHNGGFGtVRIKEPMVLGHEVAGTVVAVAPGVESVRI 84
Cdd:cd08297     3 AAVVEEFGEkpYEVKDVPVPEPGPGEVLVKLEASGVCHTDLH-AALGDWP-VKPKLPLIGGHEGAGVVVAVGPGVSGLKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  85 GDKVAV-NPSRPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAAlaeP-FSVGL 162
Cdd:cd08297    81 GDRVGVkWLYDACGKCEYCRTGDETLCPNQKNSGY-----TVDGTFAEYAIADARYVTPIPDGLSFEQAA---PlLCAGV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 163 ---HGVSRAGPLLGKRVLVSGC-GPIGVLAIAAARAHGAAEItATDVVDEPLAIARAMGADNTINVA-QDKTWVARHSAD 237
Cdd:cd08297   153 tvyKALKKAGLKPGDWVVISGAgGGLGHLGVQYAKAMGLRVI-AIDVGDEKLELAKELGADAFVDFKkSDDVEAVKELTG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 238 KGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSICGSF---RfhAEFALAVKLINEGRV 312
Cdd:cd08297   232 GGGAHAVVVTAVSAAAYEQALDYLRPGGTLVCVGLppGGFIPLDPFDLVLRGITIVGSLvgtR--QDLQEALEFAARGKV 309

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1543036938 313 DlspVVSHTFPMLQARQAFELASDRQKAMKVLIDF 347
Cdd:cd08297   310 K---PHIQVVPLEDLNEVFEKMEEGKIAGRVVVDF 341
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 4-333 1.36e-36

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: 135.44  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   4 RCMCLVIH-APddLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHyFHNGGF----------GTVRIKEPMVLGHEVAGTV 72
Cdd:cd08240     2 KAAAVVEPgKP--LEEVEIDTPKPPGTEVLVKVTACGVCHSDLH-IWDGGYdlgggktmslDDRGVKLPLVLGHEIVGEV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  73 VAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAmrtphVQGAFRNMLLCEATQCVKVADHVPLRLA 152
Cdd:cd08240    79 VAVGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRALGIF-----QDGGYAEYVIVPHSRYLVDPGGLDPALA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 153 ALAePFSvGL---HGVSRAGPLLGKR-VLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDK 228
Cdd:cd08240   154 ATL-ACS-GLtaySAVKKLMPLVADEpVVIIGAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADVVVNGSDPD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 229 TWVARHSADKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSFRFH-AEFALAVKL 306
Cdd:cd08240   232 AAKRIIKAAGGGVDAVIDFVNNSATASLAFDILAKGGKLVLVGLfGGEATLPLPLLPLRALTIQGSYVGSlEELRELVAL 311

                         330       340
                  ....*....|....*....|....*..
gi 1543036938 307 INEGRvdLSPVVSHTFPMLQARQAFEL 333
Cdd:cd08240   312 AKAGK--LKPIPLTERPLSDVNDALDD 336
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 15-345 3.66e-34

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: 129.56  E-value: 3.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  15 DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTV----RIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAV 90
Cdd:cd08265    38 ELRVEDVPVPNLKPDEILIRVKACGICGSDIHLYETDKDGYIlypgLTEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  91 NPSRPCGACKFCLEGLPNQCLDMRFYGSAmrtphVQGAFRNMLLCEATQCVKVADHVPL-------RLAALAEPFSVGLH 163
Cdd:cd08265   118 EEMMWCGMCRACRSGSPNHCKNLKELGFS-----ADGAFAEYIAVNARYAWEINELREIysedkafEAGALVEPTSVAYN 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 164 GV-SRAGPLL-GKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTIN---VAQDKTWVARHSADK 238
Cdd:cd08265   193 GLfIRGGGFRpGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYVFNptkMRDCLSGEKVMEVTK 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 239 GT-FDVMLECSGNERALRDGLE-VMRPRGVVVQLGLGG-DVSIPQNMVVAKELSICGS--FRFHAEFALAVKLINEGRVD 313
Cdd:cd08265   273 GWgADIQVEAAGAPPATIPQMEkSIAINGKIVYIGRAAtTVPLHLEVLQVRRAQIVGAqgHSGHGIFPSVIKLMASGKID 352

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1543036938 314 LSPVVSHTFPMLQARQAFELASDRqKAMKVLI 345
Cdd:cd08265   353 MTKIITARFPLEGIMEAIKAASER-TDGKITI 383
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 8-293 1.97e-33

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: 127.23  E-value: 1.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPD-DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHyFHNGGFGTVRikePMVLGHEVAGTVVAVAPGVESVRIGD 86
Cdd:cd08278     6 AVVREPGgPFVLEDVELDDPRPDEVLVRIVATGICHTDLV-VRDGGLPTPL---PAVLGHEGAGVVEAVGSAVTGLKPGD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  87 KVAVNPSRpCGACKFCLEGLPNQCLDM--------RFYGS-AMRTPHV---------QGAFRNMLLCEATQCVKVADHVP 148
Cdd:cd08278    82 HVVLSFAS-CGECANCLSGHPAYCENFfplnfsgrRPDGStPLSLDDGtpvhghffgQSSFATYAVVHERNVVKVDKDVP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 149 LRLAAlaePFSVGL-------HGVSRAGPllGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNT 221
Cdd:cd08278   161 LELLA---PLGCGIqtgagavLNVLKPRP--GSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKELGATHV 235

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1543036938 222 INVA-QDKTWVARHSADKGTfDVMLECSGNERALRDGLEVMRPRGVVVQLG---LGGDVSIPQNMVVAKELSICGS 293
Cdd:cd08278   236 INPKeEDLVAAIREITGGGV-DYALDTTGVPAVIEQAVDALAPRGTLALVGappPGAEVTLDVNDLLVSGKTIRGV 310
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 16-347 1.17e-31

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 121.68  E-value: 1.17e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHngGFGTvRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRP 95
Cdd:PRK13771   13 YRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQ--GFYP-RMKYPVILGHEVVGTVEEVGENVKGFKPGDRVASLLYAP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  96 CGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAALAePFSVGL--HGVSRAGPLLG 173
Cdd:PRK13771   90 DGTCEYCRSGEEAYCKNRLGYGE-----ELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIV-PCVTGMvyRGLRRAGVKKG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 174 KRVLVSGCGPiGVlaiaaarahgaaEITAtdvvdepLAIARAMGAdNTINV--AQDKTWVARHSADK------------- 238
Cdd:PRK13771  164 ETVLVTGAGG-GV------------GIHA-------IQVAKALGA-KVIAVtsSESKAKIVSKYADYvivgskfseevkk 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 239 -GTFDVMLECSGN---ERALRDglevMRPRGVVVQLglgGDV------SIPQNMVVAKELSICGSF---RFHAEFALavK 305
Cdd:PRK13771  223 iGGADIVIETVGTptlEESLRS----LNMGGKIIQI---GNVdpsptySLRLGYIILKDIEIIGHIsatKRDVEEAL--K 293

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1543036938 306 LINEGRVdlSPVVSHTFPMLQARQAFELASDRQKAMKVLIDF 347
Cdd:PRK13771  294 LVAEGKI--KPVIGAEVSLSEIDKALEELKDKSRIGKILVKP 333
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 8-347 4.73e-31

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: 120.43  E-value: 4.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEI-GPGQVLVKVGMGGICGSDLHYFHnggfGTV-RIKEPMVLGHEVAGTVVAVAPGVESVRIG 85
Cdd:cd08286     4 LVYHGPGKISWEDRPKPTIqEPTDAIVKMLKTTICGTDLHILK----GDVpTVTPGRILGHEGVGVVEEVGSAVTNFKVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  86 DKVAVNPSRPCGACKFCLEGLPNQC------LDMRFYGSA---MRTPHVQGAFrnmllceatqcVKVADHVPLRLA-ALA 155
Cdd:cd08286    80 DRVLISCISSCGTCGYCRKGLYSHCesggwiLGNLIDGTQaeyVRIPHADNSL-----------YKLPEGVDEEAAvMLS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 156 EPFSVGLH-GVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQD--KTWVA 232
Cdd:cd08286   149 DILPTGYEcGVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHTVNSAKGdaIEQVL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 233 RHSADKGtFDVMLECSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSFRFHAEFALAVKLINEGR 311
Cdd:cd08286   229 ELTDGRG-VDVVIEAVGIPATFELCQELVAPGGHIANVGVhGKPVDLHLEKLWIKNITITTGLVDTNTTPMLLKLVSSGK 307

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1543036938 312 VDLSPVVSHTFP---MLQARQAFELASDrQKAMKVLIDF 347
Cdd:cd08286   308 LDPSKLVTHRFKlseIEKAYDTFSAAAK-HKALKVIIDF 345
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 8-348 7.36e-31

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


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 119.10  E-value: 7.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHA---PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLhYFHNGGFGtVRIKEPMVLGHEVAGTVVAVAPGVESVRI 84
Cdd:COG0604     4 IVITEfggPEVLELEEVPVPEPGPGEVLVRVKAAGVNPADL-LIRRGLYP-LPPGLPFIPGSDAAGVVVAVGEGVTGFKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  85 GDKVAVNPsrpcgackfcleglpnqcldmrfygsamrtphVQGAFRNMLLCEATQCVKVADHVPLR-LAALAEPFSVGLH 163
Cdd:COG0604    82 GDRVAGLG--------------------------------RGGGYAEYVVVPADQLVPLPDGLSFEeAAALPLAGLTAWQ 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 164 GVSRAGPLL-GKRVLV----SGCGPI--------GVlaiaaarahgaaEITATDVVDEPLAIARAMGADNTINVAQD--K 228
Cdd:COG0604   130 ALFDRGRLKpGETVLVhgaaGGVGSAavqlakalGA------------RVIATASSPEKAELLRALGADHVIDYREEdfA 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 229 TWVARHSADKGtFDVMLECSGNErALRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSICGSF-------RFHAE 299
Cdd:COG0604   198 ERVRALTGGRG-VDVVLDTVGGD-TLARSLRALAPGGRLVSIGAasGAPPPLDLAPLLLKGLTLTGFTlfardpaERRAA 275

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1543036938 300 FALAVKLINEGRvdLSPVVSHTFPMLQARQAFELASDRQKAMKVLIDFT 348
Cdd:COG0604   276 LAELARLLAAGK--LRPVIDRVFPLEEAAEAHRLLESGKHRGKVVLTVD 322
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 15-333 9.76e-31

