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Conserved domains on  [gi|15235757|ref|NP_195510|]
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cinnamyl alcohol dehydrogenase 6 [Arabidopsis thaliana]

Protein Classification

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

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

EC:  1.1.-.-
Gene Ontology:  GO:0016491

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
15-353 0e+00

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: 510.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  15 FGWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDK 94
Cdd:cd05283   1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  95 VGVGCIVDSCRTCESCREDQENYCTKAIATYNGVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYS 174
Cdd:cd05283  81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITVYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 175 PMKYFGlTGPDKHvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMGTMDGIID 254
Cdd:cd05283 161 PLKRNG-VGPGKRvgvvgigglgHLAVKFAKALGAEVTAFSRSPSKKEDALK-LGADEFIATKDPEAMKKAAGSLDLIID 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 255 TVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYV 334
Cdd:cd05283 239 TVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGI 318
                       330
                ....*....|....*....
gi 15235757 335 NTAMDRLAKGDVRYRFVID 353
Cdd:cd05283 319 NEALERLEKGDVRYRFVLD 337
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
15-353 0e+00

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: 510.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  15 FGWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDK 94
Cdd:cd05283   1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  95 VGVGCIVDSCRTCESCREDQENYCTKAIATYNGVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYS 174
Cdd:cd05283  81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITVYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 175 PMKYFGlTGPDKHvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMGTMDGIID 254
Cdd:cd05283 161 PLKRNG-VGPGKRvgvvgigglgHLAVKFAKALGAEVTAFSRSPSKKEDALK-LGADEFIATKDPEAMKKAAGSLDLIID 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 255 TVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYV 334
Cdd:cd05283 239 TVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGI 318
                       330
                ....*....|....*....
gi 15235757 335 NTAMDRLAKGDVRYRFVID 353
Cdd:cd05283 319 NEALERLEKGDVRYRFVLD 337
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
5-359 0e+00

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 508.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    5 SGEKEQSVEAFGWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGN 84
Cdd:PLN02586   4 SPEEEHPQKAFGWAARDPSGVLSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   85 KVSKFNLGDKVGVGCIVDSCRTCESCREDQENYCTKAIATYNGVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAP 164
Cdd:PLN02586  84 NVKKFKEGDRVGVGVIVGSCKSCESCDQDLENYCPKMIFTYNSIGHDGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  165 LLCAGISMYSPMKYFGLTGPDKHVGIVGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDTLGADGFLVSTDEDQMKA 244
Cdd:PLN02586 164 LLCAGITVYSPMKYYGMTEPGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSFLVSTDPEKMKA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  245 AMGTMDGIIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKA 324
Cdd:PLN02586 244 AIGTMDYIIDTVSAVHALGPLLGLLKVNGKLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITA 323
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 15235757  325 EIEIISMDYVNTAMDRLAKGDVRYRFVIDISNTLA 359
Cdd:PLN02586 324 DIELIRMDEINTAMERLAKSDVRYRFVIDVANSLS 358
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
16-353 6.93e-136

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 390.24  E-value: 6.93e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  16 GWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKV 95
Cdd:COG1064   3 AAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDRV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  96 GVGCiVDSCRTCESCREDQENYCTKAIATynGVHHDGtinygGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSP 175
Cdd:COG1064  83 GVGW-VDSCGTCEYCRSGRENLCENGRFT--GYTTDG-----GYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 176 MKYFGLT-------------GpdkhvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQM 242
Cdd:COG1064 155 LRRAGVGpgdrvavigagglG--------------HLAVQIAKALGAEVIAVDRSPEKLELARE-LGADHVVNSSDEDPV 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 243 KAAMG--TMDGIIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEH 320
Cdd:COG1064 220 EAVREltGADVVIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEG 299
                       330       340       350
                ....*....|....*....|....*....|...
gi 15235757 321 GIKAEIEIISMDYVNTAMDRLAKGDVRYRFVID 353
Cdd:COG1064 300 KIKPEVETIPLEEANEALERLRAGKVRGRAVLD 332
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
40-152 7.24e-34

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: 120.79  E-value: 7.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    40 EVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQENYCT 119
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNLCP 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 15235757   120 KaiATYNGVHHDgtinyGGYSDHIVVDERYAVK 152
Cdd:pfam08240  81 N--GRFLGYDRD-----GGFAEYVVVPERNLVP 106
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
28-344 2.22e-26

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized. [Energy metabolism, Fermentation]


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 107.31  E-value: 2.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    28 PFVFSRRKT---GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVDSC 104
Cdd:TIGR02822  14 PLRFVERPVprpGPGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWLRRTC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   105 RTCESCREDQENYCTKAiaTYNGVHHDGtinygGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMY--------SPM 176
Cdd:TIGR02822  94 GVCRYCRRGAENLCPAS--RYTGWDTDG-----GYAEYTTVPAAFAYRLPTGYDDVELAPLLCAGIIGYrallraslPPG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   177 KYFGLTGpdkhvgivgLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALdTLGADGFLVSTDEDQMKaamgtMDGIIDTV 256
Cdd:TIGR02822 167 GRLGLYG---------FGGSAHLTAQVALAQGATVHVMTRGAAARRLAL-ALGAASAGGAYDTPPEP-----LDAAILFA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   257 SASHSISPLIGLLKSNGKLVLLGA--TEKPfDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYV 334
Cdd:TIGR02822 232 PAGGLVPPALEALDRGGVLAVAGIhlTDTP-PLNYQRHLFYERQIRSVTSNTRADAREFLELAAQHGVRVTTHTYPLSEA 310
                         330
                  ....*....|
gi 15235757   335 NTAMDRLAKG 344
Cdd:TIGR02822 311 DRALRDLKAG 320
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
15-353 0e+00

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: 510.89  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  15 FGWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDK 94
Cdd:cd05283   1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  95 VGVGCIVDSCRTCESCREDQENYCTKAIATYNGVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYS 174
Cdd:cd05283  81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITVYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 175 PMKYFGlTGPDKHvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMGTMDGIID 254
Cdd:cd05283 161 PLKRNG-VGPGKRvgvvgigglgHLAVKFAKALGAEVTAFSRSPSKKEDALK-LGADEFIATKDPEAMKKAAGSLDLIID 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 255 TVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYV 334
Cdd:cd05283 239 TVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGI 318
                       330
                ....*....|....*....
gi 15235757 335 NTAMDRLAKGDVRYRFVID 353
Cdd:cd05283 319 NEALERLEKGDVRYRFVLD 337
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
5-359 0e+00

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 508.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    5 SGEKEQSVEAFGWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGN 84
Cdd:PLN02586   4 SPEEEHPQKAFGWAARDPSGVLSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   85 KVSKFNLGDKVGVGCIVDSCRTCESCREDQENYCTKAIATYNGVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAP 164
Cdd:PLN02586  84 NVKKFKEGDRVGVGVIVGSCKSCESCDQDLENYCPKMIFTYNSIGHDGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAP 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  165 LLCAGISMYSPMKYFGLTGPDKHVGIVGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDTLGADGFLVSTDEDQMKA 244
Cdd:PLN02586 164 LLCAGITVYSPMKYYGMTEPGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSFLVSTDPEKMKA 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  245 AMGTMDGIIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKA 324
Cdd:PLN02586 244 AIGTMDYIIDTVSAVHALGPLLGLLKVNGKLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITA 323
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 15235757  325 EIEIISMDYVNTAMDRLAKGDVRYRFVIDISNTLA 359
Cdd:PLN02586 324 DIELIRMDEINTAMERLAKSDVRYRFVIDVANSLS 358
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
6-355 6.93e-149

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 424.21  E-value: 6.93e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    6 GEKEQSVEAFGWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNK 85
Cdd:PLN02514   2 GSLEAEKKTTGWAARDPSGHLSPYTYTLRKTGPEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   86 VSKFNLGDKVGVGCIVDSCRTCESCREDQENYCTKAIATYNGVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPL 165
Cdd:PLN02514  82 VSKFTVGDIVGVGVIVGCCGECSPCKSDLEQYCNKRIWSYNDVYTDGKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  166 LCAGISMYSPMKYFGLTGPDKHVGIVGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDTLGADGFLVSTDEDQMKAA 245
Cdd:PLN02514 162 LCAGVTVYSPLSHFGLKQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGADDYLVSSDAAEMQEA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  246 MGTMDGIIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAE 325
Cdd:PLN02514 242 ADSLDYIIDTVPVFHPLEPYLSLLKLDGKLILMGVINTPLQFVTPMLMLGRKVITGSFIGSMKETEEMLEFCKEKGLTSM 321
                        330       340       350
                 ....*....|....*....|....*....|
gi 15235757  326 IEIISMDYVNTAMDRLAKGDVRYRFVIDIS 355
Cdd:PLN02514 322 IEVVKMDYVNTAFERLEKNDVRYRFVVDVA 351
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
13-363 4.25e-146

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 417.89  E-value: 4.25e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   13 EAFGWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLG 92
Cdd:PLN02178   6 KAFGWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   93 DKVGVGCIVDSCRTCESCREDQENYCTKAIATYNGVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISM 172
Cdd:PLN02178  86 DRVGVGVIIGSCQSCESCNQDLENYCPKVVFTYNSRSSDGTRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  173 YSPMKYFGLTGPD-KHVGIVGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDTLGADGFLVSTDEDQMKAAMGTMDG 251
Cdd:PLN02178 166 YSPMKYYGMTKESgKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDF 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  252 IIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISM 331
Cdd:PLN02178 246 IIDTVSAEHALLPLFSLLKVSGKLVALGLPEKPLDLPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKM 325
                        330       340       350
                 ....*....|....*....|....*....|..
gi 15235757  332 DYVNTAMDRLAKGDVRYRFVIDISNTLAATRS 363
Cdd:PLN02178 326 SDINSAMDRLAKSDVRYRFVIDVANSLLPESS 357
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
16-353 6.93e-136

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 390.24  E-value: 6.93e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  16 GWAARDSSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKV 95
Cdd:COG1064   3 AAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDRV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  96 GVGCiVDSCRTCESCREDQENYCTKAIATynGVHHDGtinygGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSP 175
Cdd:COG1064  83 GVGW-VDSCGTCEYCRSGRENLCENGRFT--GYTTDG-----GYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITAYRA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 176 MKYFGLT-------------GpdkhvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQM 242
Cdd:COG1064 155 LRRAGVGpgdrvavigagglG--------------HLAVQIAKALGAEVIAVDRSPEKLELARE-LGADHVVNSSDEDPV 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 243 KAAMG--TMDGIIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEH 320
Cdd:COG1064 220 EAVREltGADVVIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEG 299
                       330       340       350
                ....*....|....*....|....*....|...
gi 15235757 321 GIKAEIEIISMDYVNTAMDRLAKGDVRYRFVID 353
Cdd:COG1064 300 KIKPEVETIPLEEANEALERLRAGKVRGRAVLD 332
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
17-352 1.81e-132

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: 381.67  E-value: 1.81e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  17 WAARD--SSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDK 94
Cdd:cd08245   1 KAAVVhaAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  95 VGVGCIVDSCRTCESCREDQENYCTKAIATyngvhhdGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYS 174
Cdd:cd08245  81 VGVGWLVGSCGRCEYCRRGLENLCQKAVNT-------GYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 175 PMKYFGLtGPDKHVGIVGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMGTMDGIID 254
Cdd:cd08245 154 ALRDAGP-RPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARK-LGADEVVDSGAELDEQAAAGGADVILV 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 255 TVSASHSISPLIGLLKSNGKLVLLGATEKP-FDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDY 333
Cdd:cd08245 232 TVVSGAAAEAALGGLRRGGRIVLVGLPESPpFSPDIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIETFPLDQ 311
                       330
                ....*....|....*....
gi 15235757 334 VNTAMDRLAKGDVRYRFVI 352
Cdd:cd08245 312 ANEAYERMEKGDVRFRFVL 330
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
37-352 1.22e-81

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: 252.17  E-value: 1.22e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVDSCRTCESCREDQEN 116
Cdd:cd08296  24 GPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGWHGGHCGTCDACRRGDFV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCTKaiATYNGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKhVGIVGLGGL 196
Cdd:cd08296 104 HCEN--GKVTGVTRD-----GGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNALRNSGAKPGDL-VAVQGIGGL 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 197 GHIGVRFAKAFGTKVTVVSSTTGKSKDALdTLGADGFLVSTDEDQMKA--AMGTMDGIIDTVSASHSISPLIGLLKSNGK 274
Cdd:cd08296 176 GHLAVQYAAKMGFRTVAISRGSDKADLAR-KLGAHHYIDTSKEDVAEAlqELGGAKLILATAPNAKAISALVGGLAPRGK 254
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15235757 275 LVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYVNTAMDRLAKGDVRYRFVI 352
Cdd:cd08296 255 LLILGAAGEPVAVSPLQLIMGRKSIHGWPSGTALDSEDTLKFSALHGVRPMVETFPLEKANEAYDRMMSGKARFRVVL 332
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
37-354 3.50e-75

