NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1623245061|gb|THM84284|]
View 

NAD(P)-dependent alcohol dehydrogenase [Klebsiella pneumoniae subsp. pneumoniae]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 10-343 1.09e-177

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: 495.86  E-value: 1.09e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  10 SASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCM 89
Cdd:cd05283     7 DASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVGVGCQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  90 VDSCQQCEECAEGLENYCDHMVLTYNGPTQDApGHTLGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLR 168
Cdd:cd05283    87 VDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDG-TITQGGYADHIVVDERFVFKI--PEGlDSAAAAPLLCAGITVYSPLK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 169 HWHVGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKSFDFILNTVAAP 248
Cdd:cd05283   164 RNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAMKKAAGSLDLIIDTVSAS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 249 HNLDAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAW 328
Cdd:cd05283   244 HDLDPYLSLLKPGGTLVLVGAPEEPLPVP-PFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGINEAL 322

                         330
                  ....*....|....*
gi 1623245061 329 ERMVKGDVKYRFVID 343
Cdd:cd05283   323 ERLEKGDVRYRFVLD 337
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 10-343 1.09e-177

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: 495.86  E-value: 1.09e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  10 SASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCM 89
Cdd:cd05283     7 DASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVGVGCQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  90 VDSCQQCEECAEGLENYCDHMVLTYNGPTQDApGHTLGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLR 168
Cdd:cd05283    87 VDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDG-TITQGGYADHIVVDERFVFKI--PEGlDSAAAAPLLCAGITVYSPLK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 169 HWHVGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKSFDFILNTVAAP 248
Cdd:cd05283   164 RNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAMKKAAGSLDLIIDTVSAS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 249 HNLDAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAW 328
Cdd:cd05283   244 HDLDPYLSLLKPGGTLVLVGAPEEPLPVP-PFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGINEAL 322

                         330
                  ....*....|....*
gi 1623245061 329 ERMVKGDVKYRFVID 343
Cdd:cd05283   323 ERLEKGDVRYRFVLD 337
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 5-343 4.50e-140

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 400.26  E-value: 4.50e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   5 AIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLV 84
Cdd:COG1064     3 AAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDRV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  85 GVGCmVDSCQQCEECAEGLENYCDHmvltyngptQDAPGHTL-GGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGIT 162
Cdd:COG1064    83 GVGW-VDSCGTCEYCRSGRENLCEN---------GRFTGYTTdGGYAEYVVVPARFLVKL--PDGlDPAEAAPLLCAGIT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 163 TYSPLRHWHVGPgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAH--VKSFDF 240
Cdd:COG1064   151 AYRALRRAGVGPgdrvavigagglgHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNSSDEDPVEAVreLTGADV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 241 ILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIR 320
Cdd:COG1064   231 VIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLP-PFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIP 309

                         330       340
                  ....*....|....*....|...
gi 1623245061 321 GDEINEAWERMVKGDVKYRFVID 343
Cdd:COG1064   310 LEEANEALERLRAGKVRGRAVLD 332
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 15-345 1.69e-111

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 328.76  E-value: 1.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  15 LESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQ 94
Cdd:PLN02586   25 LSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGVIVGSCK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  95 QCEECAEGLENYCDHMVLTYNGPTQDAPgHTLGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLRHWHVG 173
Cdd:PLN02586  105 SCESCDQDLENYCPKMIFTYNSIGHDGT-KNYGGYSDMIVVDQHFVLRF--PDNlPLDAGAPLLCAGITVYSPMKYYGMT 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 174 -PGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAA-RALGADDVVVSRNEDEMAAHVKSFDFILNTVAAPHNL 251
Cdd:PLN02586  182 ePGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAiNRLGADSFLVSTDPEKMKAAIGTMDYIIDTVSAVHAL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 252 DAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAWERM 331
Cdd:PLN02586  262 GPLLGLLKVNGKLITLGLPEKPLELP-IFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRMDEINTAMERL 340

                         330
                  ....*....|....
gi 1623245061 332 VKGDVKYRFVIDSA 345
Cdd:PLN02586  341 AKSDVRYRFVIDVA 354
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 29-141 1.99e-27

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: 103.84  E-value: 1.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  29 DVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEGLENYCD 108
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNLCP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1623245061 109 HMVLTYNgptqdapgHTLGGYSQQIVVNERYVL 141
Cdd:pfam08240  81 NGRFLGY--------DRDGGFAEYVVVPERNLV 105
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 25-312 8.99e-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: 105.39  E-value: 8.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQQCEECAEGLE 104
Cdd:TIGR02822  25 PGPGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWLRRTCGVCRYCRRGAE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCDHMvlTYNGPTQDapghtlGGYSQQIVVNERYVLRITHPEAQlAAVAPLLCAGITTYSPLRHWHVGPGKKVGVVGIG 184
Cdd:TIGR02822 105 NLCPAS--RYTGWDTD------GGYAEYTTVPAAFAYRLPTGYDD-VELAPLLCAGIIGYRALLRASLPPGGRLGLYGFG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 185 GLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDV--VVSRNEDEMAAHVKsfdFILNTVAAPHNLDAfttlLKRDG 262
Cdd:TIGR02822 176 GSAHLTAQVALAQGATVHVMTRGAAARRLALALGAASAggAYDTPPEPLDAAIL---FAPAGGLVPPALEA----LDRGG 248

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1623245061 263 TMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGI 312
Cdd:TIGR02822 249 VLAVAGIHLTDTPPLNYQRHLFYERQIRSVTSNTRADAREFLELAAQHGV 298
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 32-264 1.07e-04

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 43.53  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   32 IAIAYCGVCHSDLHQARsewaGTL-YPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqceecaeglenycdhM 110
Cdd:smart00829   1 IEVRAAGLNFRDVLIAL----GLYpGEAVLGGECAGVVTRVGPGVTGLAVGDRV-------------------------M 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  111 VLTyngptqdapghtLGGYSQQIVVNERYVLRI----THPEAqlaavAPLLCAGITTYSPLRHW-----------H---- 171
Cdd:smart00829  52 GLA------------PGAFATRVVTDARLVVPIpdgwSFEEA-----ATVPVVFLTAYYALVDLarlrpgesvliHaaag 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  172 -VGpgkkvgvvgigglgHMGIKLAHAMGAHVvaFTT--SESKRNAARALG--ADDVVVSRNEDeMAAHVKS------FDF 240
Cdd:smart00829 115 gVG--------------QAAIQLARHLGAEV--FATagSPEKRDFLRALGipDDHIFSSRDLS-FADEILRatggrgVDV 177

                          250       260
                   ....*....|....*....|....
gi 1623245061  241 ILNTVAAPHnLDAFTTLLKRDGTM 264
Cdd:smart00829 178 VLNSLSGEF-LDASLRCLAPGGRF 200
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 10-343 1.09e-177

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: 495.86  E-value: 1.09e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  10 SASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCM 89
Cdd:cd05283     7 DASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDRVGVGCQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  90 VDSCQQCEECAEGLENYCDHMVLTYNGPTQDApGHTLGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLR 168
Cdd:cd05283    87 VDSCGTCEQCKSGEEQYCPKGVVTYNGKYPDG-TITQGGYADHIVVDERFVFKI--PEGlDSAAAAPLLCAGITVYSPLK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 169 HWHVGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKSFDFILNTVAAP 248
Cdd:cd05283   164 RNGVGPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDALKLGADEFIATKDPEAMKKAAGSLDLIIDTVSAS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 249 HNLDAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAW 328
Cdd:cd05283   244 HDLDPYLSLLKPGGTLVLVGAPEEPLPVP-PFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMDGINEAL 322

                         330
                  ....*....|....*
gi 1623245061 329 ERMVKGDVKYRFVID 343
Cdd:cd05283   323 ERLEKGDVRYRFVLD 337
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 5-342 3.27e-142

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: 405.55  E-value: 3.27e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   5 AIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLV 84
Cdd:cd08245     2 AAVVHAAGGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  85 GVGCMVDSCQQCEECAEGLENYCDHMVLTyngptqdaPGHTLGGYSQQIVVNERYVLRITHPEaQLAAVAPLLCAGITTY 164
Cdd:cd08245    82 GVGWLVGSCGRCEYCRRGLENLCQKAVNT--------GYTTQGGYAEYMVADAEYTVLLPDGL-PLAQAAPLLCAGITVY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 165 SPLRHWHVGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKSFDFILNT 244
Cdd:cd08245   153 SALRDAGPRPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELARKLGADEVVDSGAELDEQAAAGGADVILVT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 245 VAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEI 324
Cdd:cd08245   233 VVSGAAAEAALGGLRRGGRIVLVGLPESPPFSPDIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIETFPLDQA 312

                         330
                  ....*....|....*...
gi 1623245061 325 NEAWERMVKGDVKYRFVI 342
Cdd:cd08245   313 NEAYERMEKGDVRFRFVL 330
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 5-343 4.50e-140

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 400.26  E-value: 4.50e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   5 AIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLV 84
Cdd:COG1064     3 AAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDRV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  85 GVGCmVDSCQQCEECAEGLENYCDHmvltyngptQDAPGHTL-GGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGIT 162
Cdd:COG1064    83 GVGW-VDSCGTCEYCRSGRENLCEN---------GRFTGYTTdGGYAEYVVVPARFLVKL--PDGlDPAEAAPLLCAGIT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 163 TYSPLRHWHVGPgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAH--VKSFDF 240
Cdd:COG1064   151 AYRALRRAGVGPgdrvavigagglgHLAVQIAKALGAEVIAVDRSPEKLELARELGADHVVNSSDEDPVEAVreLTGADV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 241 ILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIR 320
Cdd:COG1064   231 VIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLP-PFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIP 309

                         330       340
                  ....*....|....*....|...
gi 1623245061 321 GDEINEAWERMVKGDVKYRFVID 343
Cdd:COG1064   310 LEEANEALERLRAGKVRGRAVLD 332
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 15-345 1.69e-111

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 328.76  E-value: 1.69e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  15 LESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQ 94
Cdd:PLN02586   25 LSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGVIVGSCK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  95 QCEECAEGLENYCDHMVLTYNGPTQDAPgHTLGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLRHWHVG 173
Cdd:PLN02586  105 SCESCDQDLENYCPKMIFTYNSIGHDGT-KNYGGYSDMIVVDQHFVLRF--PDNlPLDAGAPLLCAGITVYSPMKYYGMT 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 174 -PGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAA-RALGADDVVVSRNEDEMAAHVKSFDFILNTVAAPHNL 251
Cdd:PLN02586  182 ePGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAiNRLGADSFLVSTDPEKMKAAIGTMDYIIDTVSAVHAL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 252 DAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAWERM 331
Cdd:PLN02586  262 GPLLGLLKVNGKLITLGLPEKPLELP-IFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRMDEINTAMERL 340

                         330
                  ....*....|....
gi 1623245061 332 VKGDVKYRFVIDSA 345
Cdd:PLN02586  341 AKSDVRYRFVIDVA 354
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 11-345 6.95e-107

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 317.12  E-value: 6.95e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  11 ASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMV 90
Cdd:PLN02514   18 PSGHLSPYTYTLRKTGPEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGVIV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  91 DSCQQCEECAEGLENYCDHMVLTYNGPTQDAPgHTLGGYSQQIVVNERYVLRITHPEAQLAAvAPLLCAGITTYSPLRHW 170
Cdd:PLN02514   98 GCCGECSPCKSDLEQYCNKRIWSYNDVYTDGK-PTQGGFASAMVVDQKFVVKIPEGMAPEQA-APLLCAGVTVYSPLSHF 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 171 HV-GPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAA-RALGADDVVVSRNEDEMAAHVKSFDFILNTVAAP 248
Cdd:PLN02514  176 GLkQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEAlEHLGADDYLVSSDAAEMQEAADSLDYIIDTVPVF 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 249 HNLDAFTTLLKRDGTMTLVGAPATP--HPSPEVfnlIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINE 326
Cdd:PLN02514  256 HPLEPYLSLLKLDGKLILMGVINTPlqFVTPML---MLGRKVITGSFIGSMKETEEMLEFCKEKGLTSMIEVVKMDYVNT 332

                         330
                  ....*....|....*....
gi 1623245061 327 AWERMVKGDVKYRFVIDSA 345
Cdd:PLN02514  333 AFERLEKNDVRYRFVVDVA 351
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 15-345 2.49e-90