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: 119.85  E-value: 9.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  15 DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnggfGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSR 94
Cdd:cd05279    12 PLSIEEIEVAPPKAGEVRIKVVATGVCHTDLHVID----GKLPTPLPVILGHEGAGIVESIGPGVTTLKPGDKVIPLFGP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  95 PCGACKFCLEGLPNQCLDM--------------RFYGSAMRTPHVQG--AFRNMLLCEATQCVKVADHVPLRLAALAE-P 157
Cdd:cd05279    88 QCGKCKQCLNPRPNLCSKSrgtngrglmsdgtsRFTCKGKPIHHFLGtsTFAEYTVVSEISLAKIDPDAPLEKVCLIGcG 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 158 FSVGLHGVSRAGPLL-GKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVA-QDKTWVA--R 233
Cdd:cd05279   168 FSTGYGAAVNTAKVTpGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECINPRdQDKPIVEvlT 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 234 HSADKGTfDVMLECSGNERALRDGLEVMRPR-GVVVQLGL---GGDVSIPQNMVVAKEL---SICGSFRFHAEFALAVKL 306
Cdd:cd05279   248 EMTDGGV-DYAFEVIGSADTLKQALDATRLGgGTSVVVGVppsGTEATLDPNDLLTGRTikgTVFGGWKSKDSVPKLVAL 326

                         330       340
                  ....*....|....*....|....*..
gi 1543036938 307 INEGRVDLSPVVSHTFPMLQARQAFEL 333
Cdd:cd05279   327 YRQKKFPLDELITHVLPFEEINDGFDL 353
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 16-332 2.31e-30

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: 119.01  E-value: 2.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnggfGTVRIKEPMVLGHEVAGTVVAVAPGVES---VRIGDKVAVNP 92
Cdd:cd08263    13 LTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLK----GELPFPPPFVLGHEISGEVVEVGPNVENpygLSVGDRVVGSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  93 SRPCGACKFCLEGLPNQC--------LDMRFYGSAMRTPHVQGAFRNMLL---------CEATQCVKVADHVPLRLAA-L 154
Cdd:cd08263    89 IMPCGKCRYCARGKENLCedffaynrLKGTLYDGTTRLFRLDGGPVYMYSmgglaeyavVPATALAPLPESLDYTESAvL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 155 AEPFSVGLHGVSRAGPL-LGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQ-DKTWVA 232
Cdd:cd08263   169 GCAGFTAYGALKHAADVrPGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAKELGATHTVNAAKeDAVAAI 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 233 RHSADKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGG---DVSIPQNMVVAKELSICGSF--RFHAEFALAVKLI 307
Cdd:cd08263   249 REITGGRGVDVVVEALGKPETFKLALDVVRDGGRAVVVGLAPggaTAEIPITRLVRRGIKIIGSYgaRPRQDLPELVGLA 328

                         330       340
                  ....*....|....*....|....*
gi 1543036938 308 NEGRVDLSPVVSHTFPMLQARQAFE 332
Cdd:cd08263   329 ASGKLDPEALVTHKYKLEEINEAYE 353
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 16-345 1.63e-29

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: 116.71  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFhNGgfgtVRIKE-PMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSR 94
Cdd:cd08281    21 LVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVI-NG----DRPRPlPMALGHEAAGVVVEVGEGVTDLEVGDHVVLVFVP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  95 PCGACKFCLEGLPNQCL--------------DMRFYGSAMRTPHVQG--AFRNMLLCEATQCVKVADHVPLRLAAL---A 155
Cdd:cd08281    96 SCGHCRPCAEGRPALCEpgaaangagtllsgGRRLRLRGGEINHHLGvsAFAEYAVVSRRSVVKIDKDVPLEIAALfgcA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 156 EPFSVGLhGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINvAQDKTWVAR-H 234
Cdd:cd08281   176 VLTGVGA-VVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARELGATATVN-AGDPNAVEQvR 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 235 SADKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGL---GGDVSIPQNMVVAKELSICGSFRFHA----EFALAVKLI 307
Cdd:cd08281   254 ELTGGGVDYAFEMAGSVPALETAYEITRRGGTTVTAGLpdpEARLSVPALSLVAEERTLKGSYMGSCvprrDIPRYLALY 333

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1543036938 308 NEGRVDLSPVVSHTFPMLQARQAFElASDRQKAMKVLI 345
Cdd:cd08281   334 LSGRLPVDKLLTHRLPLDEINEGFD-RLAAGEAVRQVI 370
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 22-294 2.43e-29

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: 115.29  E-value: 2.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  22 DAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTvriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNP-SRPCGACK 100
Cdd:cd05283    18 ERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPT---KYPLVPGHEIVGIVVAVGSKVTKFKVGDRVGVGCqVDSCGTCE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 101 FCLEGLPNQCLDMRFYGSAMRTPHV--QGAFRNMLLCEATQCVKVADHVPLRLAAlaePFSVGlhGVSRAGPLL------ 172
Cdd:cd05283    95 QCKSGEEQYCPKGVVTYNGKYPDGTitQGGYADHIVVDERFVFKIPEGLDSAAAA---PLLCA--GITVYSPLKrngvgp 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 173 GKRVLVSGCGPIGVLaiaaarahgaaeitAT--------DVVdeplAI---------ARAMGADNTINVAQDKTWvarhS 235
Cdd:cd05283   170 GKRVGVVGIGGLGHL--------------AVkfakalgaEVT----AFsrspskkedALKLGADEFIATKDPEAM----K 227

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 236 ADKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSF 294
Cdd:cd05283   228 KAAGSLDLIIDTVSASHDLDPYLSLLKPGGTLVLVGApEEPLPVPPFPLIFGRKSVAGSL 287
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 54-345 3.70e-28

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: 110.82  E-value: 3.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  54 GTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNpsrpcgackfcleglpnqcldmrfygsamrtphvqGAFRNML 133
Cdd:cd08255    14 GTEKLPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCF-----------------------------------GPHAERV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 134 LCEATQCVKVADHVPLRLAALAEPFSVGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIA 213
Cdd:cd08255    59 VVPANLLVPLPDGLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 214 RAMGADNTINVAQDKTWvarhsaDKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLG--------LGGDVSIPQNMVVA 285
Cdd:cd08255   139 EALGPADPVAADTADEI------GGRGADVVIEASGSPSALETALRLLRDRGRVVLVGwyglkpllLGEEFHFKRLPIRS 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1543036938 286 KELSICGSFRFH------AEFALAVKLINEGRVDlsPVVSHTFPMLQARQAFE-LASDRQKAMKVLI 345
Cdd:cd08255   213 SQVYGIGRYDRPrrwteaRNLEEALDLLAEGRLE--ALITHRVPFEDAPEAYRlLFEDPPECLKVVL 277
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 25-347 7.60e-28

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: 111.58  E-value: 7.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  25 EIGPGQVLVKVGMGGICGSDLhYFHNGGFGtVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLE 104
Cdd:cd08266    24 EPGPDEVLVRVKAAALNHLDL-WVRRGMPG-IKLPLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPGISCGRCEYCLA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 105 GLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVPLRLAAlAEP--FSVGLHG-VSRAGPLLGKRVLVSGC 181
Cdd:cd08266   102 GRENLCAQYGILGE-----HVDGGYAEYVAVPARNLLPIPDNLSFEEAA-AAPltFLTAWHMlVTRARLRPGETVLVHGA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 182 GPiGV-LAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDK--TWVARHSADKGTfDVMLECSGnERALRDGL 258
Cdd:cd08266   176 GS-GVgSAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDfvREVRELTGKRGV-DVVVEHVG-AATWEKSL 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 259 EVMRPRGVVVQLG--LGGDVSIPQNMVVAKELSICGSFRFH-AEFALAVKLINEGRVDlsPVVSHTFPMLQARQAFELAS 335
Cdd:cd08266   253 KSLARGGRLVTCGatTGYEAPIDLRHVFWRQLSILGSTMGTkAELDEALRLVFRGKLK--PVIDSVFPLEEAAEAHRRLE 330

                         330
                  ....*....|..
gi 1543036938 336 DRQKAMKVLIDF 347
Cdd:cd08266   331 SREQFGKIVLTP 342
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 8-347 1.30e-27

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: 110.79  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTvriKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08285     4 FAMLGIGKVGWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGE---RHGMILGHEAVGVVEEVGSEVKDFKPGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDM----RFY----GSAMRTPHVQGAFRNMllceatqcVKVADHVPLRLAA-LAEPF 158
Cdd:cd08285    81 VIVPAITPDWRSVAAQRGYPSQSGGMlggwKFSnfkdGVFAEYFHVNDADANL--------APLPDGLTDEQAVmLPDMM 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 159 SVGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTIN------VAQdktwVA 232
Cdd:cd08285   153 STGFHGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDIVDykngdvVEQ----IL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 233 RHSADKGTfDVMLECSGNERALRDGLEVMRPRGVVVQLG-LGGDVSIPQNMVV------AKEL--SICGSFRFHAEFALA 303
Cdd:cd08285   229 KLTGGKGV-DAVIIAGGGQDTFEQALKVLKPGGTISNVNyYGEDDYLPIPREEwgvgmgHKTIngGLCPGGRLRMERLAS 307

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1543036938 304 vkLINEGRVDLS-PVVSHTFPMLQARQAFELASDRQKAM-KVLIDF 347
Cdd:cd08285   308 --LIEYGRVDPSkLLTHHFFGFDDIEEALMLMKDKPDDLiKPVIIF 351
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 8-338 1.75e-27

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: 111.09  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAGEI-GPGQVLVKVGMGGICGSDLHYFHnggfGTV-RIKEPMVLGHEVAGTVVAVAPGVESVRIG 85
Cdd:cd08283     4 LVWHGKGDVRVEEVPDPKIeDPTDAIVRVTATAICGSDLHLYH----GYIpGMKKGDILGHEFMGVVEEVGPEVRNLKVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  86 DKVAVNPSRPCGACKFCLEGLPNQC-------LDMRFYGSAMRT----PHVQGAFrnmllcEATQ------------CVK 142
Cdd:cd08283    80 DRVVVPFTIACGECFYCKRGLYSQCdntnpsaEMAKLYGHAGAGifgySHLTGGY------AGGQaeyvrvpfadvgPFK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 143 VADHVPLRLAA-LAEPFSVGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNT 221
Cdd:cd08283   154 IPDDLSDEKALfLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAET 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 222 INVAQDKTWVAR---------------------HSADKGTFDVMLECSGNER--ALRDGLEVMRPRGVVVQLGL--GGDV 276
Cdd:cd08283   234 INFEEVDDVVEAlreltggrgpdvcidavgmeaHGSPLHKAEQALLKLETDRpdALREAIQAVRKGGTVSIIGVygGTVN 313