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: 235.89  E-value: 3.50e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEW-HSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVDSCRTCESCREDQE 115
Cdd:cd08297  25 GPGEVLVKLEASGVCHTDLHAALGDWpVKPKLPLIGGHEGAGVVVAVGPGVSGLKVGDRVGVKWLYDACGKCEYCRTGDE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 116 NYCTKaiATYNGVHHDGTinyggYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLT------------- 182
Cdd:cd08297 105 TLCPN--QKNSGYTVDGT-----FAEYAIADARYVTPIPDGLSFEQAAPLLCAGVTVYKALKKAGLKpgdwvvisgaggg 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 183 -GpdkhvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAM-----GTMDGIIDTV 256
Cdd:cd08297 178 lG--------------HLGVQYAKAMGLRVIAIDVGDEKLELAKE-LGADAFVDFKKSDDVEAVKeltggGGAHAVVVTA 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 257 SASHSISPLIGLLKSNGKLVLLG-ATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYVN 335
Cdd:cd08297 243 VSAAAYEQALDYLRPGGTLVCVGlPPGGFIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVKPHIQVVPLEDLN 322
                       330
                ....*....|....*....
gi 15235757 336 TAMDRLAKGDVRYRFVIDI 354
Cdd:cd08297 323 EVFEKMEEGKIAGRVVVDF 341
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
31-352 1.22e-62

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: 203.18  E-value: 1.22e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  31 FSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVDSCRTCESC 110
Cdd:cd08298  22 VPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRVGVPWLGSTCGECRYC 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 111 REDQENYCTKAIATynGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLtGPDKHVGI 190
Cdd:cd08298 102 RSGRENLCDNARFT--GYTVD-----GGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRALKLAGL-KPGQRLGL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 191 VGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEdqmkaAMGTMDGIIDTVSASHSISPLIGLLK 270
Cdd:cd08298 174 YGFGASAHLALQIARYQGAEVFAFTRSGEHQELARE-LGADWAGDSDDL-----PPEPLDAAIIFAPVGALVPAALRAVK 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 271 SNGKLVLLGATEKpfDISAFS--LILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYVNTAMDRLAKGDVRY 348
Cdd:cd08298 248 KGGRVVLAGIHMS--DIPAFDyeLLWGEKTIRSVANLTRQDGEEFLKLAAEIPIKPEVETYPLEEANEALQDLKEGRIRG 325

                ....
gi 15235757 349 RFVI 352
Cdd:cd08298 326 AAVL 329
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
40-352 2.05e-54

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: 182.43  E-value: 2.05e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEW------HSSI------YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGV----GCivds 103
Cdd:cd08240  27 EVLVKVTACGVCHSDLHIWDGGYdlgggkTMSLddrgvkLPLVLGHEIVGEVVAVGPDAADVKVGDKVLVypwiGC---- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 104 cRTCESCREDQENYCTKAiatyngvHHDGTINYGGYSDHIVV-DERYaVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLT 182
Cdd:cd08240 103 -GECPVCLAGDENLCAKG-------RALGIFQDGGYAEYVIVpHSRY-LVDPGGLDPALAATLACSGLTAYSAVKKLMPL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 183 GPDKHVGIVGLGGLGHIGVRFAKAFG-TKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQ----MKAAMGTMDGIIDTVS 257
Cdd:cd08240 174 VADEPVVIIGAGGLGLMALALLKALGpANIIVVDIDEAKLEAAKA-AGADVVVNGSDPDAakriIKAAGGGVDAVIDFVN 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 258 ASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKA-EIEIISMDYVNT 336
Cdd:cd08240 253 NSATASLAFDILAKGGKLVLVGLFGGEATLPLPLLPLRALTIQGSYVGSLEELRELVALAKAGKLKPiPLTERPLSDVND 332
                       330
                ....*....|....*.
gi 15235757 337 AMDRLAKGDVRYRFVI 352
Cdd:cd08240 333 ALDDLKAGKVVGRAVL 348
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
37-352 4.86e-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: 173.13  E-value: 4.86e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHS---SIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGV-GCIvdSCRTCESCRE 112
Cdd:cd05284  24 GPGQVLVRVGGAGVCHSDLHVIDGVWGGilpYKLPFTLGHENAGWVEEVGSGVDGLKEGDPVVVhPPW--GCGTCRYCRR 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 113 DQENYCTKAIATynGVHHDGtinygGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMK-YFGLTGPDKHVGIV 191
Cdd:cd05284 102 GEENYCENARFP--GIGTDG-----GFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVKkALPYLDPGSTVVVI 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 192 GLGGLGHIGVRFAKAFgTKVTVVSstTGKSKDALD---TLGADgFLVSTDEDQMKAAMGTMDG-----IIDTVSASHSIS 263
Cdd:cd05284 175 GVGGLGHIAVQILRAL-TPATVIA--VDRSEEALKlaeRLGAD-HVLNASDDVVEEVRELTGGrgadaVIDFVGSDETLA 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 264 PLIGLLKSNGKLVLLGATEKpFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYVNTAMDRLAK 343
Cdd:cd05284 251 LAAKLLAKGGRYVIVGYGGH-GRLPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVKVEITKFPLEDANEALDRLRE 329

                ....*....
gi 15235757 344 GDVRYRFVI 352
Cdd:cd05284 330 GRVTGRAVL 338
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
37-353 1.97e-48

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: 166.27  E-value: 1.97e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNE---WHSSiyPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVgCIVDSCRTCESCRED 113
Cdd:cd08254  25 GPGEVLVKVKAAGVCHSDLHILDGGvptLTKL--PLTLGHEIAGTVVEVGAGVTNFKVGDRVAV-PAVIPCGACALCRRG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 114 QENYCTKAiatyngvHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHVGIVGL 193
Cdd:cd08254 102 RGNLCLNQ-------GMPGLGIDGGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGEVKPGETVLVIGL 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 194 GGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMGTMDGIIDT----VSASHSISPLIGLL 269
Cdd:cd08254 175 GGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKE-LGADEVLNSLDDSPKDKKAAGLGGGFDVifdfVGTQPTFEDAQKAV 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 270 KSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYVNTAMDRLAKGDVRYR 349
Cdd:cd08254 254 KPGGRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVETRPLDEIPEVLERLHKGKVKGR 333

                ....
gi 15235757 350 FVID 353
Cdd:cd08254 334 VVLV 337
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
37-353 1.01e-45

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: 159.02  E-value: 1.01e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVgCIVDSCRTCESCREDQEN 116
Cdd:cd08259  24 GPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPGDRVIL-YYYIPCGKCEYCLSGEEN 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCtKAIATYngvhhdGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCaGISM-YSPMKYFGLtGPDKHVGIVGLGG 195
Cdd:cd08259 103 LC-RNRAEY------GEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAAC-VVGTaVHALKRAGV-KKGDTVLVTGAGG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 196 LGHIG-VRFAKAFGTKvtVVSSTTGKSK-DALDTLGADGFLVSTDEDQMKAAMGTMDGIIDTVsASHSISPLIGLLKSNG 273
Cdd:cd08259 174 GVGIHaIQLAKALGAR--VIAVTRSPEKlKILKELGADYVIDGSKFSEDVKKLGGADVVIELV-GSPTIEESLRSLNKGG 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 274 KLVLLGATE-KPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIE-IISMDYVNTAMDRLAKGDVRYRFV 351
Cdd:cd08259 251 RLVLIGNVTpDPAPLRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKPVIDrVVSLEDINEALEDLKSGKVVGRIV 330

                ..
gi 15235757 352 ID 353
Cdd:cd08259 331 LK 332
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
40-316 2.23e-44

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: 154.02  E-value: 2.23e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEWHSSI-YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQENYC 118
Cdd:cd05188   1 EVLVRVEAAGLCGTDLHIRRGGYPPPPkLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNL-GCGTCELCRELCPGGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 119 TkaiatyNGVHHDGtinygGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHVGIvglgglgh 198
Cdd:cd05188  80 I------LGEGLDG-----GFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLV-------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 199 IG--------VRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMGT----MDGIIDTVSASHSISPLI 266
Cdd:cd05188 141 LGaggvgllaAQLAKAAGARVIVTDRSDEKLELAKE-LGADHVIDYKEEDLEEELRLTggggADVVIDAVGGPETLAQAL 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15235757 267 GLLKSNGKLVLLGATEKPFDISAFSLILGR-KSIAGSGIGGMQETQEMIDF 316
Cdd:cd05188 220 RLLRPGGRIVVVGGTSGGPPLDDLRRLLFKeLTIIGSTGGTREDFEEALDL 270
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
37-345 3.23e-43

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: 152.60  E-value: 3.23e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQEN 116
Cdd:COG1063  23 GPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDRVVVEPNI-PCGECRYCRRGRYN 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCTKaiATYNGVHHDGtinyGGYSDHIVVDERYAVKIPHTLPLVSAA---PLLCAgismYSPMKYFGLT----------G 183
Cdd:COG1063 102 LCEN--LQFLGIAGRD----GGFAEYVRVPAANLVKVPDGLSDEAAAlvePLAVA----LHAVERAGVKpgdtvlvigaG 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 184 PdkhvgivglgglghIG---VRFAKAFG-TKVTVVssttGKSKDALD---TLGADGFLVSTDEDQMKAAMGTMDG----- 251
Cdd:COG1063 172 P--------------IGllaALAARLAGaARVIVV----DRNPERLElarELGADAVVNPREEDLVEAVRELTGGrgadv 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 252 IIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEiEIIS- 330
Cdd:COG1063 234 VIEAVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLE-PLITh 312
                       330
                ....*....|....*...
gi 15235757 331 ---MDYVNTAMDRLAKGD 345
Cdd:COG1063 313 rfpLDDAPEAFEAAADRA 330
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
37-346 9.39e-37

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 135.98  E-value: 9.39e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWhSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQEN 116
Cdd:COG1062  15 RPGEVLVRIVAAGLCHSDLHVRDGDL-PVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHV-VLSFIPSCGHCRYCASGRPA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCTKAIAT-YNGVHHDGTINY--------------GGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMY-------- 173
Cdd:COG1062  93 LCEAGAALnGKGTLPDGTSRLssadgepvghffgqSSFAEYAVVPERSVVKVDKDVPLELAALLGCGVQTGAgavlntak 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 174 ----SPMKYFGLTGpdkhvgivglgglghIG---VRFAKAFG-TKVTVVSSTTGKSKDALdTLGADGFLVSTDEDQMKAA 245
Cdd:COG1062 173 vrpgDTVAVFGLGG---------------VGlsaVQGARIAGaSRIIAVDPVPEKLELAR-ELGATHTVNPADEDAVEAV 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 246 MGTMDG----IIDTVSASHSISPLIGLLKSNGKLVLLG--ATEKPFDISAFSLILGRKSIAGSGIGG---MQETQEMIDF 316
Cdd:COG1062 237 RELTGGgvdyAFETTGNPAVIRQALEALRKGGTVVVVGlaPPGAEISLDPFQLLLTGRTIRGSYFGGavpRRDIPRLVDL 316
                       330       340       350
                ....*....|....*....|....*....|....
gi 15235757 317 AAEHGIKAEiEIIS----MDYVNTAMDRLAKGDV 346
Cdd:COG1062 317 YRAGRLPLD-ELITrrypLDEINEAFDDLRSGEV 349
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
34-287 2.46e-34

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: 128.80  E-value: 2.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  34 RKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSiYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgvgcIVD---SCRTCESC 110
Cdd:cd08234  20 PEPGPDEVLIKVAACGICGTDLHIYEGEFGAA-PPLVPGHEFAGVVVAVGSKVTGFKVGDRV----AVDpniYCGECFYC 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 111 REDQENYCTKAIATynGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAA---PLLCA-------GISMYSPMKYFG 180
Cdd:cd08234  95 RRGRPNLCENLTAV--GVTRN-----GGFAEYVVVPAKQVYKIPDNLSFEEAAlaePLSCAvhgldllGIKPGDSVLVFG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 181 LtGPdkhvgivglgglghIGVRFAK----AFGTKVTVVSSTTGKSKDALDtLGADGFlVSTDEDQMKAAMGTM----DGI 252
Cdd:cd08234 168 A-GP--------------IGLLLAQllklNGASRVTVAEPNEEKLELAKK-LGATET-VDPSREDPEAQKEDNpygfDVV 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15235757 253 IDTVSASHSISPLIGLLKSNGKLVLLGATE-------KPFDI 287
Cdd:cd08234 231 IEATGVPKTLEQAIEYARRGGTVLVFGVYApdarvsiSPFEI 272
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
40-353 4.01e-34