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 275.36  E-value: 2.49e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  15 LESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQ 94
Cdd:PLN02178   19 LSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIGSCQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  95 QCEECAEGLENYCDHMVLTYNGPTQDAPGHTlGGYSQQIVVNERYVLRIthPEAQLA-AVAPLLCAGITTYSPLRHWHVG 173
Cdd:PLN02178   99 SCESCNQDLENYCPKVVFTYNSRSSDGTRNQ-GGYSDVIVVDHRFVLSI--PDGLPSdSGAPLLCAGITVYSPMKYYGMT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 174 PGKKVGVVGIGG--LGHMGIKLAHAMGAHVVAFT-TSESKRNAARALGADDVVVSRNEDEMAAHVKSFDFILNTVAAPHN 250
Cdd:PLN02178  176 KESGKRLGVNGLggLGHIAVKIGKAFGLRVTVISrSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDFIIDTVSAEHA 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 251 LDAFTTLLKRDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAWER 330
Cdd:PLN02178  256 LLPLFSLLKVSGKLVALGLPEKPLDLP-IFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIKMSDINSAMDR 334

                         330
                  ....*....|....*
gi 1623245061 331 MVKGDVKYRFVIDSA 345
Cdd:PLN02178  335 LAKSDVRYRFVIDVA 349
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 25-343 5.39e-72

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: 227.03  E-value: 5.39e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAG-TLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQQCEECAEGL 103
Cdd:cd08297    24 PGPGEVLVKLEASGVCHTDLHAALGDWPVkPKLPLIGGHEGAGVVVAVGPGVSGLKVGDRVGVKWLYDACGKCEYCRTGD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 104 ENYCDHMVLTynGPTQDapghtlGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLR-------HW----- 170
Cdd:cd08297   104 ETLCPNQKNS--GYTVD------GTFAEYAIADARYVTPI--PDGlSFEQAAPLLCAGVTVYKALKkaglkpgDWvvisg 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 171 ---HVGpgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKSFDFI-----L 242
Cdd:cd08297   174 aggGLG--------------HLGVQYAKAMGLRVIAIDVGDEKLELAKELGADAFVDFKKSDDVEAVKELTGGGgahavV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 243 NTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGD 322
Cdd:cd08297   240 VTAVSAAAYEQALDYLRPGGTLVCVGLPPGGFIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVKPHIQVVPLE 319

                         330       340
                  ....*....|....*....|.
gi 1623245061 323 EINEAWERMVKGDVKYRFVID 343
Cdd:cd08297   320 DLNEVFEKMEEGKIAGRVVVD 340
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 23-342 4.34e-64

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: 206.33  E-value: 4.34e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  23 RDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQQCEECAEG 102
Cdd:cd08296    21 PLPGPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGWHGGHCGTCDACRRG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 103 LENYCDHMVltYNGPTQDapghtlGGYSQQIVVNERYVLRIthPEAQLAA-VAPLLCAGITTYSPLRHWHVGPGKKVGVV 181
Cdd:cd08296   101 DFVHCENGK--VTGVTRD------GGYAEYMLAPAEALARI--PDDLDAAeAAPLLCAGVTTFNALRNSGAKPGDLVAVQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 182 GIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVK--SFDFILNTVAAPHNLDAFTTLLK 259
Cdd:cd08296   171 GIGGLGHLAVQYAAKMGFRTVAISRGSDKADLARKLGAHHYIDTSKEDVAEALQElgGAKLILATAPNAKAISALVGGLA 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 260 RDGTMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAWERMVKGDVKYR 339
Cdd:cd08296   251 PRGKLLILGAAGEPVAVS-PLQLIMGRKSIHGWPSGTALDSEDTLKFSALHGVRPMVETFPLEKANEAYDRMMSGKARFR 329


                  ...
gi 1623245061 340 FVI 342
Cdd:cd08296   330 VVL 332
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-342 1.47e-53

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: 179.30  E-value: 1.47e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   1 MLINAIGTYSaSQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAV 80
Cdd:cd08298     4 MVLEKPGPIE-ENPLRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTRFSV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  81 GDLVGVGCMVDSCQQCEECAEGLENYCDHMVLTynGPTQDapghtlGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCA 159
Cdd:cd08298    83 GDRVGVPWLGSTCGECRYCRSGRENLCDNARFT--GYTVD------GGYAEYMVADERFAYPI--PEDyDDEEAAPLLCA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 160 GITTYSPLRHWHVGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSrneDEMAAhvKSFD 239
Cdd:cd08298   153 GIIGYRALKLAGLKPGQRLGLYGFGASAHLALQIARYQGAEVFAFTRSGEHQELARELGADWAGDS---DDLPP--EPLD 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 240 FILntVAAPhnLDAFTTL----LKRDGTMTLVGAPATPHPSPEvFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVAD 315
Cdd:cd08298   228 AAI--IFAP--VGALVPAalraVKKGGRVVLAGIHMSDIPAFD-YELLWGEKTIRSVANLTRQDGEEFLKLAAEIPIKPE 302

                         330       340
                  ....*....|....*....|....*..
gi 1623245061 316 IELIRGDEINEAWERMVKGDVKYRFVI 342
Cdd:cd08298   303 VETYPLEEANEALQDLKEGRIRGAAVL 329
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 25-342 1.25e-45

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: 158.88  E-value: 1.25e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTL---YPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcMVD---SCQQCEE 98
Cdd:cd05284    23 PGPGQVLVRVGGAGVCHSDLHVIDGVWGGILpykLPFTLGHENAGWVEEVGSGVDGLKEGDPV----VVHppwGCGTCRY 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  99 CAEGLENYCDHmvltyngptQDAPGHTL-GGYSQQIVVNERYVLRITHpEAQLAAVAPLLCAGITTYSPLR-HW-HVGPG 175
Cdd:cd05284    99 CRRGEENYCEN---------ARFPGIGTdGGFAEYLLVPSRRLVKLPR-GLDPVEAAPLADAGLTAYHAVKkALpYLDPG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 176 KKVGVVGIGGLGHMGIKLAHAM-GAHVVAFTTSESKRNAARALGADDVVVSRneDEMAAHVKS------FDFILNTVAAP 248
Cdd:cd05284   169 STVVVIGVGGLGHIAVQILRALtPATVIAVDRSEEALKLAERLGADHVLNAS--DDVVEEVREltggrgADAVIDFVGSD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 249 HNLDAFTTLLKRDGTMTLVGAPAtpHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAW 328
Cdd:cd05284   247 ETLALAAKLLAKGGRYVIVGYGG--HGRLPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVKVEITKFPLEDANEAL 324

                         330
                  ....*....|....
gi 1623245061 329 ERMVKGDVKYRFVI 342
Cdd:cd05284   325 DRLREGRVTGRAVL 338
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 11-342 2.51e-43

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: 152.77  E-value: 2.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  11 ASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEW------------AGTLYPCVPGHAIVGRVTAVGNAVSRY 78
Cdd:cd08240     9 PGKPLEEVEIDTPKPPGTEVLVKVTACGVCHSDLHIWDGGYdlgggktmslddRGVKLPLVLGHEIVGEVVAVGPDAADV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  79 AVGDLVGVGCMVdSCQQCEECAEGLENYCDhmvltyngptqdaPGHTL-----GGYSQQIVV-NERYVLRIthPEAQLAA 152
Cdd:cd08240    89 KVGDKVLVYPWI-GCGECPVCLAGDENLCA-------------KGRALgifqdGGYAEYVIVpHSRYLVDP--GGLDPAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 153 VAPLLCAGITTYSPLRhwHVGPGKKVGVVGIGGLGH---MGIKLAHAMG-AHVVAFTTSESKRNAARALGADDVVVSRNE 228
Cdd:cd08240   153 AATLACSGLTAYSAVK--KLMPLVADEPVVIIGAGGlglMALALLKALGpANIIVVDIDEAKLEAAKAAGADVVVNGSDP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 229 DEMAAHVKS----FDFILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPEVFnLIFRRRSIAGSMIGGIPETQEML 304
Cdd:cd08240   231 DAAKRIIKAagggVDAVIDFVNNSATASLAFDILAKGGKLVLVGLFGGEATLPLPL-LPLRALTIQGSYVGSLEELRELV 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1623245061 305 DFcAEHGIVADIELIRG--DEINEAWERMVKGDVKYRFVI 342
Cdd:cd08240   310 AL-AKAGKLKPIPLTERplSDVNDALDDLKAGKVVGRAVL 348
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
13-336 6.36e-43

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 151.77  E-value: 6.36e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  13 QPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHqARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMVDS 92
Cdd:COG1062     2 GPLEIEEVELDEPRPGEVLVRIVAAGLCHSDLH-VRDGDLPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHV-VLSFIPS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  93 CQQCEECAEGLENYCDHMvLTYNGPTQDAPGHT---------------LGGYSQQIVVNERYVLRItHPEAQLAAVAPLL 157
Cdd:COG1062    80 CGHCRYCASGRPALCEAG-AALNGKGTLPDGTSrlssadgepvghffgQSSFAEYAVVPERSVVKV-DKDVPLELAALLG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 158 CAGITTY-SPLRHWHVGPgkkvgvvgigglghmG---------------IKLAHAMGA-HVVAFTTSESKRNAARALGAD 220
Cdd:COG1062   158 CGVQTGAgAVLNTAKVRP---------------GdtvavfglggvglsaVQGARIAGAsRIIAVDPVPEKLELARELGAT 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 221 DVVVSRNEDeMAAHVKS-----FDFILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSP-EVFNLIFRRRSIAGSMI 294
Cdd:COG1062   223 HTVNPADED-AVEAVREltgggVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPPGAEISlDPFQLLLTGRTIRGSYF 301

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1623245061 295 GG------IPetqEMLDFCAEHGIVADiELIRG----DEINEAWERMVKGDV 336
Cdd:COG1062   302 GGavprrdIP---RLVDLYRAGRLPLD-ELITRryplDEINEAFDDLRSGEV 349
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 5-343 2.23e-41

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group 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: 147.46  E-value: 2.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   5 AIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLV 84
Cdd:cd08259     3 AAILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPGDRV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  85 GVgCMVDSCQQCEECAEGLENYCDHMVLtYNGPTQdapghtlGGYSQQIVVNERYVLRItHPEAQLAAVAPLLCAGITTY 164
Cdd:cd08259    83 IL-YYYIPCGKCEYCLSGEENLCRNRAE-YGEEVD-------GGFAEYVKVPERSLVKL-PDNVSDESAALAACVVGTAV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 165 SPLRHWHVGPGKKVGVVGIGGLGHMG-IKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKSFDFILN 243
Cdd:cd08259   153 HALKRAGVKKGDTVLVTGAGGGVGIHaIQLAKALGARVIAVTRSPEKLKILKELGADYVIDGSKFSEDVKKLGGADVVIE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 244 TVAAPhNLDAFTTLLKRDGTMTLVG----APATPHPSPevfnLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELI 319
Cdd:cd08259   233 LVGSP-TIEESLRSLNKGGRLVLIGnvtpDPAPLRPGL----LILKEIRIIGSISATKADVEEALKLVKEGKIKPVIDRV 307

                         330       340
                  ....*....|....*....|....*
gi 1623245061 320 RG-DEINEAWERMVKGDVKYRFVID 343
Cdd:cd08259   308 VSlEDINEALEDLKSGKVVGRIVLK 332
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 29-306 3.98e-41

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: 145.16  E-value: 3.98e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  29 DVQIAIAYCGVCHSDLHQARSEWAGTL-YPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEGLENYC 107
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPPPPkLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNL-GCGTCELCRELCPGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 108 DHMVltyngptqdapgHTLGGYSQQIVVNERYVLRI----THPEAqlaavAPLLCAGITTYSPLRHWHV----------- 172
Cdd:cd05188    80 ILGE------------GLDGGFAEYVVVPADNLVPLpdglSLEEA-----ALLPEPLATAYHALRRAGVlkpgdtvlvlg 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 173 -GPgkkvgvvgigglghMG---IKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNED----EMAAHVKSFDFILNT 244
Cdd:cd05188   143 aGG--------------VGllaAQLAKAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDleeeLRLTGGGGADVVIDA 208

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1623245061 245 VAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDF 306
Cdd:cd05188   209 VGGPETLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDL 270
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 24-343 1.09e-40

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: 145.47  E-value: 1.09e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  24 DPGPQDVQIAIAYCGVCHSDLH--QARSEWAGTLyPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVgCMVDSCQQCEECAE 101
Cdd:cd08254    23 EPGPGEVLVKVKAAGVCHSDLHilDGGVPTLTKL-PLTLGHEIAGTVVEVGAGVTNFKVGDRVAV-PAVIPCGACALCRR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 GLENYCDHMVLTYNGptQDapghtlGGYSQQIVVNERYVLRIthPEA---QLAAVAPllCAGITTYSPL-RHWHVGPGKK 177
Cdd:cd08254   101 GRGNLCLNQGMPGLG--ID------GGFAEYIVVPARALVPV--PDGvpfAQAAVAT--DAVLTPYHAVvRAGEVKPGET 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 178 VGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNE---DEMAAHVK-SFDFILNTVAAPHNLDA 253
Cdd:cd08254   169 VLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDspkDKKAAGLGgGFDVIFDFVGTQPTFED 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 254 FTTLLKRDGTMTLVG--APATPHPSpevFNLIFRRRSIAGSmIGGIPETQ-EMLDFCAEHGIVADIELIRGDEINEAWER 330
Cdd:cd08254   249 AQKAVKPGGRIVVVGlgRDKLTVDL---SDLIARELRIIGS-FGGTPEDLpEVLDLIAKGKLDPQVETRPLDEIPEVLER 324