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543036938 277 SIPQNMVVAKELSI-CGSFRFHAEFALAVKLINEGRVDLSPVVSHTFPMLQARQAFELASDRQ 338
Cdd:cd08283   314 KFPIGAAMNKGLTLrMGQTHVQRYLPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKE 376
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 12-346 1.78e-25

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: 104.59  E-value: 1.78e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  12 APDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLhYFHNGGFGTVrIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVavn 91
Cdd:cd08253    11 APDVLRLGDLPVPTPGPGEVLVRVHASGVNPVDT-YIRAGAYPGL-PPLPYVPGSDGAGVVEAVGEGVDGLKVGDRV--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  92 psrpcgackfcleglpnqcldmrFYGSAMRTpHVQGAFRNMLLCEATQCVKVADHVPLRL-AALAEPFSVGLHGV-SRAG 169
Cdd:cd08253    86 -----------------------WLTNLGWG-RRQGTAAEYVVVPADQLVPLPDGVSFEQgAALGIPALTAYRALfHRAG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 170 PLLGKRVLVSGcGPIGV-LAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDkTWVARHSA--DKGTFDVMLE 246
Cdd:cd08253   142 AKAGETVLVHG-GSGAVgHAAVQLARWAGARVIATASSAEGAELVRQAGADAVFNYRAE-DLADRILAatAGQGVDVIIE 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 247 CSGNERALRDgLEVMRPRGVVVQLG-LGGDVSIPQNMVVAKELSICGSFRFHA---EFALAVKLINEGRVD--LSPVVSH 320
Cdd:cd08253   220 VLANVNLAKD-LDVLAPGGRIVVYGsGGLRGTIPINPLMAKEASIRGVLLYTAtpeERAAAAEAIAAGLADgaLRPVIAR 298

                         330       340
                  ....*....|....*....|....*.
gi 1543036938 321 TFPMLQARQAFELASDRQKAMKVLID 346
Cdd:cd08253   299 EYPLEEAAAAHEAVESGGAIGKVVLD 324
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 9-345 7.08e-25

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: 103.16  E-value: 7.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   9 VIHAPDDLRLDE-QDAGEIGPGQVLVKVGMGGICGSDLHYFHnggfGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDK 87
Cdd:cd08287     5 VIHGPGDIRVEEvPDPVIEEPTDAVIRVVATCVCGSDLWPYR----GVSPTRAPAPIGHEFVGVVEEVGSEVTSVKPGDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  88 VAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAM--------RTPHVQGAfrnmLLCEATQCVKVADHVPlRLAALAEPFS 159
Cdd:cd08287    81 VIAPFAISDGTCPFCRAGFTTSCVHGGFWGAFVdggqgeyvRVPLADGT----LVKVPGSPSDDEDLLP-SLLALSDVMG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 160 VGLHGVSRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTwVARHSADKG 239
Cdd:cd08287   156 TGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAREFGATDIVAERGEEA-VARVRELTG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 240 TF--DVMLECSGNERALRDGLEVMRPRGVVVQLGL-GGDVSIPQNMVVAKELSICGSF----RFHAEFalaVKLINEGRV 312
Cdd:cd08287   235 GVgaDAVLECVGTQESMEQAIAIARPGGRVGYVGVpHGGVELDVRELFFRNVGLAGGPapvrRYLPEL---LDDVLAGRI 311

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1543036938 313 DLSPVVSHTFPMLQARQAFElASDRQKAMKVLI 345
Cdd:cd08287   312 NPGRVFDLTLPLDEVAEGYR-AMDERRAIKVLL 343
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 28-347 5.05e-24

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), 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. 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 an 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: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 101.51  E-value: 5.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  28 PGQVLVKVGMGGICGSDLHYFHnGGFGTvriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGLP 107
Cdd:cd08282    25 PTDAIVRITTTAICGSDLHMYR-GRTGA---EPGLVLGHEAMGEVEEVGSAVESLKVGDRVVVPFNVACGRCRNCKRGLT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 108 NQCLDMrfygsAMRTPHVQGAFRNMLLCEATQC----VKVADH----VPLRLAA--------LAEPFSVGLHGVSRAGPL 171
Cdd:cd08282   101 GVCLTV-----NPGRAGGAYGYVDMGPYGGGQAeylrVPYADFnllkLPDRDGAkekddylmLSDIFPTGWHGLELAGVQ 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 172 LGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADnTINVAQDKTWVARHSADKGTFDVMLECSGNE 251
Cdd:cd08282   176 PGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAESIGAI-PIDFSDGDPVEQILGLEPGGVDRAVDCVGYE 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 252 -----------RALRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSI------CGSFRFHAEFALA-------VK 305
Cdd:cd08282   255 ardrggeaqpnLVLNQLIRVTRPGGGIGIVGVyvAEDPGAGDAAAKQGELSFdfgllwAKGLSFGTGQAPVkkynrqlRD 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1543036938 306 LINEGRVDLSPVVSHTFPMLQARQAFElASDRQKAMKVLIDF 347
Cdd:cd08282   335 LILAGRAKPSFVVSHVISLEDAPEAYA-RFDKRLETKVVIKP 375
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 8-334 8.44e-23

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


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 96.86  E-value: 8.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHA---PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRI 84
Cdd:cd05289     4 VRIHEyggPEVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTLPLIPGHDVAGVVVAVGPGVTGFKV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  85 GDKVAvnpsrpcgackfcleglpnqcldmrfygsAMRTPHVQGAFRNMLLCEATQCVKVADHVPLRLAAlAEPfSVGL-- 162
Cdd:cd05289    84 GDEVF-----------------------------GMTPFTRGGAYAEYVVVPADELALKPANLSFEEAA-ALP-LAGLta 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 163 -HGVSRAGPLL-GKRVLVSG-CGPIGVLaIAAARAHGAAEITAT---DVVDEplaiARAMGADNTINVAQDKtwvARHSA 236
Cdd:cd05289   133 wQALFELGGLKaGQTVLIHGaAGGVGSF-AVQLAKARGARVIATasaANADF----LRSLGADEVIDYTKGD---FERAA 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 237 DKGTFDVMLECSGNErALRDGLEVMRPRGVVVQLglggdVSIPQNMVVAKELSICGSFRF----HAEFALAVKLINEGRv 312
Cdd:cd05289   205 APGGVDAVLDTVGGE-TLARSLALVKPGGRLVSI-----AGPPPAEQAAKRRGVRAGFVFvepdGEQLAELAELVEAGK- 277

                         330       340
                  ....*....|....*....|..
gi 1543036938 313 dLSPVVSHTFPMLQARQAFELA 334
Cdd:cd05289   278 -LRPVVDRVFPLEDAAEAHERL 298
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 9-348 9.35e-22

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 94.33  E-value: 9.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   9 VIHAPDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHyFHNGGFGTVrikEPMVLGHEVAGTVVAVAPGVESVRIGDKV 88
Cdd:PRK09422    6 VNKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLH-VANGDFGDK---TGRILGHEGIGIVKEVGPGVTSLKVGDRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  89 AVN-PSRPCGACKFCLEGLPNQCLDMRFYGSAmrtphVQGAFrnmllceATQCVKVADH---VPLRLAAlAEPFSVGLHG 164
Cdd:PRK09422   82 SIAwFFEGCGHCEYCTTGRETLCRSVKNAGYT-----VDGGM-------AEQCIVTADYavkVPEGLDP-AQASSITCAG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 165 V--------SRAGPllGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSA 236
Cdd:PRK09422  149 VttykaikvSGIKP--GQWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 237 DKGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGLGG---DVSIPQnmVVAKELSICGSF---RfhAEFALAVKLINEG 310
Cdd:PRK09422  227 KTGGAHAAVVTAVAKAAFNQAVDAVRAGGRVVAVGLPPesmDLSIPR--LVLDGIEVVGSLvgtR--QDLEEAFQFGAEG 302

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1543036938 311 RVdlSPVVsHTFPMLQARQAFELASDRQKAMKVLIDFT 348
Cdd:PRK09422  303 KV--VPKV-QLRPLEDINDIFDEMEQGKIQGRMVIDFT 337
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 8-347 2.04e-21

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: 93.82  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPD-DLRLDEQDAGEIGPGQVLVKVGMGGICGSDlHYFHNGGFGTVRIKEP-MVLGHEVAGTVVAVAPGVEsVRIG 85
Cdd:cd08230     4 IAVKPGKpGVRVVDIPEPEPTPGEVLVRTLEVGVCGTD-REIVAGEYGTAPPGEDfLVLGHEALGVVEEVGDGSG-LSPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  86 DKVAVNPSRPCGACKFCLEGLPNQCLDMRFYGSAMRTPHvqGAFRNMLLCEATQCVKVADHVpLRLAALAEPFSVGLHGV 165
Cdd:cd08230    82 DLVVPTVRRPPGKCLNCRIGRPDFCETGEYTERGIKGLH--GFMREYFVDDPEYLVKVPPSL-ADVGVLLEPLSVVEKAI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 166 -------SRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITA--TDVVDEPLAIARAMGADnTINVAQD-KTWVARHs 235
Cdd:cd08230   159 eqaeavqKRLPTWNPRRALVLGAGPIGLLAALLLRLRGFEVYVLnrRDPPDPKADIVEELGAT-YVNSSKTpVAEVKLV- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 236 adkGTFDVMLECSGNERALRDGLEVMRPRGVVVQLGL---GGDVSIPQ----NMVVAKELSICGSF---RFHAEFALAVK 305
Cdd:cd08230   237 ---GEFDLIIEATGVPPLAFEALPALAPNGVVILFGVpggGREFEVDGgelnRDLVLGNKALVGSVnanKRHFEQAVEDL 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1543036938 306 LINEGRVD--LSPVVSHTFPMLQARQAFELASDRQkaMKVLIDF 347
Cdd:cd08230   314 AQWKYRWPgvLERLITRRVPLEEFAEALTEKPDGE--IKVVIEW 355
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 13-345 2.05e-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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 93.05  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  13 PDDLRLDEQDAG--EIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVav 90
Cdd:cd08267     9 PEVLLLLEVEVPipTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPFPPIPGMDFAGEVVAVGSGVTRFKVGDEV-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  91 npsrpcgackfcleglpnqcldmrfYGSAMRTPHvqGAFRNMLLCEATQCVKVADHVPLRLAAlAEPFS--VGLHGVSRA 168
Cdd:cd08267    87 -------------------------FGRLPPKGG--GALAEYVVAPESGLAKKPEGVSFEEAA-ALPVAglTALQALRDA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 169 GPLL-GKRVLV----SGCGPIGVlaiaAARAHGAAEITATDVvDEPLAIARAMGADNTINVAQDKtwVARHSADKGTFDV 243
Cdd:cd08267   139 GKVKpGQRVLIngasGGVGTFAV----QIAKALGAHVTGVCS-TRNAELVRSLGADEVIDYTTED--FVALTAGGEKYDV 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 244 MLECSGNE-RALRDGLEVMRPRGVVVQLGLGGDVSIpqnMVVAKELSICGSFRFHAEFALA----------VKLINEGRv 312
Cdd:cd08267   212 IFDAVGNSpFSLYRASLALKPGGRYVSVGGGPSGLL---LVLLLLPLTLGGGGRRLKFFLAkpnaedleqlAELVEEGK- 287