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 128.61  E-value: 4.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   40 EVRVKVLYCGICHSDLHClKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVDSCRTCESCREDQENYCT 119
Cdd:PRK09422  27 EALVKMEYCGVCHTDLHV-ANGDFGDKTGRILGHEGIGIVKEVGPGVTSLKVGDRVSIAWFFEGCGHCEYCTTGRETLCR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  120 KaiatyngVHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTgPDKHVGIVGLGGLGHI 199
Cdd:PRK09422 106 S-------VKNAGYTVDGGMAEQCIVTADYAVKVPEGLDPAQASSITCAGVTTYKAIKVSGIK-PGQWIAIYGAGGLGNL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  200 GVRFAK-AFGTKVTVVSSTTGKSKDAlDTLGADGFLVSTDED----QMKAAMGTMDGIIDTVSASHSISPLIGLLKSNGK 274
Cdd:PRK09422 178 ALQYAKnVFNAKVIAVDINDDKLALA-KEVGADLTINSKRVEdvakIIQEKTGGAHAAVVTAVAKAAFNQAVDAVRAGGR 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15235757  275 LVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYVNTAMDRLAKGDVRYRFVID 353
Cdd:PRK09422 257 VVAVGLPPESMDLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQLRPLEDINDIFDEMEQGKIQGRMVID 335
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
40-152 7.24e-34

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: 120.79  E-value: 7.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    40 EVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQENYCT 119
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNLCP 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 15235757   120 KaiATYNGVHHDgtinyGGYSDHIVVDERYAVK 152
Cdd:pfam08240  81 N--GRFLGYDRD-----GGFAEYVVVPERNLVP 106
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
37-352 4.27e-32

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: 123.42  E-value: 4.27e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSiYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQEN 116
Cdd:cd08279  24 GPGEVLVRIAAAGLCHSDLHVVTGDLPAP-LPAVLGHEGAGVVEEVGPGVTGVKPGDHV-VLSWIPACGTCRYCSRGQPN 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCTKAIATYNGVHHDGT-------------INYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLC------------AGIS 171
Cdd:cd08279 102 LCDLGAGILGGQLPDGTrrftadgepvgamCGLGTFAEYTVVPEASVVKIDDDIPLDRAALLGCgvttgvgavvntARVR 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 172 MYSPMKYFGLTGpdkhvgivglgglghIG---VRFAKAFG-TKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMG 247
Cdd:cd08279 182 PGDTVAVIGCGG---------------VGlnaIQGARIAGaSRIIAVDPVPEKLELARR-FGATHTVNASEDDAVEAVRD 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 248 TMDGI-----IDTVSASHSISPLIGLLKSNGKLVLLGAT--EKPFDISAFSLILGRKSIAGSGIGGMQETQE---MIDFA 317
Cdd:cd08279 246 LTDGRgadyaFEAVGRAATIRQALAMTRKGGTAVVVGMGppGETVSLPALELFLSEKRLQGSLYGSANPRRDiprLLDLY 325
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15235757 318 AEHGIKAE---IEIISMDYVNTAMDRLAKGDVRyRFVI 352
Cdd:cd08279 326 RAGRLKLDelvTRRYSLDEINEAFADMLAGENA-RGVI 362
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
37-353 3.74e-31

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: 121.32  E-value: 3.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIyPLVPGHEIIGEVSEIGNKV---SKFNLGDKVgVGCIVDSCRTCESCRED 113
Cdd:cd08263  24 KEGEILIRVAACGVCHSDLHVLKGELPFPP-PFVLGHEISGEVVEVGPNVenpYGLSVGDRV-VGSFIMPCGKCRYCARG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 114 QENYCTKAiATYN---GVHHDGTINY-------------GGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMK 177
Cdd:cd08263 102 KENLCEDF-FAYNrlkGTLYDGTTRLfrldggpvymysmGGLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALK 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 178 YFGLTGPDKHVGIVGLGGLGHIGVRFAKAFG-TKVTVVSSTTGKSKDALdTLGADGFLVSTDED---QMKAAMGTM--DG 251
Cdd:cd08263 181 HAADVRPGETVAVIGVGGVGSSAIQLAKAFGaSPIIAVDVRDEKLAKAK-ELGATHTVNAAKEDavaAIREITGGRgvDV 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 252 IIDTVSASHSISPLIGLLKSNGKLVL--LGATEKPFDISAFSLILGRKSIAGS-GIGGMQETQEMIDFAAEHGIKAE--- 325
Cdd:cd08263 260 VVEALGKPETFKLALDVVRDGGRAVVvgLAPGGATAEIPITRLVRRGIKIIGSyGARPRQDLPELVGLAASGKLDPEalv 339
                       330       340
                ....*....|....*....|....*...
gi 15235757 326 IEIISMDYVNTAMDRLAKGDVRYRFVID 353
Cdd:cd08263 340 THKYKLEEINEAYENLRKGLIHGRAIVE 367
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
37-354 2.62e-29

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


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 115.25  E-value: 2.62e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSI-YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGvgcivdscrtcescredqe 115
Cdd:COG0604  26 GPGEVLVRVKAAGVNPADLLIRRGLYPLPPgLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA------------------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 116 nyctkaiatyngvhhdGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGI-SMYSPMKYFGLT------------ 182
Cdd:COG0604  87 ----------------GLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLtAWQALFDRGRLKpgetvlvhgaag 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 183 --GpdkhvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKsKDALDTLGADGFLVSTDED---QMKAAMG--TMDGIIDT 255
Cdd:COG0604 151 gvG--------------SAAVQLAKALGARVIATASSPEK-AELLRALGADHVIDYREEDfaeRVRALTGgrGVDVVLDT 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 256 VSASHsISPLIGLLKSNGKLVLLG-ATEKPFDISAFSLILGRKSIAGSGIGGMQET------QEMIDFAAEHGIKAEI-E 327
Cdd:COG0604 216 VGGDT-LARSLRALAPGGRLVSIGaASGAPPPLDLAPLLLKGLTLTGFTLFARDPAerraalAELARLLAAGKLRPVIdR 294
                       330       340
                ....*....|....*....|....*..
gi 15235757 328 IISMDYVNTAMDRLAKGDVRYRFVIDI 354
Cdd:COG0604 295 VFPLEEAAEAHRLLESGKHRGKVVLTV 321
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
35-325 5.69e-29

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


Pssm-ID: 176195 [Multi-domain]  Cd Length: 351  Bit Score: 114.94  E-value: 5.69e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLH-------CLKNEWHSSI----YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIvDS 103
Cdd:cd08233  21 PVKPGEVKIKVAWCGICGSDLHeyldgpiFIPTEGHPHLtgetAPVTLGHEFSGVVVEVGSGVTGFKVGDRVVVEPT-IK 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 104 CRTCESCREDQENYCtkaiaTYNGVHHDGTINyGGYSDHIVVDERYAVKIPHTLPLVSAA---PL-------LCAGISMY 173
Cdd:cd08233 100 CGTCGACKRGLYNLC-----DSLGFIGLGGGG-GGFAEYVVVPAYHVHKLPDNVPLEEAAlvePLavawhavRRSGFKPG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 174 SPMKYFGLtGPdkhvgivglgglghIG---VRFAKAFGTKVTVVSSTTGKSKDALDTLGADGFLVSTDEDQMKAAM---- 246
Cdd:cd08233 174 DTALVLGA-GP--------------IGlltILALKAAGASKIIVSEPSEARRELAEELGATIVLDPTEVDVVAEVRkltg 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 247 -GTMDGIIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSgIGGMQET-QEMIDFAAEHGIKA 324
Cdd:cd08233 239 gGGVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGS-ICYTREDfEEVIDLLASGKIDA 317

                .
gi 15235757 325 E 325
Cdd:cd08233 318 E 318
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
37-348 5.85e-29

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: 114.63  E-value: 5.85e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWhSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQEN 116
Cdd:cd08236  23 GPGEVLVKVKACGICGSDIPRYLGTG-AYHPPLVLGHEFSGTVEEVGSGVDDLAVGDRVAVNPLL-PCGKCEYCKKGEYS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCTKaiATYNGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAA---PLLCAgismyspMKYFGLTGPDKHVGIVGl 193
Cdd:cd08236 101 LCSN--YDYIGSRRD-----GAFAEYVSVPARNLIKIPDHVDYEEAAmiePAAVA-------LHAVRLAGITLGDTVVV- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 194 gglghIG--------VRFAKAFG-TKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQmKAAMGTMDG-----IIDTVSAS 259
Cdd:cd08236 166 -----IGagtigllaIQWLKILGaKRVIAVDIDDEKLAVARE-LGADDTINPKEEDV-EKVRELTEGrgadlVIEAAGSP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 260 HSISPLIGLLKSNGKLVLLG--ATEKPFDISAFSLILgRK--SIAGS-----GIGGMQETQEMIDFAAEHGIKAEIEI-- 328
Cdd:cd08236 239 ATIEQALALARPGGKVVLVGipYGDVTLSEEAFEKIL-RKelTIQGSwnsysAPFPGDEWRTALDLLASGKIKVEPLIth 317
                       330       340
                ....*....|....*....|.
gi 15235757 329 -ISMDYVNTAMDRLAKGDVRY 348
Cdd:cd08236 318 rLPLEDGPAAFERLADREEFS 338
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
35-355 3.10e-27

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 109.74  E-value: 3.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   35 KTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQ 114
Cdd:PRK13771  22 KPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPGDRV-ASLLYAPDGTCEYCRSGE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  115 ENYCTKAIATYNGVHhdgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLtGPDKHVGIVGLG 194
Cdd:PRK13771 101 EAYCKNRLGYGEELD-------GFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGLRRAGV-KKGETVLVTGAG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  195 GLGHI-GVRFAKAFGTKVTVVssTTGKSKDALDTLGADGFLVST--DEDQMKaaMGTMDGIIDTVsASHSISPLIGLLKS 271
Cdd:PRK13771 173 GGVGIhAIQVAKALGAKVIAV--TSSESKAKIVSKYADYVIVGSkfSEEVKK--IGGADIVIETV-GTPTLEESLRSLNM 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  272 NGKLVLLGATeKPFDISAFSL---ILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEI-ISMDYVNTAMDRLAKGDVR 347
Cdd:PRK13771 248 GGKIIQIGNV-DPSPTYSLRLgyiILKDIEIIGHISATKRDVEEALKLVAEGKIKPVIGAeVSLSEIDKALEELKDKSRI 326

                 ....*...
gi 15235757  348 YRFVIDIS 355
Cdd:PRK13771 327 GKILVKPS 334
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
35-302 4.97e-27

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


Pssm-ID: 176219 [Multi-domain]  Cd Length: 306  Bit Score: 108.56  E-value: 4.97e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVDSCRTCESCREDQ 114
Cdd:cd08258  23 EPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVSETTFSTCGRCPYCRRGD 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 115 ENYCTkaiatyngvhHDGTINY---GGYSDHIVVDERYAVKIPHTLPLVSAA---PLLCAGISMYSPMKY--------FG 180
Cdd:cd08258 103 YNLCP----------HRKGIGTqadGGFAEYVLVPEESLHELPENLSLEAAAltePLAVAVHAVAERSGIrpgdtvvvFG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 181 lTGPdkhvgivglgglghIG---VRFAKAFGTKVTVVSstTGKSKDALDT---LGADGFLVSTdEDQMKAAMGTMDG--- 251
Cdd:cd08258 173 -PGP--------------IGllaAQVAKLQGATVVVVG--TEKDEVRLDVakeLGADAVNGGE-EDLAELVNEITDGdga 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15235757 252 --IIDTVSASHSISPLIGLLKSNGKLVLLG-ATEKPFDISAFSLILGRKSIAGS 302
Cdd:cd08258 235 dvVIECSGAVPALEQALELLRKGGRIVQVGiFGPLAASIDVERIIQKELSVIGS 288
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
28-344 2.22e-26

zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct subset of the larger family of oxidoreductases that includes zinc-binding alcohol dehydrogenases and NADPH:quinone reductases (pfam00107). The gene neighborhood of members of this family is not conserved and it appears that no members are characterized. The sequence of the family includes 6 invariant cysteine residues and one invariant histidine. It appears that no member is characterized. [Energy metabolism, Fermentation]


Pssm-ID: 131869 [Multi-domain]  Cd Length: 329  Bit Score: 107.31  E-value: 2.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    28 PFVFSRRKT---GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVDSC 104
Cdd:TIGR02822  14 PLRFVERPVprpGPGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWLRRTC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   105 RTCESCREDQENYCTKAiaTYNGVHHDGtinygGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMY--------SPM 176
Cdd:TIGR02822  94 GVCRYCRRGAENLCPAS--RYTGWDTDG-----GYAEYTTVPAAFAYRLPTGYDDVELAPLLCAGIIGYrallraslPPG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   177 KYFGLTGpdkhvgivgLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALdTLGADGFLVSTDEDQMKaamgtMDGIIDTV 256
Cdd:TIGR02822 167 GRLGLYG---------FGGSAHLTAQVALAQGATVHVMTRGAAARRLAL-ALGAASAGGAYDTPPEP-----LDAAILFA 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   257 SASHSISPLIGLLKSNGKLVLLGA--TEKPfDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEIISMDYV 334
Cdd:TIGR02822 232 PAGGLVPPALEALDRGGVLAVAGIhlTDTP-PLNYQRHLFYERQIRSVTSNTRADAREFLELAAQHGVRVTTHTYPLSEA 310
                         330
                  ....*....|
gi 15235757   335 NTAMDRLAKG 344
Cdd:TIGR02822 311 DRALRDLKAG 320
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
31-317 2.20e-25