                         330
                  ....*....|...
gi 1623245061 331 MVKGDVKYRFVID 343
Cdd:cd08254   325 LHKGKVKGRVVLV 337
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 9-342 1.19e-38

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: 140.75  E-value: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   9 YSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLyPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGC 88
Cdd:cd08279     7 HEVGKPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLPAPL-PAVLGHEGAGVVEEVGPGVTGVKPGDHV-VLS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  89 MVDSCQQCEECAEGLENYCDHMVLTYNGPTQDAPGHT------------LGGYSQQIVVNERYVLRIThPEAQLAAVAPL 156
Cdd:cd08279    85 WIPACGTCRYCSRGQPNLCDLGAGILGGQLPDGTRRFtadgepvgamcgLGTFAEYTVVPEASVVKID-DDIPLDRAALL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 157 LCAGITTYSPLRH------------WHVGpgkkvgvvgigglghmGIKLAHAMGA------HVVAFTTSESKRNAARALG 218
Cdd:cd08279   164 GCGVTTGVGAVVNtarvrpgdtvavIGCG----------------GVGLNAIQGAriagasRIIAVDPVPEKLELARRFG 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 219 ADDVVVSRNEDEMAAHVK-----SFDFILNTVAAPHNLDAFTTLLKRDGTMTLVGApatPHPSPEV----FNLIFRRRSI 289
Cdd:cd08279   228 ATHTVNASEDDAVEAVRDltdgrGADYAFEAVGRAATIRQALAMTRKGGTAVVVGM---GPPGETVslpaLELFLSEKRL 304

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1623245061 290 AGSMIGG------IPetqEMLDFCAEHGIVADiELI----RGDEINEAWERMVKGDVKyRFVI 342
Cdd:cd08279   305 QGSLYGSanprrdIP---RLLDLYRAGRLKLD-ELVtrrySLDEINEAFADMLAGENA-RGVI 362
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 25-335 2.64e-38

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: 139.50  E-value: 2.64e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEGLE 104
Cdd:COG1063    22 PGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDRVVVEPNI-PCGECRYCRRGRY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCDHMVLTyngptqdapG--HTLGGYSQQIVVNERYVLRITH--PEAQLAAVAPLLCA--GITTYSPLRHWHV-----G 173
Cdd:COG1063   101 NLCENLQFL---------GiaGRDGGFAEYVRVPAANLVKVPDglSDEAAALVEPLAVAlhAVERAGVKPGDTVlvigaG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 174 PgkkvgvvgigglghMG---IKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNEDeMAAHVKS------FDFILN 243
Cdd:COG1063   172 P--------------IGllaALAARLAGAaRVIVVDRNPERLELARELGADAVVNPREED-LVEAVREltggrgADVVIE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 244 TVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPevFNLIFRR-RSIAGSMIGGIPETQEMLDFCAEHGIVADiELIRG- 321
Cdd:COG1063   237 AVGAPAALEQALDLVRPGGTVVLVGVPGGPVPID--LNALVRKeLTLRGSRNYTREDFPEALELLASGRIDLE-PLITHr 313

                         330
                  ....*....|....*..
gi 1623245061 322 ---DEINEAWERMVKGD 335
Cdd:COG1063   314 fplDDAPEAFEAAADRA 330
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 36-343 8.49e-35

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 130.15  E-value: 8.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  36 YCGVCHSDLHQARSEWaGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQQCEECAEGLENYCDHMvltyn 115
Cdd:PRK09422   34 YCGVCHTDLHVANGDF-GDKTGRILGHEGIGIVKEVGPGVTSLKVGDRVSIAWFFEGCGHCEYCTTGRETLCRSV----- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 116 gptQDApGHTL-GGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLRHWHVGPGKKVGVVGIGGLGHMGIKL 193
Cdd:PRK09422  108 ---KNA-GYTVdGGMAEQCIVTADYAVKV--PEGlDPAQASSITCAGVTTYKAIKVSGIKPGQWIAIYGAGGLGNLALQY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 194 AH-AMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVK-SFDFILNTVAAPHNLDAFTT---LLKRDGTMTLVG 268
Cdd:PRK09422  182 AKnVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQeKTGGAHAAVVTAVAKAAFNQavdAVRAGGRVVAVG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 269 APatphpsPEVFNLIFRRR-----SIAGSMIGGIPETQEMLDFCAEHGIVADIELIRGDEINEAWERMVKGDVKYRFVID 343
Cdd:PRK09422  262 LP------PESMDLSIPRLvldgiEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQLRPLEDINDIFDEMEQGKIQGRMVID 335
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 9-343 4.09e-33

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: 125.95  E-value: 4.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   9 YSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLyPCVPGHAIVGRVTAVGNAV---SRYAVGDLVg 85
Cdd:cd08263     7 KGPNPPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELPFPP-PFVLGHEISGEVVEVGPNVenpYGLSVGDRV- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  86 VGCMVDSCQQCEECAEGLENYCDHMVLTYNGPTQDAPGHT--------------LGGYSQQIVVNERYVLRIThPEAQLA 151
Cdd:cd08263    85 VGSFIMPCGKCRYCARGKENLCEDFFAYNRLKGTLYDGTTrlfrldggpvymysMGGLAEYAVVPATALAPLP-ESLDYT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 152 AVAPLLCAGITTYSPLRHWH-VGPGKKVGVVGIGGLGHMGIKLAHAMGAH-VVAFTTSESKRNAARALGADDVVVSRNED 229
Cdd:cd08263   164 ESAVLGCAGFTAYGALKHAAdVRPGETVAVIGVGGVGSSAIQLAKAFGASpIIAVDVRDEKLAKAKELGATHTVNAAKED 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 230 EMAAhVKSF------DFILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRR-RSIAGSMiGGIPETQ- 301
Cdd:cd08263   244 AVAA-IREItggrgvDVVVEALGKPETFKLALDVVRDGGRAVVVGLAPGGATAEIPITRLVRRgIKIIGSY-GARPRQDl 321

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1623245061 302 -EMLDFcAEHGIVADIELIRG----DEINEAWERMVKGDVKYRFVID 343
Cdd:cd08263   322 pELVGL-AASGKLDPEALVTHkyklEEINEAYENLRKGLIHGRAIVE 367
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 20-310 2.47e-32

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: 122.95  E-value: 2.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  20 ITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTL-YPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMVDscqqcee 98
Cdd:COG0604    20 VPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLPPgLPFIPGSDAAGVVVAVGEGVTGFKVGDRV-AGLGRG------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  99 caeglenycdhmvltyngptqdapghtlGGYSQQIVVNERYVLRIthPE----AQLAAvapLLCAGITTYSPLRHWH--- 171
Cdd:COG0604    92 ----------------------------GGYAEYVVVPADQLVPL--PDglsfEEAAA---LPLAGLTAWQALFDRGrlk 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 -------------VGpgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDeMAAHVKS- 237
Cdd:COG0604   139 pgetvlvhgaaggVG--------------SAAVQLAKALGARVIATASSPEKAELLRALGADHVIDYREED-FAERVRAl 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 238 -----FDFILNTVAAPHnLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIG--GIPETQEMLDFCAEH 310
Cdd:COG0604   204 tggrgVDVVLDTVGGDT-LARSLRALAPGGRLVSIGAASGAPPPLDLAPLLLKGLTLTGFTLFarDPAERRAALAELARL 282
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 23-294 8.04e-30

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: 116.47  E-value: 8.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  23 RDPGPQDVQIAIAYCGVCHSDLHQARSEwAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcMVD---SCQQCEEC 99
Cdd:cd08234    20 PEPGPDEVLIKVAACGICGTDLHIYEGE-FGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDRV----AVDpniYCGECFYC 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 100 AEGLENYCDHMvltyngptqDAPGHTL-GGYSQQIVVNERYVLRI---THPEAqlAAVA-PLLCA-------GITTYSpl 167
Cdd:cd08234    95 RRGRPNLCENL---------TAVGVTRnGGFAEYVVVPAKQVYKIpdnLSFEE--AALAePLSCAvhgldllGIKPGD-- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 168 rhwHV-----GPgkkvgvvgigglghMG---IKLAHAMGAHVVAF-TTSESKRNAARALGADDVVVSRNEDEMAAHV--- 235
Cdd:cd08234   162 ---SVlvfgaGP--------------IGlllAQLLKLNGASRVTVaEPNEEKLELAKKLGATETVDPSREDPEAQKEdnp 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1623245061 236 KSFDFILNTVAAPHNLDAFTTLLKRDGTMTL--VGAPATP---HPSpevfnLIFRRR-SIAGSMI 294
Cdd:cd08234   225 YGFDVVIEATGVPKTLEQAIEYARRGGTVLVfgVYAPDARvsiSPF-----EIFQKElTIIGSFI 284
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 1-336 1.66e-28

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: 113.36  E-value: 1.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   1 MLINAIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHqARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAV 80
Cdd:cd08278     1 MKTTAAVVREPGGPFVLEDVELDDPRPDEVLVRIVATGICHTDLV-VRDGGLPTPLPAVLGHEGAGVVEAVGSAVTGLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  81 GDLVGVGcmVDSCQQCEECAEGLENYCDHMV-LTYNG-------PTQDAPGHTLGG-------YSQQIVVNERYVLRITh 145
Cdd:cd08278    80 GDHVVLS--FASCGECANCLSGHPAYCENFFpLNFSGrrpdgstPLSLDDGTPVHGhffgqssFATYAVVHERNVVKVD- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 146 PEAQLAAVAPLLCaGITT-------------YSPLRHWHVGpgkkvgvvgigglghmGIKLAHAMGAHVVAFTT------ 206
Cdd:cd08278   157 KDVPLELLAPLGC-GIQTgagavlnvlkprpGSSIAVFGAG----------------AVGLAAVMAAKIAGCTTiiavdi 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 207 SESKRNAARALGADDVVVSRNEDeMAAHVKSF-----DFILNTVAAPHNLDAFTTLLKRDGTMTLVGAPAtPHPSP--EV 279
Cdd:cd08278   220 VDSRLELAKELGATHVINPKEED-LVAAIREItgggvDYALDTTGVPAVIEQAVDALAPRGTLALVGAPP-PGAEVtlDV 297

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1623245061 280 FNLIFRRRSIAGSMIGG------IPEtqeMLDFcAEHGIVADIELIR---GDEINEAWERMVKGDV 336
Cdd:cd08278   298 NDLLVSGKTIRGVIEGDsvpqefIPR---LIEL-YRQGKFPFDKLVTfypFEDINQAIADSESGKV 359
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 8-336 9.63e-28

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: 111.38  E-value: 9.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   8 TYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHqARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVG 87
Cdd:cd05279     6 LWEKGKPLSIEEIEVAPPKAGEVRIKVVATGVCHTDLH-VIDGKLPTPLPVILGHEGAGIVESIGPGVTTLKPGDKV-IP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  88 CMVDSCQQCEECAEGLENYCDHMVLTyNGPTQDAPG------------HTLG--GYSQQIVVNERYVLRIThPEAQLAAV 153
Cdd:cd05279    84 LFGPQCGKCKQCLNPRPNLCSKSRGT-NGRGLMSDGtsrftckgkpihHFLGtsTFAEYTVVSEISLAKID-PDAPLEKV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 154 APLLC------------AGITTYSPLRHWHVGPGKKVGVvgigglghMGIKLAHAmgAHVVAFTTSESKRNAARALGADD 221
Cdd:cd05279   162 CLIGCgfstgygaavntAKVTPGSTCAVFGLGGVGLSVI--------MGCKAAGA--SRIIAVDINKDKFEKAKQLGATE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 222 VVVSRNED--------EMAAhvKSFDFILNTVAAPHNLD-AFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGS 292
Cdd:cd05279   232 CINPRDQDkpivevltEMTD--GGVDYAFEVIGSADTLKqALDATRLGGGTSVVVGVPPSGTEATLDPNDLLTGRTIKGT 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1623245061 293 MIGGIPETQEMLDFCAEH--GIVADIELIRG----DEINEAWERMVKGDV 336
Cdd:cd05279   310 VFGGWKSKDSVPKLVALYrqKKFPLDELITHvlpfEEINDGFDLMRSGES 359
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 29-141 1.99e-27