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1543036938 313 dLSPVVSHTFPMLQARQAFELASDRQKAMKVLI 345
Cdd:cd08267   288 -LKPVIDSVYPLEDAPEAYRRLKSGRARGKVVI 319
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 16-182 8.45e-21

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: 91.48  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnggfG-TVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNP-S 93
Cdd:cd08298    17 LRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVE----GdLPPPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRVGVPWlG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  94 RPCGACKFCLEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKV-ADHVPLRLAALAEPFSVGLHGVSRAGPLL 172
Cdd:cd08298    93 STCGECRYCRSGRENLCDNARFTGY-----TVDGGYAEYMVADERFAYPIpEDYDDEEAAPLLCAGIIGYRALKLAGLKP 167

                         170
                  ....*....|
gi 1543036938 173 GKRVLVSGCG 182
Cdd:cd08298   168 GQRLGLYGFG 177
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 3-345 2.49e-20

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: 90.86  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   3 LRCMCLVIHAPDD-LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFhnggFGTVRIKEPMVLGHEVAGTVVAVAPGVES 81
Cdd:cd08277     1 IKCKAAVAWEAGKpLVIEEIEVAPPKANEVRIKMLATSVCHTDILAI----EGFKATLFPVILGHEGAGIVESVGEGVTN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  82 VRIGDKVaVNPSRP-CGACKFCLEGLPNQCLDMRFYGSAM-------------RTPHVQG--AFRNMLLCEATQCVKVAD 145
Cdd:cd08277    77 LKPGDKV-IPLFIGqCGECSNCRSGKTNLCQKYRANESGLmpdgtsrftckgkKIYHFLGtsTFSQYTVVDENYVAKIDP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 146 HVPLRLAALAE-PFSVGLHGVSR-AGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTIN 223
Cdd:cd08277   156 AAPLEHVCLLGcGFSTGYGAAWNtAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGATDFIN 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 224 VAQDKTWV--ARHSADKGTFDVMLECSGNERALRDGLEVMRP---RGVVVQLGLGGDVSI-PQNMVVAKEL--SICGSFR 295
Cdd:cd08277   236 PKDSDKPVseVIREMTGGGVDYSFECTGNADLMNEALESTKLgwgVSVVVGVPPGAELSIrPFQLILGRTWkgSFFGGFK 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1543036938 296 FHAEFALAVKLINEGRVDLSPVVSHTFPMLQARQAFELASdRQKAMKVLI 345
Cdd:cd08277   316 SRSDVPKLVSKYMNKKFDLDELITHVLPFEEINKGFDLMK-SGECIRTVI 364
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 14-332 9.23e-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: 85.87  E-value: 9.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  14 DDLRLDEQDAGEIGPGQVLVKVGMGGICGSDlhYFhnggfgTV-RIK-EPM--VLGHEVAGTVVAVAPGVESVRIGDKVA 89
Cdd:cd08264    12 ENLKVEDVKDPKPGPGEVLIRVKMAGVNPVD--YN------VInAVKvKPMphIPGAEFAGVVEEVGDHVKGVKKGDRVV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  90 VNPSRPCGACKFCLEGLPNQCLDMRFYGSAmrtphVQGAFRNMLLCEATQCVKVADHVPLRLAAlaepfSVGL------H 163
Cdd:cd08264    84 VYNRVFDGTCDMCLSGNEMLCRNGGIIGVV-----SNGGYAEYIVVPEKNLFKIPDSISDELAA-----SLPVaaltayH 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 164 GVSRAGPLLGKRVLVSGC-GPIGVLAiaaarahgaaeitatdvvdepLAIARAMGADnTINVAQdKTWVARHSAD----- 237
Cdd:cd08264   154 ALKTAGLGPGETVVVFGAsGNTGIFA---------------------VQLAKMMGAE-VIAVSR-KDWLKEFGADevvdy 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 238 ----------KGTFDVMLECSGnERALRDGLEVMRPRGVVVQLG--LGGDVSIPQNMVVAKELSICGSFR-FHAEFALAV 304
Cdd:cd08264   211 deveekvkeiTKMADVVINSLG-SSFWDLSLSVLGRGGRLVTFGtlTGGEVKLDLSDLYSKQISIIGSTGgTRKELLELV 289

                         330       340
                  ....*....|....*....|....*...
gi 1543036938 305 KLINegrvDLSPVVSHTFPMLQARQAFE 332
Cdd:cd08264   290 KIAK----DLKVKVWKTFKLEEAKEALK 313
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 8-346 1.03e-18

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: 85.63  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHA---PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHnggfGT--VRIKEPMVLGHEVAGTVVAVAPGVESV 82
Cdd:cd08241     4 VVCKElggPEDLVLEEVPPEPGAPGEVRIRVEAAGVNFPDLLMIQ----GKyqVKPPLPFVPGSEVAGVVEAVGEGVTGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  83 RIGDKVAVNPSrpcgackfcleglpnqcldmrfygsamrtphvQGAFRNMLLCEATQCVKVADHVPLRLAAlAEPFSVG- 161
Cdd:cd08241    80 KVGDRVVALTG--------------------------------QGGFAEEVVVPAAAVFPLPDGLSFEEAA-ALPVTYGt 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 162 -LHG-VSRAGPLLGKRVLVSGC-GPIGvlaiaaarahgaaeITATDVV-------------DEPLAIARAMGADNTINvA 225
Cdd:cd08241   127 aYHAlVRRARLQPGETVLVLGAaGGVG--------------LAAVQLAkalgarviaaassEEKLALARALGADHVID-Y 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 226 QDKTWVA--RHSADKGTFDVMLECSGN---ERALRdgleVMRPRGVVVQLGL-GGDV-SIPQNMVVAKELSICGSF---- 294
Cdd:cd08241   192 RDPDLRErvKALTGGRGVDVVYDPVGGdvfEASLR----SLAWGGRLLVIGFaSGEIpQIPANLLLLKNISVVGVYwgay 267

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1543036938 295 ------RFHAEFALAVKLINEGRvdLSPVVSHTFPMLQARQAFELASDRQKAMKVLID 346
Cdd:cd08241   268 arrepeLLRANLAELFDLLAEGK--IRPHVSAVFPLEQAAEALRALADRKATGKVVLT 323
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
199-309 2.97e-18

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 79.96  E-value: 2.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 199 EITATDVVDEPLAIARAMGADNTINVAQD--KTWVARHSADKGtFDVMLECSGNERALRDGLEVMRPRGVVVQLGLG-GD 275
Cdd:pfam00107  16 KVIAVDGSEEKLELAKELGADHVINPKETdlVEEIKELTGGKG-VDVVFDCVGSPATLEQALKLLRPGGRVVVVGLPgGP 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1543036938 276 VSIPQNMVVAKELSICGSFRF-HAEFALAVKLINE 309
Cdd:pfam00107  95 LPLPLAPLLLKELTILGSFLGsPEEFPEALDLLAS 129
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 12-346 1.24e-16

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: 79.63  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  12 APDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFhNGGFGtVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVavn 91
Cdd:cd05282    10 LPLVLELVSLPIPPPGPGEVLVRMLAAPINPSDLITI-SGAYG-SRPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRV--- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  92 psrpcgackfclegLPnqcldmrfygsamrtPHVQGAFRNMLLCEATQCVKVADHVPLRLAA--LAEPFSVGLhGVSRAG 169
Cdd:cd05282    85 --------------LP---------------LGGEGTWQEYVVAPADDLIPVPDSISDEQAAmlYINPLTAWL-MLTEYL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 170 PLL-GKRVLVSGCGpiGVLAIAAARAHGAAEITATDVVDEPLAIAR--AMGADNTINvAQDKTWVAR-HSADKGT-FDVM 244
Cdd:cd05282   135 KLPpGDWVIQNAAN--SAVGRMLIQLAKLLGFKTINVVRRDEQVEElkALGADEVID-SSPEDLAQRvKEATGGAgARLA 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 245 LECSGNERALRdGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSICGSF-----------RFHAEFALAVKLINEGR 311
Cdd:cd05282   212 LDAVGGESATR-LARSLRPGGTLVNYGLlsGEPVPFPRSVFIFKDITVRGFWlrqwlhsatkeAKQETFAEVIKLVEAGV 290

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1543036938 312 vdLSPVVSHTFPMLQARQAFELASDRQKAMKVLID 346
Cdd:cd05282   291 --LTTPVGAKFPLEDFEEAVAAAEQPGRGGKVLLT 323
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 12-110 1.65e-16

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: 79.21  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  12 APDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGtvrIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVN 91
Cdd:cd08296     9 PGGPLELVERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPG---LSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVG 85