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: 104.36  E-value: 2.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  31 FSRRKTGEEEVRVKVLYCGICHSDLHCLkNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGV-GCIVDScrTCES 109
Cdd:cd08264  19 VKDPKPGPGEVLIRVKMAGVNPVDYNVI-NAVKVKPMPHIPGAEFAGVVEEVGDHVKGVKKGDRVVVyNRVFDG--TCDM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 110 CREDQENYCTkaiatyNGvHHDGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLtGPDKHVG 189
Cdd:cd08264  96 CLSGNEMLCR------NG-GIIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYHALKTAGL-GPGETVV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 190 IVGLGGLGHI-GVRFAKAFGTKVTVVSsttgkSKDALDTLGADgFLVSTDEDQMKAAMGTM--DGIIDTVSASHSISPLi 266
Cdd:cd08264 168 VFGASGNTGIfAVQLAKMMGAEVIAVS-----RKDWLKEFGAD-EVVDYDEVEEKVKEITKmaDVVINSLGSSFWDLSL- 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 15235757 267 GLLKSNGKLVLLGA---TEKPFDISafSLILGRKSIAGSGIGGMQETQEMIDFA 317
Cdd:cd08264 241 SVLGRGGRLVTFGTltgGEVKLDLS--DLYSKQISIIGSTGGTRKELLELVKIA 292
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
37-346 3.46e-24

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: 102.07  E-value: 3.46e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIyPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQEN 116
Cdd:cd08281  32 GPGEVLVKIAAAGLCHSDLSVINGDRPRPL-PMALGHEAAGVVVEVGEGVTDLEVGDHV-VLVFVPSCGHCRPCAEGRPA 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCTKAiATYNG------------------VHHDGTinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCA---------- 168
Cdd:cd08281 110 LCEPG-AAANGagtllsggrrlrlrggeiNHHLGV---SAFAEYAVVSRRSVVKIDKDVPLEIAALFGCAvltgvgavvn 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 169 --GISMYSPMKYFGLTGpdkhvgivglgglghIG---VRFAKAFG-TKVTVVSSTTGKSKDALDtLGADGFLVSTDED-- 240
Cdd:cd08281 186 taGVRPGQSVAVVGLGG---------------VGlsaLLGAVAAGaSQVVAVDLNEDKLALARE-LGATATVNAGDPNav 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 241 -QMKAAM-GTMDGIIDTVSASHSISPLIGLLKSNGKLVLLG--ATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDF 316
Cdd:cd08281 250 eQVRELTgGGVDYAFEMAGSVPALETAYEITRRGGTTVTAGlpDPEARLSVPALSLVAEERTLKGSYMGSCVPRRDIPRY 329
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15235757 317 AAEH-GIKAEIE-----IISMDYVNTAMDRLAKGDV 346
Cdd:cd08281 330 LALYlSGRLPVDkllthRLPLDEINEGFDRLAAGEA 365
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
31-325 7.12e-24

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: 100.47  E-value: 7.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  31 FSRRKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYP-LVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCES 109
Cdd:cd08239  17 FPVPVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQgVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHYV-GCGACRN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 110 CREDQENYCTKAIATYNGVHHdgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLC-----------AGISMYSPMKY 178
Cdd:cd08239  96 CRRGWMQLCTSKRAAYGWNRD------GGHAEYMLVPEKTLIPLPDDLSFADGALLLCgigtayhalrrVGVSGRDTVLV 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 179 FGLtGPdkhvgivglgglghIG---VRFAKAFG-TKVTVVSSTTGKSKDALDtLGADgFLVSTDEDQMKAAMGTMDG--- 251
Cdd:cd08239 170 VGA-GP--------------VGlgaLMLARALGaEDVIGVDPSPERLELAKA-LGAD-FVINSGQDDVQEIRELTSGaga 232
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235757 252 --IIDTVSASHSISPLIGLLKSNGKLVLLGATEKP-FDISAfSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAE 325
Cdd:cd08239 233 dvAIECSGNTAARRLALEAVRPWGRLVLVGEGGELtIEVSN-DLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVD 308
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
40-170 9.45e-24

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: 100.65  E-value: 9.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHClKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGciVDSCRTCESCREDQENYCT 119
Cdd:cd08278  29 EVLVRIVATGICHTDLVV-RDGGLPTPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLS--FASCGECANCLSGHPAYCE 105
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235757 120 KAIA-TYNGVHHDGTINY---GG------------YSDHIVVDERYAVKIPHTLPLVSAAPLLCaGI 170
Cdd:cd08278 106 NFFPlNFSGRRPDGSTPLsldDGtpvhghffgqssFATYAVVHERNVVKVDKDVPLELLAPLGC-GI 171
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
37-352 3.66e-22

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: 95.32  E-value: 3.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIY---PLVPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdscrtcescred 113
Cdd:cd05289  26 GPGEVLVKVHAAGVNPVDLKIREGLLKAAFPltlPLIPGHDVAGVVVAVGPGVTGFKVGDEV------------------ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 114 qenyctkaiatYNGVHHDGTinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHvgivg- 192
Cdd:cd05289  88 -----------FGMTPFTRG---GAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGLKAGQTvlihga 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 193 lgglgHIGVRFAKAFGTKVTVVSSTtgKSKDALDTLGADGFLVSTDED-QMKAAMGTMDGIIDTVSAShSISPLIGLLKS 271
Cdd:cd05289 154 aggvgSFAVQLAKARGARVIATASA--ANADFLRSLGADEVIDYTKGDfERAAAPGGVDAVLDTVGGE-TLARSLALVKP 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 272 NGKLVLLgATEKPFDISAFSLILGRKSIAGSGIGgmQETQEMIDFAAEHGIKAEI-EIISMDYVNTAMDRLAKGDVRYRF 350
Cdd:cd05289 231 GGRLVSI-AGPPPAEQAAKRRGVRAGFVFVEPDG--EQLAELAELVEAGKLRPVVdRVFPLEDAAEAHERLESGHARGKV 307

                ..
gi 15235757 351 VI 352
Cdd:cd05289 308 VL 309
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
35-345 1.02e-21

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: 94.58  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQ 114
Cdd:cd08235  21 EPGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDRVFVAPHV-PCGECHYCLRGN 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 115 ENYCTKAIATynGVHHDgtinyGGYSDHIVV-----DERYAVKIPHTLPLVSAA---PLLC-------AGISMYSPMKYF 179
Cdd:cd08235 100 ENMCPNYKKF--GNLYD-----GGFAEYVRVpawavKRGGVLKLPDNVSFEEAAlvePLACcinaqrkAGIKPGDTVLVI 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 180 GLtGPdkhvgivglgglghIG---VRFAKAFGTKVTVVSSTtgkSKDALD---TLGADGFLVSTDEDQMKAAMGTMDG-- 251
Cdd:cd08235 173 GA-GP--------------IGllhAMLAKASGARKVIVSDL---NEFRLEfakKLGADYTIDAAEEDLVEKVRELTDGrg 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 252 ---IIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISA-FSLILGR-KSIAGSGIGGMQETQEMIDFAAEHGIKAEI 326
Cdd:cd08235 235 advVIVATGSPEAQAQALELVRKGGRILFFGGLPKGSTVNIdPNLIHYReITITGSYAASPEDYKEALELIASGKIDVKD 314
                       330       340
                ....*....|....*....|..
gi 15235757 327 EI---ISMDYVNTAMDRLAKGD 345
Cdd:cd08235 315 LIthrFPLEDIEEAFELAADGK 336
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
37-288 2.72e-21

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: 93.02  E-value: 2.72e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCL--KNEWHSsiYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQ 114
Cdd:cd08261  23 GAGEVLVRVKRVGICGSDLHIYhgRNPFAS--YPRILGHELSGEVVEVGEGVAGLKVGDRV-VVDPYISCGECYACRKGR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 115 ENYCTKaIATYnGVHHDgtinyGGYSDHIVVDERyAVKIPHTLPLVSAA---PL------------------LCAGismy 173
Cdd:cd08261 100 PNCCEN-LQVL-GVHRD-----GGFAEYIVVPAD-ALLVPEGLSLDQAAlvePLaigahavrragvtagdtvLVVG---- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 174 spmkyfglTGPdkhvgivglgglghIG---VRFAKAFGTKVTVVSSttgkSKDALD---TLGADGFLVSTDEDQMKAAMG 247
Cdd:cd08261 168 --------AGP--------------IGlgvIQVAKARGARVIVVDI----DDERLEfarELGADDTINVGDEDVAARLRE 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15235757 248 TMDG-----IIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDIS 288
Cdd:cd08261 222 LTDGegadvVIDATGNPASMEEAVELVAHGGRVVLVGLSKGPVTFP 267
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
37-353 4.03e-21

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: 92.66  E-value: 4.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQEN 116
Cdd:cd08260  24 PPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVPFVL-GCGTCPYCRAGDSN 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 YCTKaiatyngVHHDGTINYGGYSDHIVVD--ERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDK----HVGI 190
Cdd:cd08260 103 VCEH-------QVQPGFTHPGSFAEYVAVPraDVNLVRLPDDVDFVTAAGLGCRFATAFRALVHQARVKPGEwvavHGCG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 191 VGLGGLGHIgvrfAKAFGTKVTVVSSttgkSKDALD---TLGADGFL-VSTDEDQMKAAMGTMDG----IIDTVSASHSI 262
Cdd:cd08260 176 GVGLSAVMI----ASALGARVIAVDI----DDDKLElarELGAVATVnASEVEDVAAAVRDLTGGgahvSVDALGIPETC 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 263 SPLIGLLKSNGKLVLLGATEK-------PFDIsafsLILGRKSIAGSgiGGMQ--ETQEMIDFAAEHGIKAEIEI---IS 330
Cdd:cd08260 248 RNSVASLRKRGRHVQVGLTLGeeagvalPMDR----VVARELEIVGS--HGMPahRYDAMLALIASGKLDPEPLVgrtIS 321
                       330       340
                ....*....|....*....|...
gi 15235757 331 MDYVNTAMDRLAKGDVRYRFVID 353
Cdd:cd08260 322 LDEAPDALAAMDDYATAGITVIT 344
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
40-171 5.86e-21

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


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 92.79  E-value: 5.86e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEWHSsIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYCT 119
Cdd:cd08277  29 EVRIKMLATSVCHTDILAIEGFKAT-LFPVILGHEGAGIVESVGEGVTNLKPGDKV-IPLFIGQCGECSNCRSGKTNLCQ 106
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235757 120 KAIATYNGVHHDGT--INYGG-----------YSDHIVVDERYAVKIPHTLPLVSAApLLCAGIS 171
Cdd:cd08277 107 KYRANESGLMPDGTsrFTCKGkkiyhflgtstFSQYTVVDENYVAKIDPAAPLEHVC-LLGCGFS 170
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
35-169 1.64e-19

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: 88.47  E-value: 1.64e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIV-----DSCRTCES 109
Cdd:cd08231  22 DLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTDVAGEPLKVGDRVtwsvgAPCGRCYR 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15235757 110 CREDQENYC---TKA-IATYNGVHHdgtiNYGGYSDHIVVD-ERYAVKIPHTLPLVSAAPLLCAG 169
Cdd:cd08231 102 CLVGDPTKCenrKKYgHEASCDDPH----LSGGYAEHIYLPpGTAIVRVPDNVPDEVAAPANCAL 162
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
37-165 5.53e-19

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: 86.52  E-value: 5.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKnewHSSI------YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESC 110
Cdd:cd08232  20 GPGEVRVRVAAGGICGSDLHYYQ---HGGFgtvrlrEPMVLGHEVSGVVEAVGPGVTGLAPGQRVAVNPSR-PCGTCDYC 95
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235757 111 REDQENYCTKaiATYNGV-----HHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAA---PL 165
Cdd:cd08232  96 RAGRPNLCLN--MRFLGSamrfpHVQ-----GGFREYLVVDASQCVPLPDGLSLRRAAlaePL 151
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
37-292 6.68e-19

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: 86.39  E-value: 6.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKnewHSSI------YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGV--GCivdSCRTCE 108
Cdd:cd05285  21 GPGEVLVRVRAVGICGSDVHYYK---HGRIgdfvvkEPMVLGHESAGTVVAVGSGVTHLKVGDRVAIepGV---PCRTCE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 109 SCREDQENYCtKAI---ATYNgvhHDGTInyggySDHIVVDERYAVKIPHTLPLVSAAplLC------------AGISMY 173
Cdd:cd05285  95 FCKSGRYNLC-PDMrfaATPP---VDGTL-----CRYVNHPADFCHKLPDNVSLEEGA--LVeplsvgvhacrrAGVRPG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 174 SPMKYFGlTGPdkhvgivglgglghIG---VRFAKAFG-TKVTVvsstTGKSKDALDT---LGADGFLVSTDED------ 240
Cdd:cd05285 164 DTVLVFG-AGP--------------IGlltAAVAKAFGaTKVVV----TDIDPSRLEFakeLGATHTVNVRTEDtpesae 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15235757 241 QMKAAMGTM--DGIIDTVSASHSISPLIGLLKSNGKLVL--LGATEKPFDISAFSL 292
Cdd:cd05285 225 KIAELLGGKgpDVVIECTGAESCIQTAIYATRPGGTVVLvgMGKPEVTLPLSAASL 280
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
37-171 1.18e-18