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: 103.84  E-value: 1.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  29 DVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEGLENYCD 108
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLI-PCGKCEYCREGRYNLCP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1623245061 109 HMVLTYNgptqdapgHTLGGYSQQIVVNERYVL 141
Cdd:pfam08240  81 NGRFLGY--------DRDGGFAEYVVVPERNLV 105
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 9-336 6.23e-27

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: 109.39  E-value: 6.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   9 YSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLyPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGC 88
Cdd:cd08281    15 YADSRPLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDRPRPL-PMALGHEAAGVVVEVGEGVTDLEVGDHV-VLV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  89 MVDSCQQCEECAEGLENYCD--------------HMVLTYNGptqDAPGHTLG--GYSQQIVVNERYVLRIThPEAQLAA 152
Cdd:cd08281    93 FVPSCGHCRPCAEGRPALCEpgaaangagtllsgGRRLRLRG---GEINHHLGvsAFAEYAVVSRRSVVKID-KDVPLEI 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 153 VAPLLCAGITTysplrhwhVGPGKKVGVVGIGGLGHM----GIKLAHAMGA------HVVAFTTSESKRNAARALGADDV 222
Cdd:cd08281   169 AALFGCAVLTG--------VGAVVNTAGVRPGQSVAVvglgGVGLSALLGAvaagasQVVAVDLNEDKLALARELGATAT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 223 VVSRNEDeMAAHVKSF-----DFILNTVAAPHNLDAFTTLLKRDGTMTLVGapaTPHPSPE----VFNLIFRRRSIAGSM 293
Cdd:cd08281   241 VNAGDPN-AVEQVRELtgggvDYAFEMAGSVPALETAYEITRRGGTTVTAG---LPDPEARlsvpALSLVAEERTLKGSY 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1623245061 294 IGGIPETQEMLDFCAEH--GIVADIELIRG----DEINEAWERMVKGDV 336
Cdd:cd08281   317 MGSCVPRRDIPRYLALYlsGRLPVDKLLTHrlplDEINEGFDRLAAGEA 365
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 25-292 2.47e-26

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: 107.31  E-value: 2.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTlYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEGLE 104
Cdd:cd08236    22 PGPGEVLVKVKACGICGSDIPRYLGTGAYH-PPLVLGHEFSGTVEEVGSGVDDLAVGDRVAVNPLL-PCGKCEYCKKGEY 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCDHmvLTYNGPTQDapghtlGGYSQQIVVNERYVLRIthPE----AQLAAVAPLLCA--GIttysplRHWHVGPGKKV 178
Cdd:cd08236   100 SLCSN--YDYIGSRRD------GAFAEYVSVPARNLIKI--PDhvdyEEAAMIEPAAVAlhAV------RLAGITLGDTV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 179 GVVGIGGLGHMGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNEDEM----AAHVKSFDFILNTVAAPHNLDA 253
Cdd:cd08236   164 VVIGAGTIGLLAIQWLKILGAkRVIAVDIDDEKLAVARELGADDTINPKEEDVEkvreLTEGRGADLVIEAAGSPATIEQ 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1623245061 254 FTTLLKRDGTMTLVGAPATPHPSPEV-FNLIFRR-RSIAGS 292
Cdd:cd08236   244 ALALARPGGKVVLVGIPYGDVTLSEEaFEKILRKeLTIQGS 284
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 13-343 3.40e-26

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 106.66  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  13 QPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMVDS 92
Cdd:PRK13771   11 QGYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPGDRV-ASLLYAP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  93 CQQCEECAEGLENYCDHMVltynGPTQDAPghtlGGYSQQIVVNERYVLRIthPEA---QLAAVAPllCAGITTYSPLRH 169
Cdd:PRK13771   90 DGTCEYCRSGEEAYCKNRL----GYGEELD----GFFAEYAKVKVTSLVKV--PPNvsdEGAVIVP--CVTGMVYRGLRR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 170 WHVGPGKKVGVVGIGGLGHM-GIKLAHAMGAHVVAFTTSESKrnaARALG--ADDVVVSRNEDEMAAHVKSFDFILNTVA 246
Cdd:PRK13771  158 AGVKKGETVLVTGAGGGVGIhAIQVAKALGAKVIAVTSSESK---AKIVSkyADYVIVGSKFSEEVKKIGGADIVIETVG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 247 APhNLDAFTTLLKRDGTMTLVGapaTPHPSPeVFNL-----IFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRG 321
Cdd:PRK13771  235 TP-TLEESLRSLNMGGKIIQIG---NVDPSP-TYSLrlgyiILKDIEIIGHISATKRDVEEALKLVAEGKIKPVIGAEVS 309

                         330       340
                  ....*....|....*....|...
gi 1623245061 322 -DEINEAWERMVKGDVKYRFVID 343
Cdd:PRK13771  310 lSEIDKALEELKDKSRIGKILVK 332
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 10-331 3.63e-26

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: 106.96  E-value: 3.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  10 SASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCM 89
Cdd:cd08231     8 GPGKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTDVAGEPLKVGDR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  90 V-----DSCQQCEECAEGLENYCDHmvLTYNGPTQ-DAPGHTLGGYSQQIVV-NERYVLRIthPEAQLAAV-APLLCAGI 161
Cdd:cd08231    88 VtwsvgAPCGRCYRCLVGDPTKCEN--RKKYGHEAsCDDPHLSGGYAEHIYLpPGTAIVRV--PDNVPDEVaAPANCALA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 162 TTYSPLRhwHVGPGKKVGVVGIGGLGHMGI---KLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKS 237
Cdd:cd08231   164 TVLAALD--RAGPVGAGDTVVVQGAGPLGLyavAAAKLAGArRVIVIDGSPERLELAREFGADATIDIDELPDPQRRAIV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 238 --------FDFILNTVAAPHNLDAFTTLLKRDGTMTLVG--APATP-HPSPEVFNliFRRRSIAGSMIGGIPETQEMLDF 306
Cdd:cd08231   242 rditggrgADVVIEASGHPAAVPEGLELLRRGGTYVLVGsvAPAGTvPLDPERIV--RKNLTIIGVHNYDPSHLYRAVRF 319

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1623245061 307 CAEH-------GIVADIelIRGDEINEAWERM 331
Cdd:cd08231   320 LERTqdrfpfaELVTHR--YPLEDINEALELA 349
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 13-279 7.22e-26

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: 105.76  E-value: 7.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  13 QPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGcMVDS 92
Cdd:cd08260    11 EPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVP-FVLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  93 CQQCEECAEGLENYCDHmvltyngptQDAPGHTL-GGYSQQIVVNERYVLRITHPEAQLAAVAPLL-CAGITTYSPLRHW 170
Cdd:cd08260    90 CGTCPYCRAGDSNVCEH---------QVQPGFTHpGSFAEYVAVPRADVNLVRLPDDVDFVTAAGLgCRFATAFRALVHQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 171 -HVGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKSF-----DFILNT 244
Cdd:cd08260   161 aRVKPGEWVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGAVATVNASEVEDVAAAVRDLtgggaHVSVDA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1623245061 245 VAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPEV 279
Cdd:cd08260   241 LGIPETCRNSVASLRKRGRHVQVGLTLGEEAGVAL 275
adh_fam_2 TIGR02822
zinc-binding alcohol dehydrogenase family protein; Members of this model form a distinct ...
 25-312 8.99e-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: 105.39  E-value: 8.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQQCEECAEGLE 104
Cdd:TIGR02822  25 PGPGELLVRVRACGVCRTDLHVSEGDLPVHRPRVTPGHEVVGEVAGRGADAGGFAVGDRVGIAWLRRTCGVCRYCRRGAE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCDHMvlTYNGPTQDapghtlGGYSQQIVVNERYVLRITHPEAQlAAVAPLLCAGITTYSPLRHWHVGPGKKVGVVGIG 184
Cdd:TIGR02822 105 NLCPAS--RYTGWDTD------GGYAEYTTVPAAFAYRLPTGYDD-VELAPLLCAGIIGYRALLRASLPPGGRLGLYGFG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 185 GLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDV--VVSRNEDEMAAHVKsfdFILNTVAAPHNLDAfttlLKRDG 262
Cdd:TIGR02822 176 GSAHLTAQVALAQGATVHVMTRGAAARRLALALGAASAggAYDTPPEPLDAAIL---FAPAGGLVPPALEA----LDRGG 248

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1623245061 263 TMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGI 312
Cdd:TIGR02822 249 VLAVAGIHLTDTPPLNYQRHLFYERQIRSVTSNTRADAREFLELAAQHGV 298
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
188-309 1.35e-25

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 99.60  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 188 HMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNED-----EMAAHVKSFDFILNTVAAPHNLDAFTTLLKRDG 262
Cdd:pfam00107   4 LAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHVINPKETDlveeiKELTGGKGVDVVFDCVGSPATLEQALKLLRPGG 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1623245061 263 TMTLVGAPATPHPSPeVFNLIFRRRSIAGSMIGGIPETQEMLDFCAE 309
Cdd:pfam00107  84 RVVVVGLPGGPLPLP-LAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 23-334 1.54e-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: 102.01  E-value: 1.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  23 RDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYP-CVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAE 101
Cdd:cd08239    20 PVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQgVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHYV-GCGACRNCRR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 GLENYCDHMVLTYnGPTQDapghtlGGYSQQIVVNERYVLRIThPEAQLAAVAPLLCAGITTYSPLRHWHVGPGKKVGVV 181
Cdd:cd08239    99 GWMQLCTSKRAAY-GWNRD------GGHAEYMLVPEKTLIPLP-DDLSFADGALLLCGIGTAYHALRRVGVSGRDTVLVV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 182 GIGGLGHMGIKLAHAMGAH-VVAFTTSESKRNAARALGADDVVVSRNEDEMA----AHVKSFDFILNTVAAPH-NLDAFT 255
Cdd:cd08239   171 GAGPVGLGALMLARALGAEdVIGVDPSPERLELAKALGADFVINSGQDDVQEirelTSGAGADVAIECSGNTAaRRLALE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 256 TLLKRdGTMTLVGAPATPH--PSPEvfnLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADiELIRG----DEINEAWE 329
Cdd:cd08239   251 AVRPW-GRLVLVGEGGELTieVSND---LIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVD-RLVTHrfglDQAPEAYA 325


                  ....*
gi 1623245061 330 RMVKG 334
Cdd:cd08239   326 LFAQG 330
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 25-271 9.24e-24

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


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 99.56  E-value: 9.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLY---PCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqceecae 101
Cdd:cd05289    25 PGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPltlPLIPGHDVAGVVVAVGPGVTGFKVGDEV----------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 glenYCDhmvltyngptqdAPGHTLGGYSQQIVVNERYVLR----ITHPEAqlaAVAPLlcAGITTYSPLRHWH------ 171
Cdd:cd05289    88 ----FGM------------TPFTRGGAYAEYVVVPADELALkpanLSFEEA---AALPL--AGLTAWQALFELGglkagq 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 ----------VGpgkkvgvvgigglgHMGIKLAHAMGAHVVAfTTSESKRNAARALGADDVVVSRNED-EMAAHVKSFDF 240
Cdd:cd05289   147 tvlihgaaggVG--------------SFAVQLAKARGARVIA-TASAANADFLRSLGADEVIDYTKGDfERAAAPGGVDA 211

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1623245061 241 ILNTVAAPHNLDAFtTLLKRDGTM-TLVGAPA 271
Cdd:cd05289   212 VLDTVGGETLARSL-ALVKPGGRLvSIAGPPP 242
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 5-342 5.56e-23

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: 98.18  E-value: 5.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   5 AIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQArSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLV 84
Cdd:cd08277     5 AAVAWEAGKPLVIEEIEVAPPKANEVRIKMLATSVCHTDILAI-EGFKATLFPVILGHEGAGIVESVGEGVTNLKPGDKV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  85 gVGCMVDSCQQCEECAEGLENYCDHMVLTYNGPTQDAPG----------HTLG--GYSQQIVVNERYVLRItHPEAQLAA 152
Cdd:cd08277    84 -IPLFIGQCGECSNCRSGKTNLCQKYRANESGLMPDGTSrftckgkkiyHFLGtsTFSQYTVVDENYVAKI-DPAAPLEH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 153 VAPLLCAGITTY-SPLRHWHVGPGKKVGVVGIGglghmGIKLAHAMGAH------VVAFTTSESKRNAARALGADDVVVS 225
Cdd:cd08277   162 VCLLGCGFSTGYgAAWNTAKVEPGSTVAVFGLG-----AVGLSAIMGAKiagasrIIGVDINEDKFEKAKEFGATDFINP 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 226 RNEDEMAAHVKS------FDFILNTVAAPHNL-DAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFrRRSIAGSMIGGI- 297
Cdd:cd08277   237 KDSDKPVSEVIRemtgggVDYSFECTGNADLMnEALESTKLGWGVSVVVGVPPGAELSIRPFQLIL-GRTWKGSFFGGFk 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1623245061 298 --PETQEMLDFCAEHGIVADiELI----RGDEINEAWERMVKGDvKYRFVI 342
Cdd:cd08277   316 srSDVPKLVSKYMNKKFDLD-ELIthvlPFEEINKGFDLMKSGE-CIRTVI 364
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 25-293 7.65e-23