                          90       100
                  ....*....|....*....|
gi 1543036938  92 -PSRPCGACKFCLEGLPNQC 110
Cdd:cd08296    86 wHGGHCGTCDACRRGDFVHC 105
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 27-330 1.78e-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: 76.57  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  27 GPGQVLVKVGMGGI-----------------CGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVA 89
Cdd:cd08274    27 APGEVLIRVGACGVnntdintregwystevdGATDSTGAGEAGWWGGTLSFPRIQGADIVGRVVAVGEGVDTARIGERVL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  90 VNPSRPcgackfclEGLPNQCLDMRFYGSamrtpHVQGAFRNMLLCEATQCVKVADHVP-LRLAALAEPFSVGLHGVSRA 168
Cdd:cd08274   107 VDPSIR--------DPPEDDPADIDYIGS-----ERDGGFAEYTVVPAENAYPVNSPLSdVELATFPCSYSTAENMLERA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 169 GPLLGKRVLVSGC-GPIGVLAIAAARAHGAAEITATDVVDEplAIARAMGADNTINVAQDKTWVARhSADKGTFDVMLEC 247
Cdd:cd08274   174 GVGAGETVLVTGAsGGVGSALVQLAKRRGAIVIAVAGAAKE--EAVRALGADTVILRDAPLLADAK-ALGGEPVDVVADV 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNErALRDGLEVMRPRGVVVQLG-LGGD-VSIPQNMVVAKELSICGS-FRFHAEFALAVKLINEGRvdLSPVVSHTFPM 324
Cdd:cd08274   251 VGGP-LFPDLLRLLRPGGRYVTAGaIAGPvVELDLRTLYLKDLTLFGStLGTREVFRRLVRYIEEGE--IRPVVAKTFPL 327


                  ....*.
gi 1543036938 325 LQARQA 330
Cdd:cd08274   328 SEIREA 333
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 29-333 5.12e-15

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: 75.34  E-value: 5.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  29 GQVLVKVGMGGICGSDlHYFHNGG-----FgtvrikePMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCL 103
Cdd:cd08300    28 GEVRIKILATGVCHTD-AYTLSGAdpeglF-------PVILGHEGAGIVESVGEGVTSVKPGDHVIPLYTPECGECKFCK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 104 EGLPNQCLDMR-FYGSAM---RTP----------HVQG--AFRNMLLCEATQCVKVADHVPL-RLAALAEPFSVGLHGV- 165
Cdd:cd08300   100 SGKTNLCQKIRaTQGKGLmpdGTSrfsckgkpiyHFMGtsTFSEYTVVAEISVAKINPEAPLdKVCLLGCGVTTGYGAVl 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 166 SRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVARHSAD--KGTFDV 243
Cdd:cd08300   180 NTAKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPKDHDKPIQQVLVEmtDGGVDY 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 244 MLECSGNERALRDGLEVM-RPRGVVVQLGL---GGDVSI-PQNMVVAKEL--SICGSFRFHAEFALAVKLINEGRVDLSP 316
Cdd:cd08300   260 TFECIGNVKVMRAALEAChKGWGTSVIIGVaaaGQEISTrPFQLVTGRVWkgTAFGGWKSRSQVPKLVEDYMKGKIKVDE 339

                         330
                  ....*....|....*..
gi 1543036938 317 VVSHTFPMLQARQAFEL 333
Cdd:cd08300   340 FITHTMPLDEINEAFDL 356
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 8-345 8.85e-15

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


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 74.01  E-value: 8.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHA---PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLhYFHNGgfgTVRIKEPMVLGHEVAGTVVAVAPGVESVRI 84
Cdd:cd05286     3 VRIHKtggPEVLEYEDVPVPEPGPGEVLVRNTAIGVNFIDT-YFRSG---LYPLPLPFVLGVEGAGVVEAVGPGVTGFKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  85 GDKVAvnpsrpcgackfcleglpnqcldmrfYGSAMrtphvqGAFRNMLLCEATQCVKVADHVPLRLAAlaepfSVGLHG 164
Cdd:cd05286    79 GDRVA--------------------------YAGPP------GAYAEYRVVPASRLVKLPDGISDETAA-----ALLLQG 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 165 ------VSRAGPLL-GKRVLV----SGCGPI--------GVlaiaaarahgaaEITATDVVDEPLAIARAMGADNTIN-- 223
Cdd:cd05286   122 ltahylLRETYPVKpGDTVLVhaaaGGVGLLltqwakalGA------------TVIGTVSSEEKAELARAAGADHVINyr 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 224 ----VAQdktwVARHSADKGtFDVMLECSGNErALRDGLEVMRPRGVVVQLG-LGGDVS-IPQNMVVAKELSICGSFRFH 297
Cdd:cd05286   190 dedfVER----VREITGGRG-VDVVYDGVGKD-TFEGSLDSLRPRGTLVSFGnASGPVPpFDLLRLSKGSLFLTRPSLFH 263

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1543036938 298 -----AEFALAVK----LINEGRvdLSPVVSHTFPMLQARQAFELASDRQKAMKVLI 345
Cdd:cd05286   264 yiatrEELLARAAelfdAVASGK--LKVEIGKRYPLADAAQAHRDLESRKTTGKLLL 318
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 25-272 9.57e-15

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 74.53  E-value: 9.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  25 EIGPGQVLVKVGMGGICGSDLHYFHNG-GFGtvriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNP-SRPCGACKFC 102
Cdd:PLN02586   34 ENGDEDVTVKILYCGVCHSDLHTIKNEwGFT----RYPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGViVGSCKSCESC 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 103 LEGLPNQCLDMRFYGSAMRTPHVQ--GAFRNMLLCEATQCVKVADHVPLRLAA--LAEPFSV----GLHGVSRAGPLLGk 174
Cdd:PLN02586  110 DQDLENYCPKMIFTYNSIGHDGTKnyGGYSDMIVVDQHFVLRFPDNLPLDAGAplLCAGITVyspmKYYGMTEPGKHLG- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 175 rvlVSGCGPIG-VLAIAAARAHGAAEITATDVVDEPLAIARaMGADNTInVAQDKTwvaRHSADKGTFDVMLECSGNERA 253
Cdd:PLN02586  189 ---VAGLGGLGhVAVKIGKAFGLKVTVISSSSNKEDEAINR-LGADSFL-VSTDPE---KMKAAIGTMDYIIDTVSAVHA 260

                         250
                  ....*....|....*....
gi 1543036938 254 LRDGLEVMRPRGVVVQLGL 272
Cdd:PLN02586  261 LGPLLGLLKVNGKLITLGL 279
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 12-333 1.86e-14

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: 73.24  E-value: 1.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  12 APDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDL-----HYFHNGGfgtvrikEPMVLGHEVAGTVVAVAPGVESVRIGD 86
Cdd:cd05276    11 GPEVLELGEVPKPAPGPGEVLIRVAAAGVNRADLlqrqgLYPPPPG-------ASDILGLEVAGVVVAVGPGVTGWKVGD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  87 KVavnpsrpCGACkfcleglpnqcldmrfYGsamrtphvqGAFRNMLLCEATQCVKVADHVPLRLAA-LAEPFSV---GL 162
Cdd:cd05276    84 RV-------CALL----------------AG---------GGYAEYVVVPAGQLLPVPEGLSLVEAAaLPEVFFTawqNL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 163 HGVSRAGPllGKRVLV----SGCGPIGVLAIAAARAhgaaEITATDVVDEPLAIARAMGADNTINV-AQD-KTWVARHSA 236
Cdd:cd05276   132 FQLGGLKA--GETVLIhggaSGVGTAAIQLAKALGA----RVIATAGSEEKLEACRALGADVAINYrTEDfAEEVKEATG 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 237 DKGtFDVMLECSGNErALRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSICGS------FRFHAEFALAVK--- 305
Cdd:cd05276   206 GRG-VDVILDMVGGD-YLARNLRALAPDGRLVLIGLlgGAKAELDLAPLLRKRLTLTGStlrsrsLEEKAALAAAFRehv 283

                         330       340       350
                  ....*....|....*....|....*....|
gi 1543036938 306 --LINEGRVDlsPVVSHTFPMLQARQAFEL 333
Cdd:cd05276   284 wpLFASGRIR--PVIDKVFPLEEAAEAHRR 311
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 29-332 2.52e-14

ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of the MDR/zinc-dependent alcohol dehydrogenase-like family, oxidizes the phosphate ester of ribitol-5-phosphate to xylulose-5-phosphate of 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-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: 176199 [Multi-domain]  Cd Length: 341  Bit Score: 73.17  E-value: 2.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  29 GQVLVKVGMGGICGSDLHYFH-NGGFGTVRIKEPMVLGHEVAGTVVAVAPGveSVRIGDKVAVNPSRPCGACKFCLEglp 107
Cdd:cd08237    26 DWVIVRPTYLSICHADQRYYQgNRSPEALKKKLPMALIHEGIGVVVSDPTG--TYKVGTKVVMVPNTPVEKDEIIPE--- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 108 NQCLDMRFYGSAMrtphvqGAFRNMLLCEATQC-VKVADHVPLRLAALAEPFSVGLHGVSRAGPLLGKR---VLVSGCGP 183
Cdd:cd08237   101 NYLPSSRFRSSGY------DGFMQDYVFLPPDRlVKLPDNVDPEVAAFTELVSVGVHAISRFEQIAHKDrnvIGVWGDGN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 184 IGVlaiaaarahgaaeITATdVVDEPLAIAR--AMGADNT---INVAQDKTWVARHSADKGTFDVMLECSG---NERALR 255
Cdd:cd08237   175 LGY-------------ITAL-LLKQIYPESKlvVFGKHQEkldLFSFADETYLIDDIPEDLAVDHAFECVGgrgSQSAIN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 256 DGLEVMRPRGVVVQLGLGGD-VSIPQNMVVAKELSICGSFRF-HAEFALAVKLIN---EGRVDLSPVVSHTFPMLQAR-- 328
Cdd:cd08237   241 QIIDYIRPQGTIGLMGVSEYpVPINTRMVLEKGLTLVGSSRStREDFERAVELLSrnpEVAEYLRKLVGGVFPVRSINdi 320


                  ....*
gi 1543036938 329 -QAFE 332
Cdd:cd08237   321 hRAFE 325
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 30-333 4.28e-14

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: 72.73  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  30 QVLVKVGMGGICGSDLHYFHnggfGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGLPNQ 109
Cdd:cd08299    34 EVRIKIVATGICRSDDHVVS----GKLVTPFPVILGHEAAGIVESVGEGVTTVKPGDKVIPLFVPQCGKCRACLNPESNL 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 110 C------------LDM--RFYGSAMRTPHVQG--AFRNMLLCEATQCVKVADHVPLRLAALAE-PFSVGlHG--VSRAGP 170
Cdd:cd08299   110 ClkndlgkpqglmQDGtsRFTCKGKPIHHFLGtsTFSEYTVVDEIAVAKIDAAAPLEKVCLIGcGFSTG-YGaaVNTAKV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 171 LLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTIN----------VAQDKTwvarhsadKGT 240
Cdd:cd08299   189 TPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATECINpqdykkpiqeVLTEMT--------DGG 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 241 FDVMLECSGNERALRDGLE-VMRPRGVVVQLGLGGD---VSI-PQNMVVAKEL--SICGSFRFHAEFALAVKLINEGRVD 313
Cdd:cd08299   261 VDFSFEVIGRLDTMKAALAsCHEGYGVSVIVGVPPSsqnLSInPMLLLTGRTWkgAVFGGWKSKDSVPKLVADYMAKKFN 340