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: 85.95  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEwHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQEN 116
Cdd:cd05279  24 KAGEVRIKVVATGVCHTDLHVIDGK-LPTPLPVILGHEGAGIVESIGPGVTTLKPGDKV-IPLFGPQCGKCKQCLNPRPN 101
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15235757 117 YCTK-AIATYNGVHHDGT-------------INYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCaGIS 171
Cdd:cd05279 102 LCSKsRGTNGRGLMSDGTsrftckgkpihhfLGTSTFAEYTVVSEISLAKIDPDAPLEKVCLIGC-GFS 169
PRK10083 PRK10083
putative oxidoreductase; Provisional
40-163 6.27e-18

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 83.64  E-value: 6.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   40 EVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQENYCT 119
Cdd:PRK10083  26 EVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGERVAVDPVI-SCGHCYPCSIGKPNVCT 104
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15235757  120 KAIATynGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAA 163
Cdd:PRK10083 105 SLVVL--GVHRD-----GGFSEYAVVPAKNAHRIPDAIADQYAV 141
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
198-319 6.42e-18

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 78.80  E-value: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   198 HIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDED---QMKAAMGTM--DGIIDTVSASHSISPLIGLLKSN 272
Cdd:pfam00107   4 LAAIQLAKAAGAKVIAVDGSEEKLELAKE-LGADHVINPKETDlveEIKELTGGKgvDVVFDCVGSPATLEQALKLLRPG 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15235757   273 GKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAE 319
Cdd:pfam00107  83 GRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
40-302 4.46e-17

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: 81.50  E-value: 4.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDlHCLKNEWHSSIYP----LVPGHEIIGEVSEIGnKVSKFNLGDKVgVGCIVDSCRTCESCREDQE 115
Cdd:cd08230  27 EVLVRTLEVGVCGTD-REIVAGEYGTAPPgedfLVLGHEALGVVEEVG-DGSGLSPGDLV-VPTVRRPPGKCLNCRIGRP 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 116 NYCTkaiatyNGVHHD-GTINYGGY-SDHIVVDERYAVKIPHTL--------PL------VSAAPLLCAGISMYSPMKYF 179
Cdd:cd08230 104 DFCE------TGEYTErGIKGLHGFmREYFVDDPEYLVKVPPSLadvgvllePLsvvekaIEQAEAVQKRLPTWNPRRAL 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 180 GL-TGPdkhvgivglgglghIGVRFAKAF---GTKVTVVS--STTGKSKDALDTLGADGFLVSTDEDQMKAAMGTMDGII 253
Cdd:cd08230 178 VLgAGP--------------IGLLAALLLrlrGFEVYVLNrrDPPDPKADIVEELGATYVNSSKTPVAEVKLVGEFDLII 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15235757 254 DTVSASHSISPLIGLLKSNGKLVLLGATEK----PFDISAF--SLILGRKSIAGS 302
Cdd:cd08230 244 EATGVPPLAFEALPALAPNGVVILFGVPGGgrefEVDGGELnrDLVLGNKALVGS 298
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
36-159 5.96e-17

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: 80.78  E-value: 5.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  36 TGEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQE 115
Cdd:cd05278  23 QGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVSVPCIT-FCGRCRFCRRGYH 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15235757 116 NYCTKaiaTYNGVHHDGTINyGGYSDHIVVDE--RYAVKIPHTLPL 159
Cdd:cd05278 102 AHCEN---GLWGWKLGNRID-GGQAEYVRVPYadMNLAKIPDGLPD 143
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
40-159 7.08e-17

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: 80.82  E-value: 7.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEwHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYCT 119
Cdd:cd08299  34 EVRIKIVATGICRSDDHVVSGK-LVTPFPVILGHEAAGIVESVGEGVTTVKPGDKV-IPLFVPQCGKCRACLNPESNLCL 111
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15235757 120 KA-IATYNGVHHDGT-------------INYGGYSDHIVVDERYAVKIPHTLPL 159
Cdd:cd08299 112 KNdLGKPQGLMQDGTsrftckgkpihhfLGTSTFSEYTVVDEIAVAKIDAAAPL 165
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
35-347 3.78e-16

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: 78.03  E-value: 3.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLHCLKNEWHSSI---YPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIvdscrtcescr 111
Cdd:cd08267  23 TPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLgrpFPPIPGMDFAGEVVAVGSGVTRFKVGDEV-FGRL----------- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 112 edqenyctkaiatyngvhhdGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHvgiv 191
Cdd:cd08267  91 --------------------PPKGGGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQRvlin 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 192 g-lgglgHIGVRFAKAFGTKVTVVSSTtgKSKDALDTLGADGFLVSTDED--QMKAAMGTMDGIIDTV-SASHSISPLIG 267
Cdd:cd08267 151 gasggvgTFAVQIAKALGAHVTGVCST--RNAELVRSLGADEVIDYTTEDfvALTAGGEKYDVIFDAVgNSPFSLYRASL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 268 LLKSNGKLVLLGATEKPF-----DISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIKAEIEII-SMDYVNTAMDRL 341
Cdd:cd08267 229 ALKPGGRYVSVGGGPSGLllvllLLPLTLGGGGRRLKFFLAKPNAEDLEQLAELVEEGKLKPVIDSVyPLEDAPEAYRRL 308

                ....*.
gi 15235757 342 AKGDVR 347
Cdd:cd08267 309 KSGRAR 314
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
37-163 6.47e-16

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 77.94  E-value: 6.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   37 GEEEVRVKVLYCGICHSDLHCLK-NEWHSSIY--PLVPGHEIIGEVSEIGNKVSKFNLGDKV-GVGCIVdsCRTCESCRE 112
Cdd:PRK05396  24 GPNDVLIKVKKTAICGTDVHIYNwDEWAQKTIpvPMVVGHEFVGEVVEVGSEVTGFKVGDRVsGEGHIV--CGHCRNCRA 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15235757  113 DQENYC--TKAIatynGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAA 163
Cdd:PRK05396 102 GRRHLCrnTKGV----GVNRP-----GAFAEYLVIPAFNVWKIPDDIPDDLAA 145
Rxyl_3153 TIGR03989
NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within ...
37-168 6.91e-16

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


Pssm-ID: 274905 [Multi-domain]  Cd Length: 369  Bit Score: 78.13  E-value: 6.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQEN 116
Cdd:TIGR03989  25 KAGEVLVKLVASGLCHSDEHLVTGDLPMPRYPILGGHEGAGVVTKVGPGVTGVKPGDHV-VLSFIPACGRCRYCSTGLQN 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235757   117 YCTKAIATYNG---------VHHDGT-----INYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCA 168
Cdd:TIGR03989 104 LCDLGAALLTGsqisdgtyrFHADGQdvgqmCLLGTFSEYTVVPEASVVKIDDDIPLDKACLVGCG 169
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
40-171 1.54e-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: 76.88  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYCT 119
Cdd:cd08300  29 EVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKPGDHV-IPLYTPECGECKFCKSGKTNLCQ 107
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235757 120 KAIATY-NGVHHDGT----------INYGG---YSDHIVVDERYAVKIPHTLPLVSAAPLLCaGIS 171
Cdd:cd08300 108 KIRATQgKGLMPDGTsrfsckgkpiYHFMGtstFSEYTVVAEISVAKINPEAPLDKVCLLGC-GVT 172
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
40-171 1.98e-15

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: 76.56  E-value: 1.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYCT 119
Cdd:cd08301  29 EVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHV-LPVFTGECKECRHCKSEKSNMCD 107
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235757 120 K-AIATYNGV-HHDGT-------------INYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCaGIS 171
Cdd:cd08301 108 LlRINTDRGVmINDGKsrfsingkpiyhfVGTSTFSEYTVVHVGCVAKINPEAPLDKVCLLSC-GVS 173
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
37-278 1.98e-15

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 76.16  E-value: 1.98e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVgcivdscrtcescredqen 116
Cdd:cd08271  26 GAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKVGDRVAY------------------- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 yctkaiatyngvHHDGTiNYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKyfgltgpDKHVGIVGLGGL 196
Cdd:cd08271  87 ------------HASLA-RGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALF-------KKLRIEAGRTIL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 197 GH--------IGVRFAKAFGTKVTVVSSTtgKSKDALDTLGADGFLVSTDEDQMKAAMGTMDG-----IIDTVSASHSIS 263
Cdd:cd08271 147 ITggaggvgsFAVQLAKRAGLRVITTCSK--RNFEYVKSLGADHVIDYNDEDVCERIKEITGGrgvdaVLDTVGGETAAA 224
                       250
                ....*....|....*
gi 15235757 264 pLIGLLKSNGKLVLL 278
Cdd:cd08271 225 -LAPTLAFNGHLVCI 238
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
37-354 1.05e-14

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: 74.22  E-value: 1.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSI-YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQE 115
Cdd:cd08266  26 GPDEVLVRVKAAALNHLDLWVRRGMPGIKLpLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPGI-SCGRCEYCLAGRE 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 116 NYCTKaiATYNGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPL--VSAAPLLC----------AGISMYSPMKYFGLTG 183
Cdd:cd08266 105 NLCAQ--YGILGEHVD-----GGYAEYVAVPARNLLPIPDNLSFeeAAAAPLTFltawhmlvtrARLRPGETVLVHGAGS 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 184 pdkhvgivglgGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAM-----GTMDGIIDTVSA 258
Cdd:cd08266 178 -----------GVGSAAIQIAKLFGATVIATAGSEDKLERAKE-LGADYVIDYRKEDFVREVReltgkRGVDVVVEHVGA 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 259 SHSISPLIgLLKSNGKLVLLGAT---EKPFDISAfslILGRK-SIAGSGIGGMQETQEMIDFAAEHGIKAEIE-IISMDY 333
Cdd:cd08266 246 ATWEKSLK-SLARGGRLVTCGATtgyEAPIDLRH---VFWRQlSILGSTMGTKAELDEALRLVFRGKLKPVIDsVFPLEE 321
                       330       340
                ....*....|....*....|.
gi 15235757 334 VNTAMDRLAKGDVRYRFVIDI 354
Cdd:cd08266 322 AAEAHRRLESREQFGKIVLTP 342
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
37-347 3.07e-14

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: 72.62  E-value: 3.07e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSiYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDscrtcescredqen 116
Cdd:cd08249  25 GPDEVLVKVKAVALNPVDWKHQDYGFIPS-YPAILGCDFAGTVVEVGSGVTRFKVGDRV-AGFVHG-------------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 yctkaiatYNGVHHDgtinYGGYSDHIVVDERYAVKIPHTLPLVSAA----PLLCAGISMYSPMkyfGLTGPDKHVGIVG 192
Cdd:cd08249  89 --------GNPNDPR----NGAFQEYVVADADLTAKIPDNISFEEAAtlpvGLVTAALALFQKL---GLPLPPPKPSPAS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 193 LGGLGHI----------GVRFAKAFGTKVTVVSSTtgKSKDALDTLGADgfLV------STDEDQMKAAMGTMDGIIDTV 256
Cdd:cd08249 154 KGKPVLIwggsssvgtlAIQLAKLAGYKVITTASP--KNFDLVKSLGAD--AVfdyhdpDVVEDIRAATGGKLRYALDCI 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 257 SASHSISPLIGLLKSN--GKLVLL----GATEKPFDISaFSLILGRkSIAGSGIGGMQETQEMIDFA----AEHGIKA-E 325
Cdd:cd08249 230 STPESAQLCAEALGRSggGKLVSLlpvpEETEPRKGVK-VKFVLGY-TVFGEIPEDREFGEVFWKYLpellEEGKLKPhP 307
                       330       340
                ....*....|....*....|....
gi 15235757 326 IEIIS--MDYVNTAMDRLAKGDVR 347
Cdd:cd08249 308 VRVVEggLEGVQEGLDLLRKGKVS 331
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
35-159 6.64e-14

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: 71.88  E-value: 6.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLHCLK-NEWHSSIY--PLVPGHEIIGEVSEIGNKVSKFNLGDKVGV-GCIVdsCRTCESC 110
Cdd:cd05281  22 KPGPGEVLIKVLAASICGTDVHIYEwDEWAQSRIkpPLIFGHEFAGEVVEVGEGVTRVKVGDYVSAeTHIV--CGKCYQC 99
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15235757 111 REDQENYC--TKAIatynGVHHDGTinyggYSDHIVVDERYAVKIPHTLPL 159
Cdd:cd05281 100 RTGNYHVCqnTKIL----GVDTDGC-----FAEYVVVPEENLWKNDKDIPP 141
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
22-168 1.19e-13