(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: 97.61  E-value: 7.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLH-----------QARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMvDSC 93
Cdd:cd08233    22 VKPGEVKIKVAWCGICGSDLHeyldgpifiptEGHPHLTGETAPVTLGHEFSGVVVEVGSGVTGFKVGDRVVVEPT-IKC 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  94 QQCEECAEGLENYCDHMV---LTYNGptqdapghtlGGYSQQIVVNERYVLRIthPE----AQLAAVAPLLCAgittysp 166
Cdd:cd08233   101 GTCGACKRGLYNLCDSLGfigLGGGG----------GGFAEYVVVPAYHVHKL--PDnvplEEAALVEPLAVA------- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 167 lrhWH-----------------VGPgkkvgvvgigglghMG---IKLAHAMGAH-VVAFTTSESKRNAARALGADDVVVS 225
Cdd:cd08233   162 ---WHavrrsgfkpgdtalvlgAGP--------------IGlltILALKAAGASkIIVSEPSEARRELAEELGATIVLDP 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1623245061 226 RNEDEMAAhVKS------FDFILNTVAAPHNLDAFTTLLKRDGTMTLV---GAPATPHPspevFNLIFRRRSIAGSM 293
Cdd:cd08233   225 TEVDVVAE-VRKltggggVDVSFDCAGVQATLDTAIDALRPRGTAVNVaiwEKPISFNP----NDLVLKEKTLTGSI 296
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 25-277 1.02e-22

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: 96.92  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTL---YPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAE 101
Cdd:cd08232    19 PGPGEVRVRVAAGGICGSDLHYYQHGGFGTVrlrEPMVLGHEVSGVVEAVGPGVTGLAPGQRVAVNPSR-PCGTCDYCRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 GLENYCDHMvlTYNGPTQDAPgHTLGGYSQQIVVNERYVLRIthPEA---QLAAVA-PLLCA--GITTYSPLRHWHV--- 172
Cdd:cd08232    98 GRPNLCLNM--RFLGSAMRFP-HVQGGFREYLVVDASQCVPL--PDGlslRRAALAePLAVAlhAVNRAGDLAGKRVlvt 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 173 --GPGKKvgvvgigglghMGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNE--DEMAAHVKSFDFILNTVAA 247
Cdd:cd08232   173 gaGPIGA-----------LVVAAARRAGAaEIVATDLADAPLAVARAMGADETVNLARDplAAYAADKGDFDVVFEASGA 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 1623245061 248 PHNLDAFTTLLKRDGTMTLVGAPATPHPSP 277
Cdd:cd08232   242 PAALASALRVVRPGGTVVQVGMLGGPVPLP 271
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 25-335 8.46e-22

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: 8.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEGLE 104
Cdd:cd08235    22 PGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDRVFVAPHV-PCGECHYCLRGNE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCdhmvltyngPTQDAPGHTL-GGYSQQIVV-----NERYVLRIthPE----AQLAAVAPLLCAgittYSPLRHWHVGP 174
Cdd:cd08235   101 NMC---------PNYKKFGNLYdGGFAEYVRVpawavKRGGVLKL--PDnvsfEEAALVEPLACC----INAQRKAGIKP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 175 GKKVGVVGIGGLGHMGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNEDEMAAhVKS------FDFILntVAA 247
Cdd:cd08235   166 GDTVLVIGAGPIGLLHAMLAKASGArKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEK-VREltdgrgADVVI--VAT 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 248 PhNLDAFTT---LLKRDGTMTLVGAPATPHPSPEVFNLIFRR-RSIAGSMIGGIPETQEMLDFcAEHGIVADIELIRG-- 321
Cdd:cd08235   243 G-SPEAQAQaleLVRKGGRILFFGGLPKGSTVNIDPNLIHYReITITGSYAASPEDYKEALEL-IASGKIDVKDLITHrf 320

                         330
                  ....*....|....*.
gi 1623245061 322 --DEINEAWERMVKGD 335
Cdd:cd08235   321 plEDIEEAFELAADGK 336
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 25-293 4.17e-21

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: 91.99  E-value: 4.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDSCQQCEECAEGLE 104
Cdd:cd08258    24 PGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVSETTFSTCGRCPYCRRGDY 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCDHMVLTynGPTQDapghtlGGYSQQIVVNERYVLRIthPE---AQLAAVA-PLLCA--GITTYSPLRHWH----VGP 174
Cdd:cd08258   104 NLCPHRKGI--GTQAD------GGFAEYVLVPEESLHEL--PEnlsLEAAALTePLAVAvhAVAERSGIRPGDtvvvFGP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 175 GKkvgvvgigglghMGI---KLAHAMGAHVVAFTTSESK--RNAARALGADDVVVSrnEDEMAAHVKSFD--FILNTV-- 245
Cdd:cd08258   174 GP------------IGLlaaQVAKLQGATVVVVGTEKDEvrLDVAKELGADAVNGG--EEDLAELVNEITdgDGADVVie 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1623245061 246 ---AAPHNLDAFtTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSM 293
Cdd:cd08258   240 csgAVPALEQAL-ELLRKGGRIVQVGIFGPLAASIDVERIIQKELSVIGSR 289
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 24-336 2.86e-19

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: 87.31  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  24 DPGPQDVQIAIAYCGVCHSDLHqARSEWAGTL--YPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAE 101
Cdd:cd08266    24 EPGPDEVLVRVKAAALNHLDLW-VRRGMPGIKlpLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPGI-SCGRCEYCLA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 GLENYCDHM-VLTYngptqdapgHTLGGYSQQIVVNERYVLRIthPEA---QLAAVAPLlcagitTYspLRHWH------ 171
Cdd:cd08266   102 GRENLCAQYgILGE---------HVDGGYAEYVAVPARNLLPI--PDNlsfEEAAAAPL------TF--LTAWHmlvtra 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 ----------------VGpgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHV 235
Cdd:cd08266   163 rlrpgetvlvhgagsgVG--------------SAAIQIAKLFGATVIATAGSEDKLERAKELGADYVIDYRKEDFVREVR 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 236 K-----SFDFILNTVAAPHNLDAFtTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEH 310
Cdd:cd08266   229 EltgkrGVDVVVEHVGAATWEKSL-KSLARGGRLVTCGATTGYEAPIDLRHVFWRQLSILGSTMGTKAELDEALRLVFRG 307

                         330       340
                  ....*....|....*....|....*..
gi 1623245061 311 GIVADIELIRG-DEINEAWERMVKGDV 336
Cdd:cd08266   308 KLKPVIDSVFPlEEAAEAHRRLESREQ 334
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 24-334 3.33e-18

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 83.80  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  24 DPGPQDVQIAIAYCGVCHSDLHQARSEWAGTL---YPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMvdscqqceeca 100
Cdd:cd08267    23 TPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLgrpFPPIPGMDFAGEVVAVGSGVTRFKVGDEV-FGRL----------- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 101 eglenycdhmvltyngptqdaPGHTLGGYSQQIVVNERYVLR----ITHPEAqlAAVApllCAGITTYSPLRHWH----- 171
Cdd:cd08267    91 ---------------------PPKGGGALAEYVVAPESGLAKkpegVSFEEA--AALP---VAGLTALQALRDAGkvkpg 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 -----------VGpgkkvgvvgigglgHMGIKLAHAMGAHVVAfTTSESKRNAARALGADDVVVSRNEDEMA--AHVKSF 238
Cdd:cd08267   145 qrvlingasggVG--------------TFAVQIAKALGAHVTG-VCSTRNAELVRSLGADEVIDYTTEDFVAltAGGEKY 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 239 DFILNTVAApHNLDAFTTL--LKRDGTMTLVGAPAT----PHPSPEVFNLIFRRRSIAGSMiggiPETQEMLDFCAEHgi 312
Cdd:cd08267   210 DVIFDAVGN-SPFSLYRASlaLKPGGRYVSVGGGPSglllVLLLLPLTLGGGGRRLKFFLA----KPNAEDLEQLAEL-- 282

                         330       340
                  ....*....|....*....|....*....
gi 1623245061 313 VAD------IELI-RGDEINEAWERMVKG 334
Cdd:cd08267   283 VEEgklkpvIDSVyPLEDAPEAYRRLKSG 311
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 23-292 9.34e-18

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: 83.33  E-value: 9.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  23 RDPGPQDVQIAIAYCGVCHSDLHQARSEWAG-------TLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQ 95
Cdd:cd08265    47 PNLKPDEILIRVKACGICGSDIHLYETDKDGyilypglTEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTAEEMM-WCGM 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  96 CEECAEGLENYCDHMVLTynGPTQDapghtlGGYSQQIVVNERYVLRIT-----HPEAQL----AAVAPLLCA------- 159
Cdd:cd08265   126 CRACRSGSPNHCKNLKEL--GFSAD------GAFAEYIAVNARYAWEINelreiYSEDKAfeagALVEPTSVAynglfir 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 160 --GITTYSPLRHWHVGPGKKVgvvgigglghmGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVK 236
Cdd:cd08265   198 ggGFRPGAYVVVYGAGPIGLA-----------AIALAKAAGAsKVIAFEISEERRNLAKEMGADYVFNPTKMRDCLSGEK 266

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1623245061 237 SFD---------FILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHP-SPEVFNLifRRRSIAGS 292
Cdd:cd08265   267 VMEvtkgwgadiQVEAAGAPPATIPQMEKSIAINGKIVYIGRAATTVPlHLEVLQV--RRAQIVGA 330
mycoS_dep_FDH TIGR03451
S-(hydroxymethyl)mycothiol dehydrogenase; Members of this protein family are ...
 10-336 1.41e-17

S-(hydroxymethyl)mycothiol dehydrogenase; Members of this protein family are mycothiol-dependent formaldehyde dehydrogenase (EC 1.2.1.66). This protein is found, so far, only in the Actinobacteria (Mycobacterium sp., Streptomyces sp., Corynebacterium sp., and related species), where mycothione replaces glutathione. [Cellular processes, Detoxification]


Pssm-ID: 132492 [Multi-domain]  Cd Length: 358  Bit Score: 82.54  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  10 SASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQaRSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCM 89
Cdd:TIGR03451   9 SKGAPVELETIVVPDPGPGEVIVDIQACGVCHTDLHY-REGGINDEFPFLLGHEAAGVVEAVGEGVTDVAPGDYV-VLNW 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  90 VDSCQQCEECAEGLENYC-------DHMVLTYNGPTQDAPGhtLGGYSQQIVVNERYVLRItHPEAQLAAVAPLLC---- 158
Cdd:TIGR03451  87 RAVCGQCRACKRGRPWYCfdthnatQKMTLTDGTELSPALG--IGAFAEKTLVHAGQCTKV-DPAADPAAAGLLGCgvma 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 159 ---AGITTYSPLRHWHVGPGKKVGVVGIGGLghmGIKLAHAMgaHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAhV 235
Cdd:TIGR03451 164 glgAAVNTGGVKRGDSVAVIGCGGVGDAAIA---GAALAGAS--KIIAVDIDDRKLEWAREFGATHTVNSSGTDPVEA-I 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 236 KSF------DFILNTVAAPHNL-DAFTTllkRD--GTMTLVGAPaTPH-----PSPEVFNlifRRRSIAGSMIGG-IPET 300
Cdd:TIGR03451 238 RALtggfgaDVVIDAVGRPETYkQAFYA---RDlaGTVVLVGVP-TPDmtlelPLLDVFG---RGGALKSSWYGDcLPER 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1623245061 301 Q--EMLDFCAEHGIVAD---IELIRGDEINEAWERMVKGDV 336
Cdd:TIGR03451 311 DfpMLVDLYLQGRLPLDafvTERIGLDDVEEAFDKMHAGDV 351
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 25-233 6.54e-17

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: 80.31  E-value: 6.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQarseWAGT----LYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcMVD---SCQQCE 97
Cdd:cd08261    22 PGAGEVLVRVKRVGICGSDLHI----YHGRnpfaSYPRILGHELSGEVVEVGEGVAGLKVGDRV----VVDpyiSCGECY 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  98 ECAEGLENYCDHM-VLtyngptqdapG-HTLGGYSQQIVVNERYVLRITH-PEAQLAAVAPLLCAgittYSPLRHWHVGP 174
Cdd:cd08261    94 ACRKGRPNCCENLqVL----------GvHRDGGFAEYIVVPADALLVPEGlSLDQAALVEPLAIG----AHAVRRAGVTA 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1623245061 175 GKKVGVvgigglghMG--------IKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAA 233
Cdd:cd08261   160 GDTVLV--------VGagpiglgvIQVAKARGARVIVVDIDDERLEFARELGADDTINVGDEDVAAR 218
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 25-307 1.35e-16