                         330       340
                  ....*....|....*....|
gi 1543036938 314 LSPVVSHTFPMLQARQAFEL 333
Cdd:cd08299   341 LDPLITHTLPFEKINEGFDL 360
PLN02740 PLN02740
Alcohol dehydrogenase-like
 3-345 1.43e-13

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 70.98  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   3 LRCMCLVIHAPDD-LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHngGFGTVRIKEPMVLGHEVAGTVVAVAPGVES 81
Cdd:PLN02740    9 ITCKAAVAWGPGEpLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWK--GENEAQRAYPRILGHEAAGIVESVGEGVED 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  82 VRIGDKVAVNPSRPCGACKFCLEGLPNQCL---------------DMRFYGSAMRTP--HV--QGAFRNMLLCEATQCVK 142
Cdd:PLN02740   87 LKAGDHVIPIFNGECGDCRYCKRDKTNLCEtyrvdpfksvmvndgKTRFSTKGDGQPiyHFlnTSTFTEYTVLDSACVVK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 143 VADHVPL-RLAALAEPFSVGLHGV-SRAGPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADN 220
Cdd:PLN02740  167 IDPNAPLkKMSLLSCGVSTGVGAAwNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKEMGITD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 221 TINVAQDKTWV---ARHSADKGTfDVMLECSGNERALRDG-LEVMRPRGVVVQLGLGGDVSI----PQNMVVAKELSIC- 291
Cdd:PLN02740  247 FINPKDSDKPVherIREMTGGGV-DYSFECAGNVEVLREAfLSTHDGWGLTVLLGIHPTPKMlplhPMELFDGRSITGSv 325

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1543036938 292 -GSFRFHAEFALAVKLINEGRVDLSPVVSHTFPMLQARQAFELASDrQKAMKVLI 345
Cdd:PLN02740  326 fGDFKGKSQLPNLAKQCMQGVVNLDGFITHELPFEKINEAFQLLED-GKALRCLL 379
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 13-347 4.68e-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: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 69.10  E-value: 4.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  13 PDDLRLDEQDAGEIGPGQVLVKVgmggicgsdlHY----FH-----NGGFGTvRIKEPMVLGHEVAGTVVAVAPGVESVR 83
Cdd:cd08276    12 LDNLKLVEEPVPEPGPGEVLVRV----------HAvslnYRdllilNGRYPP-PVKDPLIPLSDGAGEVVAVGEGVTRFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  84 IGDKVAVNpsrpcgackF---CLEGLPNQCLDMRFYGsamrtPHVQGAFRNMLLCEATQCVKVADHVPLRLAAlAEPFS- 159
Cdd:cd08276    81 VGDRVVPT---------FfpnWLDGPPTAEDEASALG-----GPIDGVLAEYVVLPEEGLVRAPDHLSFEEAA-TLPCAg 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 160 ----VGLHGVSRAGPllGKRVLVSGCGpiGV-LAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINVAQDKTWVA-- 232
Cdd:cd08276   146 ltawNALFGLGPLKP--GDTVLVQGTG--GVsLFALQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPDWGEev 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 233 -RHSADKGtFDVMLEcSGNERALRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSI----CGSfrfHAEFALAVK 305
Cdd:cd08276   222 lKLTGGRG-VDHVVE-VGGPGTLAQSIKAVAPGGVISLIGFlsGFEAPVLLLPLLTKGATLrgiaVGS---RAQFEAMNR 296

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1543036938 306 LINegRVDLSPVVSHTFPMLQARQAFELASDRQKAMKVLIDF 347
Cdd:cd08276   297 AIE--AHRIRPVIDRVFPFEEAKEAYRYLESGSHFGKVVIRV 336
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 12-347 7.58e-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: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 68.35  E-value: 7.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  12 APDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIkePMVLGHEVAGTVVAVAPGVESVRIGDKVAvn 91
Cdd:cd08272    11 GPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARPPL--PAILGCDVAGVVEAVGEGVTRFRVGDEVY-- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  92 psrpcgackFCLEGLPNqcldmrfygsamrtphVQGAFrnmllceATQCVKVADHVPLRLAAL--AEPFSVGLHG----- 164
Cdd:cd08272    87 ---------GCAGGLGG----------------LQGSL-------AEYAVVDARLLALKPANLsmREAAALPLVGitawe 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 165 --VSRAGPLLGKRVLVSGcGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTINvaQDKTW---VARHSADKG 239
Cdd:cd08272   135 glVDRAAVQAGQTVLIHG-GAGGVGHVAVQLAKAAGARVYATASSEKAAFARSLGADPIIY--YRETVveyVAEHTGGRG 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 240 tFDVMLECSGNErALRDGLEVMRPRGVVVQLGLGGdvsiPQNMVVA--KELSIcgsfrfHAEFALAVKLINEGRVD---- 313
Cdd:cd08272   212 -FDVVFDTVGGE-TLDASFEAVALYGRVVSILGGA----THDLAPLsfRNATY------SGVFTLLPLLTGEGRAHhgei 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1543036938 314 ------------LSPVVS-HTFPMLQARQAFELASDRQKAMKVLIDF 347
Cdd:cd08272   280 lreaarlvergqLRPLLDpRTFPLEEAAAAHARLESGSARGKIVIDV 326
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 61-345 1.08e-11

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: 64.76  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  61 PMVLGHEVAGTVVAVAPGVESVRIGDKVAVnpsrpcgackfcleglpnqcldmrFYGSAMrtphvqGAFRNMLLCEATQC 140
Cdd:cd08251    38 PFTPGFEASGVVRAVGPHVTRLAVGDEVIA------------------------GTGESM------GGHATLVTVPEDQV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 141 VkvadHVPLRL-----AALAEPFSVGLHGVSRAGPLLGKRVLVS----GCGPIGVlaiaAARAHGAAEITATDVVDEPLA 211
Cdd:cd08251    88 V----RKPASLsfeeaCALPVVFLTVIDAFARAGLAKGEHILIQtatgGTGLMAV----QLARLKGAEIYATASSDDKLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 212 IARAMGADNTIN-VAQD-KTWVARHSADKGTfDVMLECSGNErALRDGLEVMRPRGVVVQLGLGG-------DVSIPQN- 281
Cdd:cd08251   160 YLKQLGVPHVINyVEEDfEEEIMRLTGGRGV-DVVINTLSGE-AIQKGLNCLAPGGRYVEIAMTAlksapsvDLSVLSNn 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1543036938 282 ----MVVAKELSICGSFRFHAEFALAVKLINEGrvDLSPVVSHTFPMLQARQAFELASDRQKAMKVLI 345
Cdd:cd08251   238 qsfhSVDLRKLLLLDPEFIADYQAEMVSLVEEG--ELRPTVSRIFPFDDIGEAYRYLSDRENIGKVVV 303
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 13-92 1.70e-11

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 64.54  E-value: 1.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  13 PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLhYFHNGGFGTVRIkEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNP 92
Cdd:cd08268    12 PEVLRIEELPVPAPGAGEVLIRVEAIGLNRADA-MFRRGAYIEPPP-LPARLGYEAAGVVEAVGAGVTGFAVGDRVSVIP 89
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 7-346 5.89e-10

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 59.91  E-value: 5.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   7 CLVIHA---PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLhyFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVR 83
Cdd:cd08275     2 AVVLTGfggLDKLKVEKEALPEPSSGEVRVRVEACGLNFADL--MARQGLYDSAPKPPFVPGFECAGTVEAVGEGVKDFK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  84 IGDKVavnpsrpcgackFCLeglpnqcldMRFygsamrtphvqGAFRNMLLCEATQCVKVADHVPLRLAAlAEPFS---- 159
Cdd:cd08275    80 VGDRV------------MGL---------TRF-----------GGYAEVVNVPADQVFPLPDGMSFEEAA-AFPVNylta 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 160 -VGLHGVSRAGPllGKRVLV----SGCG-----------PIGVLAiaaarahgaaeiTATDVVDEPLaiaRAMGADNTIN 223
Cdd:cd08275   127 yYALFELGNLRP--GQSVLVhsaaGGVGlaagqlcktvpNVTVVG------------TASASKHEAL---KENGVTHVID 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 224 -VAQDKTWVARHSADKGtFDVMLECSGNErALRDGLEVMRPRGVVVQLGL-----GGDVSI--------------PQNMV 283
Cdd:cd08275   190 yRTQDYVEEVKKISPEG-VDIVLDALGGE-DTRKSYDLLKPMGRLVVYGAanlvtGEKRSWfklakkwwnrpkvdPMKLI 267

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1543036938 284 VAKeLSICG---SFRFH------AEFALAVKLINEGRVDlsPVVSHTFPMLQARQAFELASDRQKAMKVLID 346
Cdd:cd08275   268 SEN-KSVLGfnlGWLFEerelltEVMDKLLKLYEEGKIK--PKIDSVFPFEEVGEAMRRLQSRKNIGKVVLT 336
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 60-345 5.91e-10

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: 59.51  E-value: 5.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  60 EPMVLGHEVAGTVVAVAPGVESVRIGDKVAvnpsrpcgackfcleGLpnqcldmrfygsamrtphVQGAFRNMLLCEATQ 139
Cdd:cd05195    27 DETPLGLECSGIVTRVGSGVTGLKVGDRVM---------------GL------------------APGAFATHVRVDARL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 140 CVKVADHVPLRLAA-LAEPFSVGLHGVSRAGPL-LGKRVLV-SGCGPIGvlaiaaarahgaaeITAtdvvdepLAIARAM 216
Cdd:cd05195    74 VVKIPDSLSFEEAAtLPVAYLTAYYALVDLARLqKGESVLIhAAAGGVG--------------QAA-------IQLAQHL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 217 GAD---------------------------NTINVAQDktwVARHSADKGtFDVMLeCSGNERALRDGLEVMRPRGVVVQ 269
Cdd:cd05195   133 GAEvfatvgseekreflrelggpvdhifssRDLSFADG---ILRATGGRG-VDVVL-NSLSGELLRASWRCLAPFGRFVE 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 270 LGLGGdvsIPQNMVVAKELSICG-SF--------------RFHAEFALAVKLINEGRvdLSPVVSHTFPMLQARQAFELA 334
Cdd:cd05195   208 IGKRD---ILSNSKLGMRPFLRNvSFssvdldqlarerpeLLRELLREVLELLEAGV--LKPLPPTVVPSASEIDAFRLM 282