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: 70.85  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  22 SSGHLSPFVFSRRKTGEEEVRVKVLYCGICHSDLHCLKN---EWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVg 98
Cdd:cd08269   3 GPGRFEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFNQgrpWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAG- 81
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15235757  99 civdscrtcescredqenyctkaiatyngvhhdgtINYGGYSDHIVVDERYAVKIPHTLP--LVSAAPLLCA 168
Cdd:cd08269  82 -----------------------------------LSGGAFAEYDLADADHAVPLPSLLDgqAFPGEPLGCA 118
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
37-280 1.50e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 70.71  E-value: 1.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWH-SSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVgcivdscrtcescredqe 115
Cdd:cd08268  26 GAGEVLIRVEAIGLNRADAMFRRGAYIePPPLPARLGYEAAGVVEAVGAGVTGFAVGDRVSV------------------ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 116 nyctkaIATYNgvHHDgtinYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHVGIVGLGG 195
Cdd:cd08268  88 ------IPAAD--LGQ----YGTYAEYALVPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 196 LGHI-GVRFAKAFGTKVTVVSSTTGKsKDALDTLGADGFLVSTDEDQMKAAMGTMDG-----IIDTVSASHsISPLIGLL 269
Cdd:cd08268 156 SVGLaAIQIANAAGATVIATTRTSEK-RDALLALGAAHVIVTDEEDLVAEVLRITGGkgvdvVFDPVGGPQ-FAKLADAL 233
                       250
                ....*....|.
gi 15235757 270 KSNGKLVLLGA 280
Cdd:cd08268 234 APGGTLVVYGA 244
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
34-153 2.27e-13

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: 70.62  E-value: 2.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  34 RKTGEEEVRVKVLYCGICHSDLHCLKNEWHSSI-------YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRT 106
Cdd:cd08265  47 PNLKPDEILIRVKACGICGSDIHLYETDKDGYIlypglteFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTAEEMM-WCGM 125
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15235757 107 CESCREDQENYCtKAIATYnGVHHDgtinyGGYSDHIVVDERYAVKI 153
Cdd:cd08265 126 CRACRSGSPNHC-KNLKEL-GFSAD-----GAFAEYIAVNARYAWEI 165
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
37-353 3.93e-13

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: 69.64  E-value: 3.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLK-----------NEWHSSIYPLVPGHEIIGEVSEIGNKVS-KFNLGDKVgVGCIVDSC 104
Cdd:cd08262  22 GPGQVLVKVLACGICGSDLHATAhpeamvddaggPSLMDLGADIVLGHEFCGEVVDYGPGTErKLKVGTRV-TSLPLLLC 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 105 RTCESCredqenyctkAIATYNGvhhdgtiNYGGYSDHIVVDERYAVKIPHTLPLVSAA---PLLC-------AGISMYS 174
Cdd:cd08262 101 GQGASC----------GIGLSPE-------APGGYAEYMLLSEALLLRVPDGLSMEDAAltePLAVglhavrrARLTPGE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 175 PMKYFGlTGPdkhvgivglgglghIG---VRFAKAFGTKVTVVSSTTGKSKDALDTLGADGFLVSTDED--------QMK 243
Cdd:cd08262 164 VALVIG-CGP--------------IGlavIAALKARGVGPIVASDFSPERRALALAMGADIVVDPAADSpfaawaaeLAR 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 244 AAMGTMDGIIDTVSASHSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIK 323
Cdd:cd08262 229 AGGPKPAVIFECVGAPGLIQQIIEGAPPGGRIVVVGVCMESDNIEPALAIRKELTLQFSLGYTPEEFADALDALAEGKVD 308
                       330       340       350
                ....*....|....*....|....*....|...
gi 15235757 324 AE---IEIISMDYVNTAMDRLAKGDVRYRFVID 353
Cdd:cd08262 309 VApmvTGTVGLDGVPDAFEALRDPEHHCKILVD 341
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
43-119 5.90e-13

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: 69.20  E-value: 5.90e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15235757  43 VKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIvDSCRTCESCREDQENYCT 119
Cdd:cd08286  30 VKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKVGDRVLISCI-SSCGTCGYCRKGLYSHCE 105
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
38-302 9.23e-13

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 68.32  E-value: 9.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   38 EEEVRVKVLYCGICHSDL-HCLKNEWHssIYPLVPGHEIIGEVSEIGNKVSKFNLGDkvGVGCI-VDSCRTCESCREDQE 115
Cdd:PRK10309  25 QDDVLVKVASSGLCGSDIpRIFKNGAH--YYPITLGHEFSGYVEAVGSGVDDLHPGD--AVACVpLLPCFTCPECLRGFY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  116 NYCTKaiatYNGVhhdGTINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGpdKHVGIVGLGG 195
Cdd:PRK10309 101 SLCAK----YDFI---GSRRDGGNAEYIVVKRKNLFALPTDMPIEDGAFIEPITVGLHAFHLAQGCEG--KNVIIIGAGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  196 LGHIGVRFAKAFGTK-VTVVSSTTGKSKDALdTLGADGFLVSTD--EDQMKAAMGTM---DGIIDTVSASHSISPLIGLL 269
Cdd:PRK10309 172 IGLLAIQCAVALGAKsVTAIDINSEKLALAK-SLGAMQTFNSREmsAPQIQSVLRELrfdQLILETAGVPQTVELAIEIA 250
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15235757  270 KSNGKLVLLGATEKPFDISA--FSLILgRK--SIAGS 302
Cdd:PRK10309 251 GPRAQLALVGTLHHDLHLTSatFGKIL-RKelTVIGS 286
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
40-353 1.18e-12

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: 67.91  E-value: 1.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEwhssiY------PLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCivdscrtcescred 113
Cdd:cd08241  29 EVRIRVEAAGVNFPDLLMIQGK-----YqvkpplPFVPGSEVAGVVEAVGEGVTGFKVGDRVVALT-------------- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 114 qenyctkaiatyngvhhdgtiNYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMyspmkYFGLT----------- 182
Cdd:cd08241  90 ---------------------GQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTA-----YHALVrrarlqpgetv 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 183 -------GpdkhvgivglgglghIG---VRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDED---QMKAAMGT- 248
Cdd:cd08241 144 lvlgaagG---------------VGlaaVQLAKALGARVIAAASSEEKLALARA-LGADHVIDYRDPDlreRVKALTGGr 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 249 -MDGIIDTVSASHSiSPLIGLLKSNGKLVLLGatekpF---DISAFSL-ILGRKSIA--GSGIGGMQET---------QE 312
Cdd:cd08241 208 gVDVVYDPVGGDVF-EASLRSLAWGGRLLVIG-----FasgEIPQIPAnLLLLKNISvvGVYWGAYARRepellranlAE 281
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15235757 313 MIDFAAEHGIKAEI-EIISMDYVNTAMDRLAKGDVRYRFVID 353
Cdd:cd08241 282 LFDLLAEGKIRPHVsAVFPLEQAAEALRALADRKATGKVVLT 323
PLN02740 PLN02740
Alcohol dehydrogenase-like
28-171 1.28e-12

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 68.28  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   28 PFVFSRRKT---GEEEVRVKVLYCGICHSDLHCLK--NEWHSSiYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVD 102
Cdd:PLN02740  22 PLVMEEIRVdppQKMEVRIKILYTSICHTDLSAWKgeNEAQRA-YPRILGHEAAGIVESVGEGVEDLKAGDHV-IPIFNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  103 SCRTCESCREDQENYCT-------KAIATYNG------------VHHdgTINYGGYSDHIVVDERYAVKIPHTLPLVSAA 163
Cdd:PLN02740 100 ECGDCRYCKRDKTNLCEtyrvdpfKSVMVNDGktrfstkgdgqpIYH--FLNTSTFTEYTVLDSACVVKIDPNAPLKKMS 177

                 ....*...
gi 15235757  164 PLLCaGIS 171
Cdd:PLN02740 178 LLSC-GVS 184
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
37-168 1.54e-12

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


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 67.82  E-value: 1.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCL---KNEW---HSSIY---PLVPGHEIIGEVSEIGNKVSK--FNLGDKVGVGCIVdSCR 105
Cdd:cd08256  23 GPGEILVKVEACGICAGDIKCYhgaPSFWgdeNQPPYvkpPMIPGHEFVGRVVELGEGAEErgVKVGDRVISEQIV-PCW 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15235757 106 TCESCREDQENYCTKaiatyngvhHD----GTINYGGYSDHIVVDERYAV-KIPHTLPLVSAA---PLLCA 168
Cdd:cd08256 102 NCRFCNRGQYWMCQK---------HDlygfQNNVNGGMAEYMRFPKEAIVhKVPDDIPPEDAIliePLACA 163
PLN02702 PLN02702
L-idonate 5-dehydrogenase
36-279 3.97e-12

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 66.72  E-value: 3.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   36 TGEEEVRVKVLYCGICHSDLHCLKNEWHSSIY---PLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCRE 112
Cdd:PLN02702  39 LGPHDVRVRMKAVGICGSDVHYLKTMRCADFVvkePMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGI-SCWRCNLCKE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  113 DQENYC--TKAIATyNGVHhdgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAplLCAGISMYSPMKYFGLTGPDKHVGI 190
Cdd:PLN02702 118 GRYNLCpeMKFFAT-PPVH-------GSLANQVVHPADLCFKLPENVSLEEGA--MCEPLSVGVHACRRANIGPETNVLV 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  191 VGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDTLGADG-FLVST-DED------QMKAAMGT-MDGIIDTVSASHS 261
Cdd:PLN02702 188 MGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEiVLVSTnIEDveseveEIQKAMGGgIDVSFDCVGFNKT 267
                        250
                 ....*....|....*...
gi 15235757  262 ISPLIGLLKSNGKLVLLG 279
Cdd:PLN02702 268 MSTALEATRAGGKVCLVG 285
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
40-352 9.87e-12

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 65.36  E-value: 9.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDlhCLKNE---WHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGvgcivdsCRTcescredqen 116
Cdd:cd08273  29 EVVVKVEASGVSFAD--VQMRRglyPDQPPLPFTPGYDLVGRVDALGSGVTGFEVGDRVA-------ALT---------- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 117 yctkaiatyngvhhdgtiNYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDK----Hvgivg 192
Cdd:cd08273  90 ------------------RVGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQrvliH----- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 193 lggLGHIGV-----RFAKAFGTKVTVVSSTtgKSKDALDTLGADGFLVSTDE--DQMKaAMGTMDGIIDTVSASHsISPL 265
Cdd:cd08273 147 ---GASGGVgqallELALLAGAEVYGTASE--RNHAALRELGATPIDYRTKDwlPAML-TPGGVDVVFDGVGGES-YEES 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 266 IGLLKSNGKLVLLGAT------EKPF--------DISAFSLILGRKSIAGSGIGG---------MQETQEMIDFAAEHGI 322
Cdd:cd08273 220 YAALAPGGTLVCYGGNssllqgRRSLaalgsllaRLAKLKLLPTGRRATFYYVWRdraedpklfRQDLTELLDLLAKGKI 299
                       330       340       350
                ....*....|....*....|....*....|.
gi 15235757 323 KAEI-EIISMDYVNTAMDRLAKGDVRYRFVI 352
Cdd:cd08273 300 RPKIaKRLPLSEVAEAHRLLESGKVVGKIVL 330
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
33-127 2.46e-11

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: 63.80  E-value: 2.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  33 RRKTGEEEVRVKVLYCGICHSDLHCLKNEWHssiYPLVPGHEIIGEVSEIGNKvskfNLGDKVGVGCIVDSCRTCESCRE 112
Cdd:cd08242  19 KPEPPPGEALVRVLLAGICNTDLEIYKGYYP---FPGVPGHEFVGIVEEGPEA----ELVGKRVVGEINIACGRCEYCRR 91
                        90
                ....*....|....*....
gi 15235757 113 DQENYC----TKAIATYNG 127
Cdd:cd08242  92 GLYTHCpnrtVLGIVDRDG 110
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
43-120 4.97e-11

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: 63.04  E-value: 4.97e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15235757  43 VKVLYCGICHSDLHCLKNEWHSSiYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYCTK 120
Cdd:cd08284  30 VKVTAAAICGSDLHIYRGHIPST-PGFVLGHEFVGEVVEVGPEVRTLKVGDRV-VSPFTIACGECFYCRRGQSGRCAK 105
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
37-279 8.11e-11

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: 62.46  E-value: 8.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLhcLKNEWHssiYPL------VPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdscrtcesc 110
Cdd:cd05276  26 GPGEVLIRVAAAGVNRADL--LQRQGL---YPPppgasdILGLEVAGVVVAVGPGVTGWKVGDRV--------------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 111 redqenyCtkAIAtyNGvhhdgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKhvgi 190
Cdd:cd05276  86 -------C--ALL--AG---------GGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGLKAGE---- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 191 vglGGLGH-----IG---VRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDED---QMKAAMGT--MDGIIDTVS 257
Cdd:cd05276 142 ---TVLIHggasgVGtaaIQLAKALGARVIATAGSEEKLEACRA-LGADVAINYRTEDfaeEVKEATGGrgVDVILDMVG 217
                       250       260
                ....*....|....*....|..
gi 15235757 258 ASHsISPLIGLLKSNGKLVLLG 279
Cdd:cd05276 218 GDY-LARNLRALAPDGRLVLIG 238
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
35-323 1.70e-10