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: 79.32  E-value: 1.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLyPCVPGHAIVGRVTAVGNAVSRYAVGDLVGV-GCMVDScqQCEECAEGL 103
Cdd:cd08264    24 PGPGEVLIRVKMAGVNPVDYNVINAVKVKPM-PHIPGAEFAGVVEEVGDHVKGVKKGDRVVVyNRVFDG--TCDMCLSGN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 104 ENYCDhmvltyNG-----PTQdapghtlGGYSQQIVVNERYVLRIthPEA---QLAAVAPLlcAGITTYSPLRHWHVGPG 175
Cdd:cd08264   101 EMLCR------NGgiigvVSN-------GGYAEYIVVPEKNLFKI--PDSisdELAASLPV--AALTAYHALKTAGLGPG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 176 KKVGVVGIGGLGHM-GIKLAHAMGAHVVAFttseSKRNAARALGADDVVVSRN-EDEMAAHVKSFDFILNTVAAPHnLDA 253
Cdd:cd08264   164 ETVVVFGASGNTGIfAVQLAKMMGAEVIAV----SRKDWLKEFGADEVVDYDEvEEKVKEITKMADVVINSLGSSF-WDL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1623245061 254 FTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFC 307
Cdd:cd08264   239 SLSVLGRGGRLVTFGTLTGGEVKLDLSDLYSKQISIIGSTGGTRKELLELVKIA 292
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 24-291 1.86e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 79.18  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  24 DPGPQDVQIAIAYCGVCHSDL--HQARSEWAgTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGcmvdscqqceecae 101
Cdd:cd08268    24 APGAGEVLIRVEAIGLNRADAmfRRGAYIEP-PPLPARLGYEAAGVVEAVGAGVTGFAVGDRVSVI-------------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 glenycdhmvltyngPTQDApgHTLGGYSQQIVVNERYVLRitHPE---AQLAAVapLLCAGITTYSPLRHWH------- 171
Cdd:cd08268    89 ---------------PAADL--GQYGTYAEYALVPAAAVVK--LPDglsFVEAAA--LWMQYLTAYGALVELAglrpgds 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 ---------VGPgkkvgvvgigglghMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNED---EMAAHV--KS 237
Cdd:cd08268   148 vlitaasssVGL--------------AAIQIANAAGATVIATTRTSEKRDALLALGAAHVIVTDEEDlvaEVLRITggKG 213

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1623245061 238 FDFILNTVAAPHnLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAG 291
Cdd:cd08268   214 VDVVFDPVGGPQ-FAKLADALAPGGTLVVYGALSGEPTPFPLKAALKKSLTFRG 266
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 25-331 2.47e-14

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 72.95  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEW-AGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMvdscqqceecaegl 103
Cdd:cd08276    25 PGPGEVLVRVHAVSLNYRDLLILNGRYpPPVKDPLIPLSDGAGEVVAVGEGVTRFKVGDRV-VPTF-------------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 104 enycdHMVLTYNGPTQDAPGHTLGG-----YSQQIVVNERYVLRI----THPEAqlaavAPLLCAGITTYSPLRHW-HVG 173
Cdd:cd08276    90 -----FPNWLDGPPTAEDEASALGGpidgvLAEYVVLPEEGLVRApdhlSFEEA-----ATLPCAGLTAWNALFGLgPLK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 174 PGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKS------FDFILNTVAA 247
Cdd:cd08276   160 PGDTVLVQGTGGVSLFALQFAKAAGARVIATSSSDEKLERAKALGADHVINYRTTPDWGEEVLKltggrgVDHVVEVGGP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 248 ---PHNLDAfttlLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIELIRG-DE 323
Cdd:cd08276   240 gtlAQSIKA----VAPGGVISLIGFLSGFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAIEAHRIRPVIDRVFPfEE 315


                  ....*...
gi 1623245061 324 INEAWERM 331
Cdd:cd08276   316 AKEAYRYL 323
dearomat_had TIGR03201
6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase; Members of this protein family are ...
 10-220 5.98e-14

6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase; Members of this protein family are 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase, an enzyme in the anaerobic metabolism of aromatic enzymes by way of benzoyl-CoA, as seen in Thauera aromatica, Geobacter metallireducens, and Azoarcus sp. The experimentally characterized form from T. aromatica uses only NAD+, not NADP+. Note that Rhodopseudomonas palustris uses a different pathway to perform a similar degradation of benzoyl-CoA to 3-hydroxpimelyl-CoA.


Pssm-ID: 132245 [Multi-domain]  Cd Length: 349  Bit Score: 71.86  E-value: 5.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  10 SASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLhqarsewaGTLYPCVP---------GHAIVGRVTAVGNAVSRYaV 80
Cdd:TIGR03201   6 EPGKPMVKTRVEIPELGAGDVVVKVAGCGVCHTDL--------SYYYMGVRtnhalplalGHEISGRVIQAGAGAASW-I 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  81 GDLVGVGCMVdSCQQCEECAEGLENYCDhmvltyngpTQDAPGHTL-GGYSQQIVVNERYV-----LRITHPEAQLAAVA 154
Cdd:TIGR03201  77 GKAVIVPAVI-PCGECELCKTGRGTICR---------AQKMPGNDMqGGFASHIVVPAKGLcvvdeARLAAAGLPLEHVS 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1623245061 155 PLLCAGITTYSPLRHWHVGPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGAD 220
Cdd:TIGR03201 147 VVADAVTTPYQAAVQAGLKKGDLVIVIGAGGVGGYMVQTAKAMGAAVVAIDIDPEKLEMMKGFGAD 212
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 20-286 1.31e-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: 70.46  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  20 ITRRDPGPQDVQIAIAYCGVCHSDLH---QARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqc 96
Cdd:cd08269    12 HPRPTPGPGQVLVRVEGCGVCGSDLPafnQGRPWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRV------------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  97 eecaeglenycdhMVLTYngptqdapghtlGGYSQQIVVNERYVLRIthPEAQLA---AVAPLLCA--GITTYSPLRHWH 171
Cdd:cd08269    80 -------------AGLSG------------GAFAEYDLADADHAVPL--PSLLDGqafPGEPLGCAlnVFRRGWIRAGKT 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 VgpgkkvgvvGIGGLGHMG---IKLAHAMGAH-VVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVK-----SFDFIL 242
Cdd:cd08269   133 V---------AVIGAGFIGllfLQLAAAAGARrVIAIDRRPARLALARELGATEVVTDDSEAIVERVREltggaGADVVI 203

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1623245061 243 NTVAAPHNLDAFTTLLKRDGTMTLVGAPATpHPSPEVFNLIFRR 286
Cdd:cd08269   204 EAVGHQWPLDLAGELVAERGRLVIFGYHQD-GPRPVPFQTWNWK 246
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 14-229 1.47e-13

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: 70.61  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  14 PLESMAITRRDPGPQD---VQIAIAYCGVCHSDL------HQARSEwagtlYPCVPGHAIVGRVTAVGNAVSRYAVGDLV 84
Cdd:cd08241    11 GPEDLVLEEVPPEPGApgeVRIRVEAAGVNFPDLlmiqgkYQVKPP-----LPFVPGSEVAGVVEAVGEGVTGFKVGDRV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  85 GVGCMvdscqqceecaeglenycdhmvltyngptqdapghtLGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITT 163
Cdd:cd08241    86 VALTG------------------------------------QGGFAEEVVVPAAAVFPL--PDGlSFEEAAALPVTYGTA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 164 YSPLRH--------W---H-----VGPgkkvgvvgigglghMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRN 227
Cdd:cd08241   128 YHALVRrarlqpgeTvlvLgaaggVGL--------------AAVQLAKALGARVIAAASSEEKLALARALGADHVIDYRD 193


                  ..
gi 1623245061 228 ED 229
Cdd:cd08241   194 PD 195
PRK10083 PRK10083
putative oxidoreductase; Provisional
 17-163 2.58e-13

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 69.77  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  17 SMAITRR---DPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSC 93
Cdd:PRK10083   11 SLAIEERpipQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGERVAVDPVI-SC 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1623245061  94 QQCEECAEGLENYCDHMVLTynGPTQDapghtlGGYSQQIVVNERYVLRITH--PEAQLAAVAPLLCAGITT 163
Cdd:PRK10083   90 GHCYPCSIGKPNVCTSLVVL--GVHRD------GGFSEYAVVPAKNAHRIPDaiADQYAVMVEPFTIAANVT 153
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 25-292 2.70e-13

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 69.78  E-value: 2.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARsewaGtLYPCVPGHAIV------GRVTAVGNAVSRYAVGDLVgvgcmvdscqqcee 98
Cdd:cd05276    25 PGPGEVLIRVAAAGVNRADLLQRQ----G-LYPPPPGASDIlglevaGVVVAVGPGVTGWKVGDRV-------------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  99 CAeglenycdhmvLTyngptqdaPGhtlGGYSQQIVVNERYVLRIthPE----AQLAAVAPLLCagiTTYSPLRH----- 169
Cdd:cd05276    86 CA-----------LL--------AG---GGYAEYVVVPAGQLLPV--PEglslVEAAALPEVFF---TAWQNLFQlgglk 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 170 ------WH-----VGpgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNED---EMAAHV 235
Cdd:cd05276   139 agetvlIHggasgVG--------------TAAIQLAKALGARVIATAGSEEKLEACRALGADVAINYRTEDfaeEVKEAT 204

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1623245061 236 --KSFDFILNTVAAPH---NLDAfttlLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGS 292
Cdd:cd05276   205 ggRGVDVILDMVGGDYlarNLRA----LAPDGRLVLIGLLGGAKAELDLAPLLRKRLTLTGS 262
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 25-238 1.54e-12

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: 67.47  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQaRSewaGtLYPC----VPGHAIVGRVTAVGNAVSRYAVGDLVGvgcmvdscqqceeca 100
Cdd:cd05286    24 PGPGEVLVRNTAIGVNFIDTYF-RS---G-LYPLplpfVLGVEGAGVVEAVGPGVTGFKVGDRVA--------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 101 eglenycdhmvltYNGPtqdapghtLGGYSQQIVVNERYVLRIthPEA-QLAAVAPLLCAGITTYSPLRHWH-------- 171
Cdd:cd05286    84 -------------YAGP--------PGAYAEYRVVPASRLVKL--PDGiSDETAAALLLQGLTAHYLLRETYpvkpgdtv 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1623245061 172 --------VGpgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEmAAHVKSF 238
Cdd:cd05286   141 lvhaaaggVG--------------LLLTQWAKALGATVIGTVSSEEKAELARAAGADHVINYRDEDF-VERVREI 200
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 24-110 4.99e-12

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: 65.98  E-value: 4.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  24 DPGPQDVQIAIAYCGVCHSDLH----------QARSewagtlyPCVPGHAIVGRVTAVGNAVSRYAVGDLVGV--GCmvd 91
Cdd:cd05285    19 EPGPGEVLVRVRAVGICGSDVHyykhgrigdfVVKE-------PMVLGHESAGTVVAVGSGVTHLKVGDRVAIepGV--- 88

                          90
                  ....*....|....*....
gi 1623245061  92 SCQQCEECAEGLENYCDHM 110
Cdd:cd05285    89 PCRTCEFCKSGRYNLCPDM 107
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 25-285 8.54e-12

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: 65.36  E-value: 8.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTlYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMVDSCQQCEECAEGLE 104
Cdd:cd08284    23 QDPTDAIVKVTAAAICGSDLHIYRGHIPST-PGFVLGHEFVGEVVEVGPEVRTLKVGDRV-VSPFTIACGECFYCRRGQS 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCDHMVLTYNGPTQdapghTLGGYSQQIVvneryvlRITHPEAQLAAV-------APLLCAGI--TTYSPLRHWHVGPG 175
Cdd:cd08284   101 GRCAKGGLFGYAGSP-----NLDGAQAEYV-------RVPFADGTLLKLpdglsdeAALLLGDIlpTGYFGAKRAQVRPG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 176 KKVGVVGIGGLGHMGIKLAHAMGAH-VVAFTTSESKRNAARALGAddVVVSRNEDEMAAHVKS------FDFILNTVAAP 248
Cdd:cd08284   169 DTVAVIGCGPVGLCAVLSAQVLGAArVFAVDPVPERLERAAALGA--EPINFEDAEPVERVREategrgADVVLEAVGGA 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1623245061 249 HNLDAFTTLLKRDGTMTLVG---APATPHPSPEVF--NLIFR 285
Cdd:cd08284   247 AALDLAFDLVRPGGVISSVGvhtAEEFPFPGLDAYnkNLTLR 288
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 189-327 1.06e-11