                         330
                  ....*....|.
gi 1543036938 335 SDRQKAMKVLI 345
Cdd:cd05195   283 QSGKHIGKVVL 293
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 12-345 1.07e-09

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


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 58.92  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  12 APDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVN 91
Cdd:cd08244    11 PPEVLVPEDVPDPVPGPGQVRIAVAAAGVHFVDTQLRSGWGPGPFPPELPYVPGGEVAGVVDAVGPGVDPAWLGRRVVAH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  92 PSRPCGackfcleglpnqcldmrfyGSAMRTphvqgafrnmlLCEATQCVKVADHVPLRLA-ALAEPFSVGLHGVSRAGP 170
Cdd:cd08244    91 TGRAGG-------------------GYAELA-----------VADVDSLHPVPDGLDLEAAvAVVHDGRTALGLLDLATL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 171 LLGKRVLV-SGCGPIGVLAIAAARAHGAAEITATDVvDEPLAIARAMGADNTINvAQDKTW--VARHSADKGTFDVMLEC 247
Cdd:cd08244   141 TPGDVVLVtAAAGGLGSLLVQLAKAAGATVVGAAGG-PAKTALVRALGADVAVD-YTRPDWpdQVREALGGGGVTVVLDG 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGNERAlRDGLEVMRPRGVVVQLGL--GGDVSIPQNMVVAKELSICGSF-------RFHAEFALAVKLINEGRvdLSPVV 318
Cdd:cd08244   219 VGGAIG-RAALALLAPGGRFLTYGWasGEWTALDEDDARRRGVTVVGLLgvqaergGLRALEARALAEAAAGR--LVPVV 295

                         330       340
                  ....*....|....*....|....*..
gi 1543036938 319 SHTFPMLQARQAFELASDRQKAMKVLI 345
Cdd:cd08244   296 GQTFPLERAAEAHAALEARSTVGKVLL 322
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 17-324 2.16e-09

crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase/reductase family, catalyzes the NADPH-dependent conversion of crotonyl-CoA to butyryl-CoA, a step in (2S)-methylmalonyl-CoA production for straight-chain fatty acid biosynthesis. Like enoyl reductase, another enzyme in fatty acid synthesis, crotonyl-CoA reductase is a member of the zinc-dependent alcohol dehydrogenase-like medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 58.20  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  17 RLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFGTV-------RIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVA 89
Cdd:cd08246    31 QLEDVPVPELGPGEVLVAVMAAGVNYNNVWAALGEPVSTFaarqrrgRDEPYHIGGSDASGIVWAVGEGVKNWKVGDEVV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  90 VNPSRPCGACKFCLEGLPNQCLDMRFYGsaMRTPHvqGAFRNMLLCEATQCVKVADHvpLRLAALAEPFSVG------LH 163
Cdd:cd08246   111 VHCSVWDGNDPERAGGDPMFDPSQRIWG--YETNY--GSFAQFALVQATQLMPKPKH--LSWEEAAAYMLVGatayrmLF 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 164 GVSRAGPLLGKRVLVSG-CGPIGVLAIAAARAHGAAEITatdVV--DEPLAIARAMGADNTINVAQDKTWVAR--HSADK 238
Cdd:cd08246   185 GWNPNTVKPGDNVLIWGaSGGLGSMAIQLARAAGANPVA---VVssEEKAEYCRALGAEGVINRRDFDHWGVLpdVNSEA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 239 GTFDV---------MLECSGNERALRDGLE------------VMRPRGVVVQLG--LGGDVSIPQNMVVAKELSICGSFR 295
Cdd:cd08246   262 YTAWTkearrfgkaIWDILGGREDPDIVFEhpgratfptsvfVCDRGGMVVICAgtTGYNHTYDNRYLWMRQKRIQGSHF 341

                         330       340       350
                  ....*....|....*....|....*....|
gi 1543036938 296 FHAEFALAV-KLINEGRVDlsPVVSHTFPM 324
Cdd:cd08246   342 ANDREAAEAnRLVMKGRID--PCLSKVFSL 369
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 25-110 2.75e-09

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 57.88  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  25 EIGPGQVLVKVGMGGICGSDLHYFHNGGFGTvriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNP-SRPCGACKFCL 103
Cdd:PLN02514   31 KTGPEDVVIKVIYCGICHTDLHQIKNDLGMS---NYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGViVGCCGECSPCK 107


                  ....*..
gi 1543036938 104 EGLPNQC 110
Cdd:PLN02514  108 SDLEQYC 114
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 8-153 5.03e-09

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: 56.82  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHAPDDLRLDEQDAG--EIGPGQVLVKVGMGGICGSDLHYFHNGgfgtVRIKEPMVLGHEVAGTVVAVAPGVESVRIG 85
Cdd:cd08249     4 AVLTGPGGGLLVVVDVPvpKPGPDEVLVKVKAVALNPVDWKHQDYG----FIPSYPAILGCDFAGTVVEVGSGVTRFKVG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1543036938  86 DKVavnpsrpCGACkfcleglpnqcldmrfYGSAMRTPHvQGAFRNMLLCEATQCVKVADHVPLRLAA 153
Cdd:cd08249    80 DRV-------AGFV----------------HGGNPNDPR-NGAFQEYVVADADLTAKIPDNISFEEAA 123
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 25-272 1.33e-08

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 55.80  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  25 EIGPGQVLVKVGMGGICGSDLHYFHNG-GFGtvriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNP-SRPCGACKFC 102
Cdd:PLN02178   28 ENGENDVTVKILFCGVCHSDLHTIKNHwGFS----RYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGViIGSCQSCESC 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 103 LEGLPNQCLDMRFYGSAMRTPHV--QGAFRNMLLCEATQCVKVADHV------PLRLAALAEPFSVGLHGVSRAGpllGK 174
Cdd:PLN02178  104 NQDLENYCPKVVFTYNSRSSDGTrnQGGYSDVIVVDHRFVLSIPDGLpsdsgaPLLCAGITVYSPMKYYGMTKES---GK 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 175 RVLVSGCGPIG-VLAIAAARAHGAAEITATDVVDEPLAIARaMGADNTINVAQDKtwvaRHSADKGTFDVMLECSGNERA 253
Cdd:PLN02178  181 RLGVNGLGGLGhIAVKIGKAFGLRVTVISRSSEKEREAIDR-LGADSFLVTTDSQ----KMKEAVGTMDFIIDTVSAEHA 255

                         250
                  ....*....|....*....
gi 1543036938 254 LRDGLEVMRPRGVVVQLGL 272
Cdd:PLN02178  256 LLPLFSLLKVSGKLVALGL 274
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 6-90 1.36e-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: 55.69  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   6 MCLVIHAPDD------LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHyFHNGGFGTVRiKEPMVLGHEVAGTVVAVAPGV 79
Cdd:cd08291     2 KALLLEEYGKplevkeLSLPEPEVPEPGPGEVLIKVEAAPINPSDLG-FLKGQYGSTK-ALPVPPGFEGSGTVVAAGGGP 79

                          90
                  ....*....|..
gi 1543036938  80 ESVR-IGDKVAV 90
Cdd:cd08291    80 LAQSlIGKRVAF 91
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 28-333 1.44e-08

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: 55.76  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  28 PGQVLVKVGMGGICGSDLhYFHNGGFGTVRIkePMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRPCGACKFCLEGLP 107
Cdd:cd08301    27 AMEVRIKILHTSLCHTDV-YFWEAKGQTPLF--PRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGECKECRHCKSEKS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 108 NQC-------------LDM--RFYGSAMRTPHVQG--AFRNMLLCEATQCVKVADHVPL-RLAALAEPFSVGLHGVSR-A 168
Cdd:cd08301   104 NMCdllrintdrgvmiNDGksRFSINGKPIYHFVGtsTFSEYTVVHVGCVAKINPEAPLdKVCLLSCGVSTGLGAAWNvA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 169 GPLLGKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTIN----------VAQDKTwvarhsadK 238
Cdd:cd08301   184 KVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKFGVTEFVNpkdhdkpvqeVIAEMT--------G 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 239 GTFDVMLECSGNERALRDGLEVMRPR-GVVVQLGL-GGDVSIPQN-MVVAKELSICGSF----RFHAEFALAVKLINEGR 311
Cdd:cd08301   256 GGVDYSFECTGNIDAMISAFECVHDGwGVTVLLGVpHKDAVFSTHpMNLLNGRTLKGTLfggyKPKTDLPNLVEKYMKKE 335

                         330       340
                  ....*....|....*....|..
gi 1543036938 312 VDLSPVVSHTFPMLQARQAFEL 333
Cdd:cd08301   336 LELEKFITHELPFSEINKAFDL 357
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 57-345 1.23e-07

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 52.39  E-value: 1.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   57 RIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAvnpsrpcgackfcleGLpnqcldmrfygsamrtphVQGAFRNMLLCE 136
Cdd:smart00829  19 LYPGEAVLGGECAGVVTRVGPGVTGLAVGDRVM---------------GL------------------APGAFATRVVTD 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  137 ATQCVKVADHVPLRLAAlaepfSV---------GLHGVSRAGPllGKRVLV-SGCGPIGvlaiaaarahgaaeITAtdvv 206
Cdd:smart00829  66 ARLVVPIPDGWSFEEAA-----TVpvvfltayyALVDLARLRP--GESVLIhAAAGGVG--------------QAA---- 120

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  207 depLAIARAMGAD--------------NTINVAQD----------KTWVARHSADKGtFDVMLECSGNErALRDGLEVMR 262
Cdd:smart00829 121 ---IQLARHLGAEvfatagspekrdflRALGIPDDhifssrdlsfADEILRATGGRG-VDVVLNSLSGE-FLDASLRCLA 195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  263 PRGVVVQLGLgGDVSIPQNMVVAKELSiCGSF-------------RFHAEFALAVKLINEGRvdLSPVVSHTFPMLQARQ 329
Cdd:smart00829 196 PGGRFVEIGK-RDIRDNSQLAMAPFRP-NVSYhavdldaleegpdRIRELLAEVLELFAEGV--LRPLPVTVFPISDAED 271