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 61.40  E-value: 1.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLHCLKNEW-HSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdscrtcescred 113
Cdd:cd08276  24 EPGPGEVLVRVHAVSLNYRDLLILNGRYpPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRV------------------ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 114 qenyctkaIATYNGVHHDGTINY------------GGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYS------P 175
Cdd:cd08276  86 --------VPTFFPNWLDGPPTAedeasalggpidGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNalfglgP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 176 MK-----YFGLTGpdkhvgivglgglghiGV-----RFAKAFGTKVTVVSSTTGKSkDALDTLGADGFL-VSTDEDQMKA 244
Cdd:cd08276 158 LKpgdtvLVQGTG----------------GVslfalQFAKAAGARVIATSSSDEKL-ERAKALGADHVInYRTTPDWGEE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 245 AMGTMDG-----IIDTVSASH---SISpligLLKSNGKLVLLGA-TEKPFDISAFSLILGRKSIAGSGIGGMQETQEMID 315
Cdd:cd08276 221 VLKLTGGrgvdhVVEVGGPGTlaqSIK----AVAPGGVISLIGFlSGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNR 296

                ....*...
gi 15235757 316 FAAEHGIK 323
Cdd:cd08276 297 AIEAHRIR 304
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
38-119 3.09e-10

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: 61.07  E-value: 3.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  38 EEEVRVKVLYCGICHSDLHclknewhssIY--------PLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCES 109
Cdd:cd08282  25 PTDAIVRITTTAICGSDLH---------MYrgrtgaepGLVLGHEAMGEVEEVGSAVESLKVGDRVVVPFNV-ACGRCRN 94
                        90
                ....*....|
gi 15235757 110 CREDQENYCT 119
Cdd:cd08282  95 CKRGLTGVCL 104
PLN02827 PLN02827
Alcohol dehydrogenase-like
40-181 5.57e-10

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 60.30  E-value: 5.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   40 EVRVKVLYCGICHSDLhclkNEWHS-SIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYC 118
Cdd:PLN02827  39 EIRIKVVSTSLCRSDL----SAWESqALFPRIFGHEASGIVESIGEGVTEFEKGDHV-LTVFTGECGSCRHCISGKSNMC 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  119 TKAIATYNGVHHD---------GTINY-----GGYSDHIVVDERYAVKIPHTLPLVSAAPLLC------------AGISM 172
Cdd:PLN02827 114 QVLGLERKGVMHSdqktrfsikGKPVYhycavSSFSEYTVVHSGCAVKVDPLAPLHKICLLSCgvaaglgaawnvADVSK 193

                 ....*....
gi 15235757  173 YSPMKYFGL 181
Cdd:PLN02827 194 GSSVVIFGL 202
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
68-353 7.34e-09

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: 56.46  E-value: 7.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  68 PLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCivdscrtcescredqenyctkaiatynGVHHDGTinyggYSDHIVVDE 147
Cdd:cd08248  74 PLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAV---------------------------PPWSQGT-----HAEYVVVPE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 148 RYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPD--KHVGIVGLGGLGHIG---VRFAKAFGTKVTVVSSTtgKSK 222
Cdd:cd08248 122 NEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGGLNPKnaAGKRVLILGGSGGVGtfaIQLLKAWGAHVTTTCST--DAI 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 223 DALDTLGADGFLVSTDEDQMKA--AMGTMDGIIDTVSAShSISPLIGLLKSNGKLV-----LLGATEK---PFDISAFSL 292
Cdd:cd08248 200 PLVKSLGADDVIDYNNEDFEEEltERGKFDVILDTVGGD-TEKWALKLLKKGGTYVtlvspLLKNTDKlglVGGMLKSAV 278
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15235757 293 ILGRKSIAGSGIG-------------GMQETQEMIdfaaEHG-IKAEIE-IISMDYVNTAMDRLAKGDVRYRFVID 353
Cdd:cd08248 279 DLLKKNVKSLLKGshyrwgffspsgsALDELAKLV----EDGkIKPVIDkVFPFEEVPEAYEKVESGHARGKTVIK 350
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
40-280 7.42e-09

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: 56.52  E-value: 7.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEWHSSI-YPLVPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdscrtcescredqenyc 118
Cdd:cd05282  28 EVLVRMLAAPINPSDLITISGAYGSRPpLPAVPGNEGVGVVVEVGSGVSGLLVGQRV----------------------- 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 119 tkaiATYNGvhhdgtinYGGYSDHIVVDERYAVKIPHTLPLVSAA-----P----LLCAGISMYSPMKYFGLTGpdkhvg 189
Cdd:cd05282  85 ----LPLGG--------EGTWQEYVVAPADDLIPVPDSISDEQAAmlyinPltawLMLTEYLKLPPGDWVIQNA------ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 190 ivglgGLGHIG---VRFAKAFGTK-VTVVSSTtgKSKDALDTLGADGFLVSTDED---QMKAAMGT--MDGIIDTVSASh 260
Cdd:cd05282 147 -----ANSAVGrmlIQLAKLLGFKtINVVRRD--EQVEELKALGADEVIDSSPEDlaqRVKEATGGagARLALDAVGGE- 218
                       250       260
                ....*....|....*....|
gi 15235757 261 SISPLIGLLKSNGKLVLLGA 280
Cdd:cd05282 219 SATRLARSLRPGGTLVNYGL 238
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
37-299 1.01e-08

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: 55.91  E-value: 1.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHClknewHSSIYPL----VPGHEIIGEVSEIGNKVSKFNLGDKVGvgcivdscrtcescre 112
Cdd:cd05286  25 GPGEVLVRNTAIGVNFIDTYF-----RSGLYPLplpfVLGVEGAGVVEAVGPGVTGFKVGDRVA---------------- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 113 dqenYCTKaiatyngvhhdgtinYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYspmkYF------------- 179
Cdd:cd05286  84 ----YAGP---------------PGAYAEYRVVPASRLVKLPDGISDETAAALLLQGLTAH----YLlretypvkpgdtv 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 180 ------GLTGpdkhvgivglgglgHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDEDQMKAAMG------ 247
Cdd:cd05286 141 lvhaaaGGVG--------------LLLTQWAKALGATVIGTVSSEEKAELARA-AGADHVINYRDEDFVERVREitggrg 205
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15235757 248 ---TMDGI-IDTVSAShsisplIGLLKSNGKLVLLGATEKPfdISAFSL-ILGRKSI 299
Cdd:cd05286 206 vdvVYDGVgKDTFEGS------LDSLRPRGTLVSFGNASGP--VPPFDLlRLSKGSL 254
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
40-282 3.63e-08

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: 54.51  E-value: 3.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEWHSSI-YPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCivdscrtcescredqenyc 118
Cdd:cd08275  28 EVRVRVEACGLNFADLMARQGLYDSAPkPPFVPGFECAGTVEAVGEGVKDFKVGDRVMGLT------------------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 119 tkaiatyngvhhdgtiNYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHvgivglgGLGH 198
Cdd:cd08275  89 ----------------RFGGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAYYALFELGNLRPGQS-------VLVH 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 199 I---GV-----RFAKAFgTKVTVVSSTTGKSKDALDTLGADGFLVSTDED---QM-KAAMGTMDGIIDTVSAShSISPLI 266
Cdd:cd08275 146 SaagGVglaagQLCKTV-PNVTVVGTASASKHEALKENGVTHVIDYRTQDyveEVkKISPEGVDIVLDALGGE-DTRKSY 223
                       250
                ....*....|....*.
gi 15235757 267 GLLKSNGKLVLLGATE 282
Cdd:cd08275 224 DLLKPMGRLVVYGAAN 239
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
36-291 5.07e-08

polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that is similar to fatty acid synthesis. Enoyl reductase reduces a double to single bond. Erythromycin is one example of a polyketide generated by 3 complex enzymes (megasynthases). 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 53.59  E-value: 5.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  36 TGEEEVRVKVLYCGICHSDLHCLKNEWHS-SIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGcivdscrTCEScredq 114
Cdd:cd08251   5 PGPGEVRIQVRAFSLNFGDLLCVRGLYPTmPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAG-------TGES----- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 115 enyctkaiatyngvhhdgtinYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHVGIVGLG 194
Cdd:cd08251  73 ---------------------MGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAGLAKGEHILIQTATG 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 195 GLGHIGVRFAKAFGTKVTVVSSTTGKsKDALDTLGADGFLVSTDED------QMKAAMGtMDGIIDTVSASHsISPLIGL 268
Cdd:cd08251 132 GTGLMAVQLARLKGAEIYATASSDDK-LEYLKQLGVPHVINYVEEDfeeeimRLTGGRG-VDVVINTLSGEA-IQKGLNC 208
                       250       260
                ....*....|....*....|....*..
gi 15235757 269 LKSNGKLVLLGAT----EKPFDISAFS 291
Cdd:cd08251 209 LAPGGRYVEIAMTalksAPSVDLSVLS 235
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
38-302 6.93e-08

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 53.54  E-value: 6.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   38 EEEVRVKVLYCGICHSDLHCLKN--EWHSSI-YPLVPGHEIIGEVSEIGNkvSKFNLGDKVGVGcIVDSCRTCESCREDQ 114
Cdd:PRK09880  27 NNGTLVQITRGGICGSDLHYYQEgkVGNFVIkAPMVLGHEVIGKIVHSDS--SGLKEGQTVAIN-PSKPCGHCKYCLSHN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  115 ENYCTK----AIATYNGvHHDGtinygGYSDHIVVDERYAVKIPHTLP---LVSAAPLlcaGISMYSPMKYFGLTGpdKH 187
Cdd:PRK09880 104 ENQCTTmrffGSAMYFP-HVDG-----GFTRYKVVDTAQCIPYPEKADekvMAFAEPL---AVAIHAAHQAGDLQG--KR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  188 VGIVGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKDALDTLGADGFLVSTDED--QMKAAMGTMDGIIDTVSASHSISPL 265
Cdd:PRK09880 173 VFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQNDDldHYKAEKGYFDVSFEVSGHPSSINTC 252
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15235757  266 IGLLKSNGKLVLLGATEKPFDISAFSLILGRKSIAGS 302
Cdd:PRK09880 253 LEVTRAKGVMVQVGMGGAPPEFPMMTLIVKEISLKGS 289
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
43-118 1.23e-07

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


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 52.92  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  43 VKVLYCGICHSDLHCLknewHSSIYPLVP----GHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYC 118
Cdd:cd08283  30 VRVTATAICGSDLHLY----HGYIPGMKKgdilGHEFMGVVEEVGPEVRNLKVGDRV-VVPFTIACGECFYCKRGLYSQC 104
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
38-354 2.26e-07

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 51.94  E-value: 2.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  38 EEEVRVKVLYCGICHSDLHCLKneWHSSI---YPLVPGHEIIGEVSEIGNkvSKFNLGDKVgvgcivdscrtcescredq 114
Cdd:cd08289  27 EGDVLIRVAYSSVNYKDGLASI--PGGKIvkrYPFIPGIDLAGTVVESND--PRFKPGDEV------------------- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 115 enyctkaIAT-YN-GVHHdgtinYGGYSDHIVVDERYAVKIPHTLPLVSAAPL----LCAGISMYSpMKYFGLTgPDKHV 188
Cdd:cd08289  84 -------IVTsYDlGVSH-----HGGYSEYARVPAEWVVPLPKGLTLKEAMILgtagFTAALSIHR-LEENGLT-PEQGP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 189 GIVGLGG--LGHIGVRFAKAFGTKVTvvsSTTGKS--KDALDTLGADGFLVSTD--EDQMKAAMGTM-DGIIDTVSASHs 261
Cdd:cd08289 150 VLVTGATggVGSLAVSILAKLGYEVV---ASTGKAdaADYLKKLGAKEVIPREElqEESIKPLEKQRwAGAVDPVGGKT- 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 262 ISPLIGLLKSNGKLVLLGATEKP-FDISAFSLILGRKSIAG--SGIGGMQETQEM-----IDFAAEHGIKAEIEIISMDY 333
Cdd:cd08289 226 LAYLLSTLQYGGSVAVSGLTGGGeVETTVFPFILRGVNLLGidSVECPMELRRRIwrrlaTDLKPTQLLNEIKQEITLDE 305
                       330       340
                ....*....|....*....|.
gi 15235757 334 VNTAMDRLAKGDVRYRFVIDI 354
Cdd:cd08289 306 LPEALKQILQGRVTGRTVVKL 326
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
43-125 2.43e-07

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: 51.86  E-value: 2.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  43 VKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGCIVdSCRTCESCREDQENYCTKAI 122
Cdd:cd08285  29 VRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGDRVIVPAIT-PDWRSVAAQRGYPSQSGGML 107

                ...
gi 15235757 123 ATY 125
Cdd:cd08285 108 GGW 110
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
37-231 5.38e-07