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: 64.94  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 189 MGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNE--DEMAAHVKSFDFILNTVAAPHNLDAFtTLLKRDGTMTL 266
Cdd:cd08243   158 AALKLAKALGATVTATTRSPERAALLKELGADEVVIDDGAiaEQLRAAPGGFDKVLELVGTATLKDSL-RHLRPGGIVCM 236

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1623245061 267 VGAPATPhPSPEVFNLI-----FRRRSIAGSMIGGIPET--QEMLDFCAEHGIVADIELI-RGDEINEA 327
Cdd:cd08243   237 TGLLGGQ-WTLEDFNPMddipsGVNLTLTGSSSGDVPQTplQELFDFVAAGHLDIPPSKVfTFDEIVEA 304
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 27-293 2.76e-11

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: 63.87  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  27 PQDVQIAIAYCGVCHSDLHQARSEwAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMVDSCQQCEECAEGLENY 106
Cdd:cd08287    25 PTDAVIRVVATCVCGSDLWPYRGV-SPTRAPAPIGHEFVGVVEEVGSEVTSVKPGDFV-IAPFAISDGTCPFCRAGFTTS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 107 CDHmvltyngptQDAPGHTLGGYSQQIVvneryvlRITHPEAQLAAV------APLLCAGITTYSPL--RHWH------V 172
Cdd:cd08287   103 CVH---------GGFWGAFVDGGQGEYV-------RVPLADGTLVKVpgspsdDEDLLPSLLALSDVmgTGHHaavsagV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 173 GPGKKVGVVGIGGLGHMGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNEDEMAAhVKSF------DFILNTV 245
Cdd:cd08287   167 RPGSTVVVVGDGAVGLCAVLAAKRLGAeRIIAMSRHEDRQALAREFGATDIVAERGEEAVAR-VRELtggvgaDAVLECV 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1623245061 246 AAPHNLDAFTTLLKRDGTMTLVGApatPHPSPE--VFNLIFRRRSIAGSM 293
Cdd:cd08287   246 GTQESMEQAIAIARPGGRVGYVGV---PHGGVEldVRELFFRNVGLAGGP 292
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 26-235 4.73e-11

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 63.26  E-value: 4.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  26 GPQDVQIAIAYCGVCHSDLHQARSEWAGTLY---PCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEG 102
Cdd:PLN02702   40 GPHDVRVRMKAVGICGSDVHYLKTMRCADFVvkePMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGI-SCWRCNLCKEG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 103 LENYCDHMVLTYNGPTQdapghtlGGYSQQIVVNERYVLRIthPEA---QLAAVAPLLCAGITTyspLRHWHVGPGKKVG 179
Cdd:PLN02702  119 RYNLCPEMKFFATPPVH-------GSLANQVVHPADLCFKL--PENvslEEGAMCEPLSVGVHA---CRRANIGPETNVL 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1623245061 180 VVGIGGLGHMGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVV-VSRNEDEMAAHV 235
Cdd:PLN02702  187 VMGAGPIGLVTMLAARAFGApRIVIVDVDDERLSVAKQLGADEIVlVSTNIEDVESEV 244
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 25-273 1.05e-10

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: 61.87  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQAR-SEWAGT--LYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAE 101
Cdd:cd05281    23 PGPGEVLIKVLAASICGTDVHIYEwDEWAQSriKPPLIFGHEFAGEVVEVGEGVTRVKVGDYVSAETHI-VCGKCYQCRT 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 GLENYCDHMVLTyngptqdapG-HTLGGYSQQIVVNERyVLRITHPE--AQLAAV-APLLCAGITTY-SPLRHWHV---- 172
Cdd:cd05281   102 GNYHVCQNTKIL---------GvDTDGCFAEYVVVPEE-NLWKNDKDipPEIASIqEPLGNAVHTVLaGDVSGKSVlitg 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 173 -GPGKKvgvvgigglghMGIKLAHAMGAH-VVAFTTSESKRNAARALGADDVVVSRNEDemAAHVKS------FDFILNT 244
Cdd:cd05281   172 cGPIGL-----------MAIAVAKAAGASlVIASDPNPYRLELAKKMGADVVINPREED--VVEVKSvtdgtgVDVVLEM 238

                         250       260
                  ....*....|....*....|....*....
gi 1623245061 245 VAAPHNLDAFTTLLKRDGTMTLVGAPATP 273
Cdd:cd05281   239 SGNPKAIEQGLKALTPGGRVSILGLPPGP 267
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 9-230 1.96e-10

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: 61.48  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   9 YSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSD---LHQARSEwagTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVg 85
Cdd:cd08300     9 WEAGKPLSIEEVEVAPPKAGEVRIKILATGVCHTDaytLSGADPE---GLFPVILGHEGAGIVESVGEGVTSVKPGDHV- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  86 VGCMVDSCQQCEECAEGLENYCDHMVLTY-NGPTQDAPG----------HTLG--GYSQQIVVNERYVLRItHPEAQLAA 152
Cdd:cd08300    85 IPLYTPECGECKFCKSGKTNLCQKIRATQgKGLMPDGTSrfsckgkpiyHFMGtsTFSEYTVVAEISVAKI-NPEAPLDK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 153 VAPLLCaGITT-Y------------SPLRHWHVGpgkkvgvvgigglghmGIKLAHAMGA------HVVAFTTSESKRNA 213
Cdd:cd08300   164 VCLLGC-GVTTgYgavlntakvepgSTVAVFGLG----------------AVGLAVIQGAkaagasRIIGIDINPDKFEL 226

                         250
                  ....*....|....*..
gi 1623245061 214 ARALGADDVVVSRNEDE 230
Cdd:cd08300   227 AKKFGATDCVNPKDHDK 243
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 20-331 2.00e-10

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: 61.14  E-value: 2.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  20 ITRRDPGPQ---DVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQC 96
Cdd:cd05278    15 EEVPDPKIQgphDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVSVPCIT-FCGRC 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  97 EECAEGLENYCdhmvlTYNGPTQDAPGHTLGGYSQQIVVNE--RYVLRI--THPEAQLAAVAPLLCAGittysplrhWH- 171
Cdd:cd05278    94 RFCRRGYHAHC-----ENGLWGWKLGNRIDGGQAEYVRVPYadMNLAKIpdGLPDEDALMLSDILPTG---------FHg 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 -----VGPGKKVGVVGIGGLGHMGIKLAHAMGAH-VVAFTTSESKRNAARALGADDVVVSRNeDEMAAHVKS------FD 239
Cdd:cd05278   160 aelagIKPGSTVAVIGAGPVGLCAVAGARLLGAArIIAVDSNPERLDLAKEAGATDIINPKN-GDIVEQILEltggrgVD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 240 FILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVAD---I 316
Cdd:cd05278   239 CVIEAVGFEETFEQAVKVVRPGGTIANVGVYGKPDPLPLLGEWFGKNLTFKTGLVPVRARMPELLDLIEEGKIDPSkliT 318

                         330
                  ....*....|....*
gi 1623245061 317 ELIRGDEINEAWERM 331
Cdd:cd05278   319 HRFPLDDILKAYRLF 333
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 25-343 3.83e-10

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: 60.29  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHqARSEWAGTL--YPCVPGHAIVGRVTAVGNAVSRYAVGDlvgvgcmvdscqqceecaeg 102
Cdd:cd08253    25 PGPGEVLVRVHASGVNPVDTY-IRAGAYPGLppLPYVPGSDGAGVVEAVGEGVDGLKVGD-------------------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 103 lenycdhMVLTYNGptqdAPGHTLGGYSQQIVVNERYVLRIthPE----AQLAAVApllCAGITTYSPLRHW-------- 170
Cdd:cd08253    84 -------RVWLTNL----GWGRRQGTAAEYVVVPADQLVPL--PDgvsfEQGAALG---IPALTAYRALFHRagakaget 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 171 ---H-----VGpgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAA-----HVKS 237
Cdd:cd08253   148 vlvHggsgaVG--------------HAAVQLARWAGARVIATASSAEGAELVRQAGADAVFNYRAEDLADRilaatAGQG 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 238 FDFILNTVAAPhNLDAFTTLLKRDGTMTLVGAPATPhPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAEHGIVADIE 317
Cdd:cd08253   214 VDVIIEVLANV-NLAKDLDVLAPGGRIVVYGSGGLR-GTIPINPLMAKEASIRGVLLYTATPEERAAAAEAIAAGLADGA 291

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1623245061 318 LIRG-------DEINEAWERMVKGDVKYRFVID 343
Cdd:cd08253   292 LRPViareyplEEAAAAHEAVESGGAIGKVVLD 324
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
27-292 9.36e-10

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 59.08  E-value: 9.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  27 PQDVQIAIAYCGVCHSDLHQARSEWAgTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLvgVGCM-VDSCQQCEECAEGLEN 105
Cdd:PRK10309   25 QDDVLVKVASSGLCGSDIPRIFKNGA-HYYPITLGHEFSGYVEAVGSGVDDLHPGDA--VACVpLLPCFTCPECLRGFYS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 106 YCDHmvltYN--GPTQDapghtlGGYSQQIVVNERYVLRITH--PEAQLAAVAPLLCAgittyspLRHWHVGPGKKVGVV 181
Cdd:PRK10309  102 LCAK----YDfiGSRRD------GGNAEYIVVKRKNLFALPTdmPIEDGAFIEPITVG-------LHAFHLAQGCEGKNV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 182 GIGGLGHMG---IKLAHAMGAH-VVAFTTSESKRNAARALGADDVVVSR--NEDEMAAHVKSFDF---ILNTVAAPHNLD 252
Cdd:PRK10309  165 IIIGAGTIGllaIQCAVALGAKsVTAIDINSEKLALAKSLGAMQTFNSRemSAPQIQSVLRELRFdqlILETAGVPQTVE 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1623245061 253 AFTTLLKRDGTMTLVGapaTPHP----SPEVFNLIFRRR-SIAGS 292
Cdd:PRK10309  245 LAIEIAGPRAQLALVG---TLHHdlhlTSATFGKILRKElTVIGS 286
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 24-309 9.61e-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: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 59.23  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  24 DPGPQDVQIAIAYCGVCHSDLH------------QARSE-------WAGTL-YPCVPGHAIVGRVTAVGNAVSRYAVGDL 83
Cdd:cd08274    25 TPAPGEVLIRVGACGVNNTDINtregwystevdgATDSTgageagwWGGTLsFPRIQGADIVGRVVAVGEGVDTARIGER 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  84 VgvgcMVDSCQQceECAEGLENYCDHMvltyngptqdapGHTL-GGYSQQIVVNERYVLRITHP--EAQLAAVApllCAG 160
Cdd:cd08274   105 V----LVDPSIR--DPPEDDPADIDYI------------GSERdGGFAEYTVVPAENAYPVNSPlsDVELATFP---CSY 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 161 ITTYSPLRHWHVGPGKKVGVVGIGGLGHMG-IKLAHAMGAHVVAfTTSESKRNAARALGAdDVVVSRNE----DEMAAHV 235
Cdd:cd08274   164 STAENMLERAGVGAGETVLVTGASGGVGSAlVQLAKRRGAIVIA-VAGAAKEEAVRALGA-DTVILRDApllaDAKALGG 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1623245061 236 KSFDFILNTVAAPHnLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGIPETQEMLDFCAE 309
Cdd:cd08274   242 EPVDVVADVVGGPL-FPDLLRLLRPGGRYVTAGAIAGPVVELDLRTLYLKDLTLFGSTLGTREVFRRLVRYIEE 314
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 25-273 2.03e-09

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: 58.09  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQAR-----------SEWAGTLYPCVPGHAIVGRVTAVGNAVS-RYAVGDLVgVGCMVDS 92
Cdd:cd08262    21 PGPGQVLVKVLACGICGSDLHATAhpeamvddaggPSLMDLGADIVLGHEFCGEVVDYGPGTErKLKVGTRV-TSLPLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  93 CQQCEECAEGLENycdhmvltyngptqDAPghtlGGYSQQIVVNERYVLRI--THPEAQLAAVAPLLC-------AGITT 163
Cdd:cd08262   100 CGQGASCGIGLSP--------------EAP----GGYAEYMLLSEALLLRVpdGLSMEDAALTEPLAVglhavrrARLTP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 164 YSPLRHWHVGPgkkvgvvgigglghmgIKLA-----HAMGAH-VVAFTTSESKRNAARALGADDVVVSRNEDEMAAHVKS 237
Cdd:cd08262   162 GEVALVIGCGP----------------IGLAviaalKARGVGpIVASDFSPERRALALAMGADIVVDPAADSPFAAWAAE 225