                          330
                   ....*....|....*.
gi 1543036938  330 AFELASDRQKAMKVLI 345
Cdd:smart00829 272 AFRYMQQGKHIGKVVL 287
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 13-333 1.12e-06

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 49.57  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  13 PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLhyFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAvnp 92
Cdd:cd08273    12 PEVLKVVEADLPEPAAGEVVVKVEASGVSFADV--QMRRGLYPDQPPLPFTPGYDLVGRVDALGSGVTGFEVGDRVA--- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  93 srpcgackfcleglpnqCLDMRfygsamrtphvqGAFRNMLLCEATQCVKVADHVPLR-LAALAEPFSVG---LHGVSRa 168
Cdd:cd08273    87 -----------------ALTRV------------GGNAEYINLDAKYLVPVPEGVDAAeAVCLVLNYVTAyqmLHRAAK- 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 169 gPLLGKRVLVSGC-GPIGvLAIAAARAHGAAEITATdVVDEPLAIARAMGAdnTINVAQDKTWVARHSADKGtFDVMLEC 247
Cdd:cd08273   137 -VLTGQRVLIHGAsGGVG-QALLELALLAGAEVYGT-ASERNHAALRELGA--TPIDYRTKDWLPAMLTPGG-VDVVFDG 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 248 SGnERALRDGLEVMRPRGVVVQLG-----LGGDVSIPQNMVVAKELSICGSF--------------------RFHAEFAL 302
Cdd:cd08273   211 VG-GESYEESYAALAPGGTLVCYGgnsslLQGRRSLAALGSLLARLAKLKLLptgrratfyyvwrdraedpkLFRQDLTE 289

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1543036938 303 AVKLINEGRvdLSPVVSHTFPMLQARQAFEL 333
Cdd:cd08273   290 LLDLLAKGK--IRPKIAKRLPLSEVAEAHRL 318
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 28-346 1.16e-06

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


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 49.91  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  28 PGQVLVKV--------------GMGGICGSDLHYFHNGGFGTVRIkePMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPS 93
Cdd:cd08248    29 PNQVLIKVhaasvnpidvlmrsGYGRTLLNKKRKPQSCKYSGIEF--PLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAVP 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  94 rpcgackfcleglpnqcldmrfygsamrtPHVQGAFRNMLLCEATQCVKVADHVPLRLAAlAEPFsVGL--------HGV 165
Cdd:cd08248   107 -----------------------------PWSQGTHAEYVVVPENEVSKKPKNLSHEEAA-SLPY-AGLtawsalvnVGG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 166 SRAGPLLGKRVLV-SGCGPIGVLaIAAARAHGAAEITAT---DVVDeplaIARAMGADNTINvaQDKTWVARHSADKGTF 241
Cdd:cd08248   156 LNPKNAAGKRVLIlGGSGGVGTF-AIQLLKAWGAHVTTTcstDAIP----LVKSLGADDVID--YNNEDFEEELTERGKF 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 242 DVMLECSGNERAlRDGLEVMRPRGVVV-----------QLGLGGdvSIPQNMVVAKELSICGSFR--------FH-AEFA 301
Cdd:cd08248   229 DVILDTVGGDTE-KWALKLLKKGGTYVtlvspllkntdKLGLVG--GMLKSAVDLLKKNVKSLLKgshyrwgfFSpSGSA 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1543036938 302 LA--VKLINEGRvdLSPVVSHTFPMLQARQAFELASDRQKAMKVLID 346
Cdd:cd08248   306 LDelAKLVEDGK--IKPVIDKVFPFEEVPEAYEKVESGHARGKTVIK 350
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
217-345 1.38e-06

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 46.94  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 217 GADNTINVAQdkTWVARHSADKGtFDVMLECSGNErALRDGLEVMRPRGVVVQLGLGGDVSIPqnMVVAKELS------- 289
Cdd:pfam13602   2 GADEVIDYRT--TDFVQATGGEG-VDVVLDTVGGE-AFEASLRVLPGGGRLVTIGGPPLSAGL--LLPARKRGgrgvkyl 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1543036938 290 --ICGSFRFHAEFALAVKLINEGRvdLSPVVSHTFPMLQARQAFELASDRQKAMKVLI 345
Cdd:pfam13602  76 flFVRPNLGADILQELADLIEEGK--LRPVIDRVFPLEEAAEAHRYLESGRARGKIVL 131
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 27-89 3.14e-06

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: 48.41  E-value: 3.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543036938  27 GPGQVLVKVGMGGICGSDLHYFHNGGFGTVriKEPMVLGHEVAGTVVAVAPGVESVRIGDKVA 89
Cdd:cd08250    29 GPGEVLVKNRFVGINASDINFTAGRYDPGV--KPPFDCGFEGVGEVVAVGEGVTDFKVGDAVA 89
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 8-345 4.05e-06

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: 47.99  E-value: 4.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938   8 LVIHA---PDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYfHNGGFGTVriKEPMVLGHEVAGTVVAvAPGVEsVRI 84
Cdd:cd08243     4 IVIEQpggPEVLKLREIPIPEPKPGWVLIRVKAFGLNRSEIFT-RQGHSPSV--KFPRVLGIEAVGEVEE-APGGT-FTP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  85 GDKVAVnpsrpcgackfcleglpnqcldmrFYGSAMRTphVQGAFRNMLLCEATQCVKVADHVPL-RLAALAEPFSV--- 160
Cdd:cd08243    79 GQRVAT------------------------AMGGMGRT--FDGSYAEYTLVPNEQVYAIDSDLSWaELAALPETYYTawg 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 161 ---GLHGVSRagpllGKRVLVSGcGPIGV-LAIAAARAHGAAEITATDVVDEPLAIARAMGADNtinVAQDKTWVARH-S 235
Cdd:cd08243   133 slfRSLGLQP-----GDTLLIRG-GTSSVgLAALKLAKALGATVTATTRSPERAALLKELGADE---VVIDDGAIAEQlR 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 236 ADKGTFDVMLECSGNErALRDGLEVMRPRGVVVQLG-LGGDVSIP-----QNMVVAKELSICGSFRFH-AEFALA--VKL 306
Cdd:cd08243   204 AAPGGFDKVLELVGTA-TLKDSLRHLRPGGIVCMTGlLGGQWTLEdfnpmDDIPSGVNLTLTGSSSGDvPQTPLQelFDF 282

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1543036938 307 INEGRVDLSPvvSHTFPMLQARQAFELASDRQKAMKVLI 345
Cdd:cd08243   283 VAAGHLDIPP--SKVFTFDEIVEAHAYMESNRAFGKVVV 319
PLN02827 PLN02827
Alcohol dehydrogenase-like
 16-223 4.87e-06

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 47.97  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  16 LRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGFgtvrikEPMVLGHEVAGTVVAVAPGVESVRIGDKVAVNPSRP 95
Cdd:PLN02827   25 LVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWESQAL------FPRIFGHEASGIVESIGEGVTEFEKGDHVLTVFTGE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  96 CGACKFCLEGLPNQC--LDMRFYG---SAMRTP-HVQG----------AFRNMLLCEATQCVKVADHVPL-RLAALAEPF 158
Cdd:PLN02827   99 CGSCRHCISGKSNMCqvLGLERKGvmhSDQKTRfSIKGkpvyhycavsSFSEYTVVHSGCAVKVDPLAPLhKICLLSCGV 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1543036938 159 SVGLHGVSRAGPLL-GKRVLVSGCGPIGVLAIAAARAHGAAEITATDVVDEPLAIARAMGADNTIN 223
Cdd:PLN02827  179 AAGLGAAWNVADVSkGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFIN 244
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 12-90 6.99e-06

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 47.27  E-value: 6.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543036938  12 APDDLRLDEQDAGEIGPGQVLVKVGMGGICGSDlhyFHNGGFGTVRIKEPMVLGHEVAGTVVAVAPGVESVRIGDKVAV 90
Cdd:cd08271    11 AALQLTLEEIEIPGPGAGEVLVKVHAAGLNPVD---WKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKVGDRVAY 86
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
175-347 8.00e-05

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 43.09  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 175 RVLVSGCGPIGVLAIAAARAHGAAEIT----ATDVVDEPLAIARAMGAdntINVAQDKTWVARHSADKGTFDVMLECSGN 250
Cdd:pfam16912  33 SALVLGNGPLGLLALAMLRVQRGFDRVyclgRRDRPDPTIDLVEELGA---TYVDSRETPVDEIPAAHEPMDLVYEATGY 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938 251 ERALRDGLEVMRPRGVVVQLGLGGDVSIP------QNMVVAKELSICGSFRFH-AEFALAVKLINEGRVD-LSPVVSHTF 322
Cdd:pfam16912 110 APHAFEAIDALAPNGVAALLGVPTSWTFEidggalHRELVLHNKALVGSVNANrRHFEAAADTLAAAPEWfLDALVTGVV 189

                         170       180
                  ....*....|....*....|....*
gi 1543036938 323 PMLQARQAFElasDRQKAMKVLIDF 347
Cdd:pfam16912 190 PLDEFEEAFE---DGDDDIKTVVEF 211
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 13-94 1.68e-04

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: 43.09  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  13 PDD-LRLDEQDAGEIGPGQVLVKVGMGGIcgsdlhyfHNGGFGTVRIK------EPMVLGHEVAGTVVAVAPGVESVRIG 85
Cdd:cd08292    12 PADvLEIGEVPKPTPGAGEVLVRTTLSPI--------HNHDLWTIRGTygykpeLPAIGGSEAVGVVDAVGEGVKGLQVG 83


                  ....*....
gi 1543036938  86 DKVAVNPSR 94
Cdd:cd08292    84 QRVAVAPVH 92
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 15-92 1.72e-03

L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, catalyzes the NADPH-dependent conversion of l-sorbose 1-phosphate to d-glucitol 6-phosphate in the metabolism of L-sorbose to (also converts d-fructose 1-phosphate to d-mannitol 6-phosphate). 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.


Pssm-ID: 176200 [Multi-domain]  Cd Length: 410  Bit Score: 40.12  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543036938  15 DLRLDEQDAGEIGPGQVLVKVGMGGICGSDLHYFHNGGfGTVRI-----KEPMVLGHEVAGTVVAVAPGVES-VRIGDKV 88
Cdd:cd08238    13 DLRLEKFELPEIADDEILVRVISDSLCFSTWKLALQGS-DHKKVpndlaKEPVILGHEFAGTILKVGKKWQGkYKPGQRF 91


                  ....
gi 1543036938  89 AVNP 92
Cdd:cd08238    92 VIQP 95
 
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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