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: 50.72  E-value: 5.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHclkneWHSSIY------PLVPGHEIIGEVSEIGNKVSKFNLGDKVGvgcivdscrtcesc 110
Cdd:cd08250  29 GPGEVLVKNRFVGINASDIN-----FTAGRYdpgvkpPFDCGFEGVGEVVAVGEGVTDFKVGDAVA-------------- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 111 redqenyctkaiatyngvhhdgTINYGGYSDHIVVDERYAVKIPHTLPLVSaaPLLCAGISMYSPMKYFG-LTGPDKHVG 189
Cdd:cd08250  90 ----------------------TMSFGAFAEYQVVPARHAVPVPELKPEVL--PLLVSGLTASIALEEVGeMKSGETVLV 145
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15235757 190 IVGLGGLGHIGVRFAKAFGTKVTVVSSTTGKSKdALDTLGAD 231
Cdd:cd08250 146 TAAAGGTGQFAVQLAKLAGCHVIGTCSSDEKAE-FLKSLGCD 186
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
40-323 6.13e-07

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: 50.76  E-value: 6.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHcLKNEWHSS---------------------IYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgvg 98
Cdd:cd08274  30 EVLIRVGACGVNNTDIN-TREGWYSTevdgatdstgageagwwggtlSFPRIQGADIVGRVVAVGEGVDTARIGERV--- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  99 cIVDscrTCESCREDQENYctkaIATYNGVHHDGtinygGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKY 178
Cdd:cd08274 106 -LVD---PSIRDPPEDDPA----DIDYIGSERDG-----GFAEYTVVPAENAYPVNSPLSDVELATFPCSYSTAENMLER 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 179 FGLTGPDKHVGIVGLGGLGHIGVRFAKAFGTKVTVVsstTGKSK-DALDTLGADGFL---VSTDEDQMKAAMGTMDGIID 254
Cdd:cd08274 173 AGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAV---AGAAKeEAVRALGADTVIlrdAPLLADAKALGGEPVDVVAD 249
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 255 TVSAShSISPLIGLLKSNGKLVLLGATEKPF-DISAFSLILGRKSIAGSGIGGMQETQEMIDFAAEHGIK 323
Cdd:cd08274 250 VVGGP-LFPDLLRLLRPGGRYVTAGAIAGPVvELDLRTLYLKDLTLFGSTLGTREVFRRLVRYIEEGEIR 318
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
40-168 1.73e-06

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: 49.10  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNewHSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVgVGcivdscrtcescredqenyct 119
Cdd:cd05195   2 EVEVEVKAAGLNFRDVLVALG--LLPGDETPLGLECSGIVTRVGSGVTGLKVGDRV-MG--------------------- 57
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15235757 120 kaiatyngvhhdgtINYGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCA 168
Cdd:cd05195  58 --------------LAPGAFATHVRVDARLVVKIPDSLSFEEAATLPVA 92
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
43-132 3.46e-06

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: 48.46  E-value: 3.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  43 VKVLYCGICHSDLHclkneWHSSIYPLVP----GHEIIGEVSEIGNKVSKFNLGDKVgVGCIVDSCRTCESCREDQENYC 118
Cdd:cd08287  30 IRVVATCVCGSDLW-----PYRGVSPTRApapiGHEFVGVVEEVGSEVTSVKPGDFV-IAPFAISDGTCPFCRAGFTTSC 103
                        90
                ....*....|....
gi 15235757 119 TKaiATYNGVHHDG 132
Cdd:cd08287 104 VH--GGFWGAFVDG 115
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
40-313 3.55e-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: 41.94  E-value: 3.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  40 EVRVKVLYCGICHSDLHCLKNEW-HSSIYPLVPGHEIIGEVSEIGNKVSKFNLGDKVGVGcivdscrtcescredqenyc 118
Cdd:cd08292  30 EVLVRTTLSPIHNHDLWTIRGTYgYKPELPAIGGSEAVGVVDAVGEGVKGLQVGQRVAVA-------------------- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 119 tkaiatynGVHhdgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHVGIVGLGGLGH 198
Cdd:cd08292  90 --------PVH-------GTWAEYFVAPADGLVPLPDGISDEVAAQLIAMPLSALMLLDFLGVKPGQWLIQNAAGGAVGK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 199 IGVRFAKAFGTKV-TVVSSTTGKSKdaLDTLGaDGFLVSTD----EDQMKAAMGTmDGI---IDTVSASHSiSPLIGLLK 270
Cdd:cd08292 155 LVAMLAAARGINViNLVRRDAGVAE--LRALG-IGPVVSTEqpgwQDKVREAAGG-APIsvaLDSVGGKLA-GELLSLLG 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15235757 271 SNGKLVLLGA-TEKPFDISAFSLILgrKSIAGSGIGGMQETQEM 313
Cdd:cd08292 230 EGGTLVSFGSmSGEPMQISSGDLIF--KQATVRGFWGGRWSQEM 271
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
37-320 4.04e-04

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


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 41.80  E-value: 4.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  37 GEEEVRVKVLYCGICHSDLHCLKNEWHSSIY-PLVPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdscrtcescredqe 115
Cdd:cd08253  26 GPGEVLVRVHASGVNPVDTYIRAGAYPGLPPlPYVPGSDGAGVVEAVGEGVDGLKVGDRV-------------------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 116 nYCTKAiaTYNGVHhdgtinyGGYSDHIVVDERYAVKIPHTLPLVSAApllCAGISMYSpmKYFGLTGPDKHVGIVGLGG 195
Cdd:cd08253  86 -WLTNL--GWGRRQ-------GTAAEYVVVPADQLVPLPDGVSFEQGA---ALGIPALT--AYRALFHRAGAKAGETVLV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 196 L------GHIGVRFAKAFGTKVTVVSSTTGKSKDALDtLGADGFLVSTDED---QMKAAMGT--MDGIIDTVSASHsISP 264
Cdd:cd08253 151 HggsgavGHAAVQLARWAGARVIATASSAEGAELVRQ-AGADAVFNYRAEDladRILAATAGqgVDVIIEVLANVN-LAK 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15235757 265 LIGLLKSNGKLVLLGATEKPFDISAFSLIlgRKSIAGSGIGGMQETQEMIDFAAEH 320
Cdd:cd08253 229 DLDVLAPGGRIVVYGSGGLRGTIPINPLM--AKEASIRGVLLYTATPEERAAAAEA 282
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
35-332 4.25e-04

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: 41.83  E-value: 4.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEeeVRVKVLYCGICHSDLHCLKNEWHSSIYPLVPGHEIIGEVSEIGNkvSKFNLGDKV-----GVGCIVDscrtces 109
Cdd:cd08243  26 KPGW--VLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPG--GTFTPGQRVatamgGMGRTFD------- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 110 credqenyctkaiatyngvhhdgtinyGGYSDHIVVDERYAVKIPHTLP--LVSAAP--LLCAGISMYSPMKY------- 178
Cdd:cd08243  95 ---------------------------GSYAEYTLVPNEQVYAIDSDLSwaELAALPetYYTAWGSLFRSLGLqpgdtll 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 179 -------FGLTgpdkhvgivglgglghiGVRFAKAFGtkVTVVSSTTGKSK-DALDTLGADGFLV--STDEDQMKAAMGT 248
Cdd:cd08243 148 irggtssVGLA-----------------ALKLAKALG--ATVTATTRSPERaALLKELGADEVVIddGAIAEQLRAAPGG 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 249 MDGIIDTVSAShSISPLIGLLKSNGKLVLLGATEKPFDISAFSLILG-----RKSIAGSGIGGMQET--QEMIDFAAEHG 321
Cdd:cd08243 209 FDKVLELVGTA-TLKDSLRHLRPGGIVCMTGLLGGQWTLEDFNPMDDipsgvNLTLTGSSSGDVPQTplQELFDFVAAGH 287
                       330
                ....*....|..
gi 15235757 322 IKAEI-EIISMD 332
Cdd:cd08243 288 LDIPPsKVFTFD 299
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
68-231 1.22e-03

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 40.23  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  68 PLVPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdscrtcescredqenyctkaIATYNGVhhdGTINyGGYSDHIVVDE 147
Cdd:cd08272  58 PAILGCDVAGVVEAVGEGVTRFRVGDEV--------------------------YGCAGGL---GGLQ-GSLAEYAVVDA 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 148 RYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHVGIVGLGGLG-HIGVRFAKAFGTKVTvvssTTGKSKDA-- 224
Cdd:cd08272 108 RLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVgHVAVQLAKAAGARVY----ATASSEKAaf 183

                ....*..
gi 15235757 225 LDTLGAD 231
Cdd:cd08272 184 ARSLGAD 190
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
35-163 1.80e-03

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  35 KTGEEEVRVKVLYCGICHSDLHCLKnewhsSIYPL----------VPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdsc 104
Cdd:cd08290  26 PGPPNEVLVKMLAAPINPADINQIQ-----GVYPIkppttpeppaVGGNEGVGEVVKVGSGVKSLKPGDWV--------- 91
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15235757 105 rtcescredqenyctkaIATYNGVhhdGTinyggYSDHIVVDERYAVKIPHTLPLVSAA 163
Cdd:cd08290  92 -----------------IPLRPGL---GT-----WRTHAVVPADDLIKVPNDVDPEQAA 125
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
19-354 2.32e-03

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 39.46  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    19 ARDSSGHLSPFVFSRRKT--GEEEVRVKVLYCGICHSDLHCLKNewHSSI---YPLVPGHEIIGEVSEigNKVSKFNLGD 93
Cdd:TIGR02823   5 VEKEDGKVSAQVETLDLSdlPEGDVLIKVAYSSLNYKDALAITG--KGGVvrsYPMIPGIDAAGTVVS--SEDPRFREGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757    94 KVgvgcIVDSCRTcescredqenyctkaiatynGVHHDgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGIS-M 172
Cdd:TIGR02823  81 EV----IVTGYGL--------------------GVSHD-----GGYSQYARVPADWLVPLPEGLSLREAMALGTAGFTaA 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   173 YSPMKY--FGLT---GPdkhvgivglgglghIGVRFA------------KAFGTKVTVVsstTGKS--KDALDTLGADGF 233
Cdd:TIGR02823 132 LSVMALerNGLTpedGP--------------VLVTGAtggvgslavailSKLGYEVVAS---TGKAeeEDYLKELGASEV 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   234 LVSTDEDQMKAAM--GTMDGIIDTVsASHSISPLIGLLKSNGKLVLLGATEKP-FDISAFSLILGRKSIAG--SGIGGMQ 308
Cdd:TIGR02823 195 IDREDLSPPGKPLekERWAGAVDTV-GGHTLANVLAQLKYGGAVAACGLAGGPdLPTTVLPFILRGVSLLGidSVYCPMA 273
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15235757   309 ETQEM-----IDFAAEHgIKAEIEIISMDYVNTAMDRLAKGDVRYRFVIDI 354
Cdd:TIGR02823 274 LREAAwqrlaTDLKPRN-LESITREITLEELPEALEQILAGQHRGRTVVDV 323
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
68-279 4.02e-03

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


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 38.41  E-value: 4.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  68 PLVPGHEIIGEVSEIGNKVSKFNLGDKVgvgcivdscrtcescredqenYCtkaiatyngvhhdgtinYGGYSDHIVVDE 147
Cdd:cd08255  21 PLPPGYSSVGRVVEVGSGVTGFKPGDRV---------------------FC-----------------FGPHAERVVVPA 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757 148 RYAVKIPHTLPLVSAAP----------LLCAGISMYSPMKYFGLtgpdkhvgivglGGLGHIGVRFAKAFG-TKVTVVSS 216
Cdd:cd08255  63 NLLVPLPDGLPPERAALtalaatalngVRDAEPRLGERVAVVGL------------GLVGLLAAQLAKAAGaREVVGVDP 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15235757 217 TTGKSKDALDTLGADGflVSTDEDQMKAAMGtMDGIIDTVSASHSISPLIGLLKSNGKLVLLG 279
Cdd:cd08255 131 DAARRELAEALGPADP--VAADTADEIGGRG-ADVVIEASGSPSALETALRLLRDRGRVVLVG 190
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
38-302 4.75e-03

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 38.47  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757   38 EEEVRVKVLYCGICHSDLhcLKNEWHssiYPLVPGH-EIIG-EVS----EIGNKVSKFNLGDKVgvgcivdscrtcescr 111
Cdd:PTZ00354  28 RNDVLIKVSAAGVNRADT--LQRQGK---YPPPPGSsEILGlEVAgyveDVGSDVKRFKEGDRV---------------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  112 edqenyctkaIATYNGvhhdgtinyGGYSDHIVVDERYAVKIPHTLPLVSAAPLLCAGISMYSPMKYFGLTGPDKHvgiv 191
Cdd:PTZ00354  87 ----------MALLPG---------GGYAEYAVAHKGHVMHIPQGYTFEEAAAIPEAFLTAWQLLKKHGDVKKGQS---- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15235757  192 glgGLGHIG--------VRFAKAFGTKVTVVSSTTGKSkDALDTLGADGFLVSTDE----DQMKAAMG--TMDGIIDTVS 257
Cdd:PTZ00354 144 ---VLIHAGasgvgtaaAQLAEKYGAATIITTSSEEKV-DFCKKLAAIILIRYPDEegfaPKVKKLTGekGVNLVLDCVG 219
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15235757  258 ASHsISPLIGLLKSNGKLVLL----GATEKPFDISafSLILGRKSIAGS 302
Cdd:PTZ00354 220 GSY-LSETAEVLAVDGKWIVYgfmgGAKVEKFNLL--PLLRKRASIIFS 265
 
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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