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1623245061 238 FDF--------ILNTVAAPHNLDAFTTLLKRDGTMTLVGAPATP 273
Cdd:cd08262   226 LARaggpkpavIFECVGAPGLIQQIIEGAPPGGRIVVVGVCMES 269
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 25-229 2.46e-09

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 57.91  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLH-QARSEWA-GTL-YPCVPGHAIVGRVTAVGNAVSRYAVGDLV-GVGCMVdsCQQCEECA 100
Cdd:PRK05396   23 PGPNDVLIKVKKTAICGTDVHiYNWDEWAqKTIpVPMVVGHEFVGEVVEVGSEVTGFKVGDRVsGEGHIV--CGHCRNCR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 101 EGLENYCDHMV-LTYNGPtqdapghtlGGYSQQIVVNERYVLRitHPEA---QLAAV-APLLCAGITTYS-PLRHWHV-- 172
Cdd:PRK05396  101 AGRRHLCRNTKgVGVNRP---------GAFAEYLVIPAFNVWK--IPDDipdDLAAIfDPFGNAVHTALSfDLVGEDVli 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1623245061 173 ---GPGKKvgvvgigglghMGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNED 229
Cdd:PRK05396  170 tgaGPIGI-----------MAAAVAKHVGArHVVITDVNEYRLELARKMGATRAVNVAKED 219
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 20-337 3.66e-09

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: 57.25  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  20 ITRRDPGPQDVQIAIAYCGVCHSDLHQARsewaGTL-YPCVPGHAIVGRVTAVGNAvsryavgDLVG---VGCMVDSCQQ 95
Cdd:cd08242    17 LPKPEPPPGEALVRVLLAGICNTDLEIYK----GYYpFPGVPGHEFVGIVEEGPEA-------ELVGkrvVGEINIACGR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  96 CEECAEGLENYCDHM-VLTYNGptQDapghtlGGYSQQIVVNERYVLRITHPEAQLAAVA--PLLCAGittySPLRHWHV 172
Cdd:cd08242    86 CEYCRRGLYTHCPNRtVLGIVD--RD------GAFAEYLTLPLENLHVVPDLVPDEQAVFaePLAAAL----EILEQVPI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 173 GPGKKVGVVGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAAhvksFDFILNTVAAPHNLD 252
Cdd:cd08242   154 TPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLGVETVLPDEAESEGGG----FDVVVEATGSPSGLE 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 253 AFTTLLKRDGTMTL---VGAPATPHPSPEVFNLIfrrrSIAGSMIGGIPETQEMLdfcaEHGIVADIELIRG----DEIN 325
Cdd:cd08242   230 LALRLVRPRGTVVLkstYAGPASFDLTKAVVNEI----TLVGSRCGPFAPALRLL----RKGLVDVDPLITAvyplEEAL 301

                         330
                  ....*....|...
gi 1623245061 326 EAWER-MVKGDVK 337
Cdd:cd08242   302 EAFERaAEPGALK 314
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 9-334 5.90e-09

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: 56.92  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   9 YSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGC 88
Cdd:cd08301     9 WEAGKPLVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHV-LPV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  89 MVDSCQQCEECAEGLENYCDHM-------VLTYNGPTQ-----DAPGHTLGG--YSQQIVVNERYVLRIThPEAQLAAVA 154
Cdd:cd08301    88 FTGECKECRHCKSEKSNMCDLLrintdrgVMINDGKSRfsingKPIYHFVGTstFSEYTVVHVGCVAKIN-PEAPLDKVC 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 155 PLLCaGITTySPLRHWHVGPGKKVGVVGIGGLGHMGikLAHAMGAH------VVAFTTSESKRNAARALGADDVVVSRNE 228
Cdd:cd08301   167 LLSC-GVST-GLGAAWNVAKVKKGSTVAIFGLGAVG--LAVAEGARirgasrIIGVDLNPSKFEQAKKFGVTEFVNPKDH 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 229 DEMAAHV----------KSFDFILNTVAAphnLDAFTTLLKRDGTMTLVGAPATPHPSPEVFNLIFRRRSIAGSMIGGI- 297
Cdd:cd08301   243 DKPVQEViaemtgggvdYSFECTGNIDAM---ISAFECVHDGWGVTVLLGVPHKDAVFSTHPMNLLNGRTLKGTLFGGYk 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1623245061 298 PETQemLDFCAEHGIVADIEL-------IRGDEINEAWERMVKG 334
Cdd:cd08301   320 PKTD--LPNLVEKYMKKELELekfitheLPFSEINKAFDLLLKG 361
PLN02827 PLN02827
Alcohol dehydrogenase-like
 4-334 7.58e-09

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 56.45  E-value: 7.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   4 NAIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEwagTLYPCVPGHAIVGRVTAVGNAVSRYAVGDL 83
Cdd:PLN02827   14 RAAVAWGAGEALVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWESQ---ALFPRIFGHEASGIVESIGEGVTEFEKGDH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  84 VgVGCMVDSCQQCEECAEGLENYCDHMVLTYNG----------PTQDAPGH---TLGGYSQQIVVNERYVLRIThPEAQL 150
Cdd:PLN02827   91 V-LTVFTGECGSCRHCISGKSNMCQVLGLERKGvmhsdqktrfSIKGKPVYhycAVSSFSEYTVVHSGCAVKVD-PLAPL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 151 AAVAPLLC---AGITTYsplrhWHVGPGKKVGVVGIGGLGHMGIKLAHAM----GAHVVAFTTSESKRNAARALGADDVV 223
Cdd:PLN02827  169 HKICLLSCgvaAGLGAA-----WNVADVSKGSSVVIFGLGTVGLSVAQGAklrgASQIIGVDINPEKAEKAKTFGVTDFI 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 224 VSRNEDEMAAHV----------KSFDFILNTVAAphnldafTTLLKR--DG---TMTLvgapATPHPSPEV---FNLIFR 285
Cdd:PLN02827  244 NPNDLSEPIQQVikrmtgggadYSFECVGDTGIA-------TTALQScsDGwglTVTL----GVPKAKPEVsahYGLFLS 312

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1623245061 286 RRSIAGSMIGGI-PETQ--EMLDFCAEHGIVADiELIRG----DEINEAWERMVKG 334
Cdd:PLN02827  313 GRTLKGSLFGGWkPKSDlpSLVDKYMNKEIMID-EFITHnlsfDEINKAFELMREG 367
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 21-272 9.73e-09

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: 56.12  E-value: 9.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  21 TRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGT-LYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGvgCMVDScqqceec 99
Cdd:cd08273    21 DLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQpPLPFTPGYDLVGRVDALGSGVTGFEVGDRVA--ALTRV------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 100 aeglenycdhmvltyngptqdapghtlGGYSQQIVVNERYVLRIThPEAQLAAVAPLLCAGITTYSPLRHwhvgpgKKVG 179
Cdd:cd08273    92 ---------------------------GGNAEYINLDAKYLVPVP-EGVDAAEAVCLVLNYVTAYQMLHR------AAKV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 180 VVGIGGLGHMG--------IKLAHAMGAHVVAfTTSESKRNAARALGAdDVVVSRNEDEMAAHV--KSFDFILNTVAAPH 249
Cdd:cd08273   138 LTGQRVLIHGAsggvgqalLELALLAGAEVYG-TASERNHAALRELGA-TPIDYRTKDWLPAMLtpGGVDVVFDGVGGES 215

                         250       260
                  ....*....|....*....|...
gi 1623245061 250 nLDAFTTLLKRDGTMTLVGAPAT 272
Cdd:cd08273   216 -YEESYAALAPGGTLVCYGGNSS 237
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 27-267 1.63e-08

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: 55.31  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  27 PQDVQIAIAYcG--VCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCmvdscqqceecaegle 104
Cdd:cd08248    43 PIDVLMRSGY-GrtLLNKKRKPQSCKYSGIEFPLTLGRDCSGVVVDIGSGVKSFEIGDEVWGAV---------------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 nycdhmvltyngptqdaPGHTLGGYSQQIVVNERYVLR----ITHPEAqlaavAPLLCAGITTYSPLrhWHVGPGKKVGV 180
Cdd:cd08248   106 -----------------PPWSQGTHAEYVVVPENEVSKkpknLSHEEA-----ASLPYAGLTAWSAL--VNVGGLNPKNA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 181 VGIGGLGHMG--------IKLAHAMGAHVVAfTTSESKRNAARALGADDVVVSRNED---EMAAHVKsFDFILNTVAAPh 249
Cdd:cd08248   162 AGKRVLILGGsggvgtfaIQLLKAWGAHVTT-TCSTDAIPLVKSLGADDVIDYNNEDfeeELTERGK-FDVILDTVGGD- 238

                         250
                  ....*....|....*....
gi 1623245061 250 NLDAFTTLLKRDGT-MTLV 267
Cdd:cd08248   239 TEKWALKLLKKGGTyVTLV 257
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 27-129 1.73e-08

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: 55.29  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  27 PQDVQIAIAYCGVCHSDLHQARSEWaGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVdSCQQCEECAEGLENY 106
Cdd:cd08282    25 PTDAIVRITTTAICGSDLHMYRGRT-GAEPGLVLGHEAMGEVEEVGSAVESLKVGDRVVVPFNV-ACGRCRNCKRGLTGV 102

                          90       100
                  ....*....|....*....|....*
gi 1623245061 107 CdhmvLTYN-GPTQDAPGHT-LGGY 129
Cdd:cd08282   103 C----LTVNpGRAGGAYGYVdMGPY 123
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 27-107 1.90e-08

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: 55.33  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  27 PQDVQIAIAYCGVCHSDLHQarseWAGTLYPCVP----GHAIVGRVTAVGNAVSRYAVGDLVGVGCMvDSCQQCEECAEG 102
Cdd:cd08286    25 PTDAIVKMLKTTICGTDLHI----LKGDVPTVTPgrilGHEGVGVVEEVGSAVTNFKVGDRVLISCI-SSCGTCGYCRKG 99


                  ....*
gi 1623245061 103 LENYC 107
Cdd:cd08286   100 LYSHC 104
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 28-292 2.43e-08

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 54.69  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  28 QDVQIAIAYCGVCHSDLHQARSEWAGTL---YPCVPGHAIVGRVTAVGNavSRYAVGDLVGVGcMVDSCQQCEECAEGLE 104
Cdd:PRK09880   28 NGTLVQITRGGICGSDLHYYQEGKVGNFvikAPMVLGHEVIGKIVHSDS--SGLKEGQTVAIN-PSKPCGHCKYCLSHNE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 NYCDHMvlTYNGPTQDAPgHTLGGYSQQIVVNERYVlrITHPE---AQLAAVA-PLLC-------AGITTYSPLRHWHVG 173
Cdd:PRK09880  105 NQCTTM--RFFGSAMYFP-HVDGGFTRYKVVDTAQC--IPYPEkadEKVMAFAePLAVaihaahqAGDLQGKRVFVSGVG 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 174 PGKKvgvvgigglghMGIKLAHAMGA-HVVAFTTSESKRNAARALGADDVVVSRNED--EMAAHVKSFDFILNTVAAPHN 250
Cdd:PRK09880  180 PIGC-----------LIVAAVKTLGAaEIVCADVSPRSLSLAREMGADKLVNPQNDDldHYKAEKGYFDVSFEVSGHPSS 248

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1623245061 251 LDAFTTLLKRDGTMTLVGAPATPhPSPEVFNLIFRRRSIAGS 292
Cdd:PRK09880  249 INTCLEVTRAKGVMVQVGMGGAP-PEFPMMTLIVKEISLKGS 289
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 25-102 3.44e-08

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: 54.34  E-value: 3.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDL---HQARSEWAGTLY------PCVPGHAIVGRVTAVGNAVSR--YAVGDLVgVGCMVDSC 93
Cdd:cd08256    22 PGPGEILVKVEACGICAGDIkcyHGAPSFWGDENQppyvkpPMIPGHEFVGRVVELGEGAEErgVKVGDRV-ISEQIVPC 100


                  ....*....
gi 1623245061  94 QQCEECAEG 102
Cdd:cd08256   101 WNCRFCNRG 109
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 27-129 4.76e-08

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: 54.08  E-value: 4.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  27 PQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMVDSCQQCEECAEGLENY 106
Cdd:cd08283    25 PTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGDRV-VVPFTIACGECFYCKRGLYSQ 103

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1623245061 107 CD------HMVLTYNGPTQDAPG--HTLGGY 129
Cdd:cd08283   104 CDntnpsaEMAKLYGHAGAGIFGysHLTGGY 134
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 11-296 9.58e-08

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: 53.09  E-value: 9.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  11 ASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHqARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMV 90
Cdd:cd08299    16 PKKPFSIEEIEVAPPKAHEVRIKIVATGICRSDDH-VVSGKLVTPFPVILGHEAAGIVESVGEGVTTVKPGDKV-IPLFV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  91 DSCQQCEECAEGLENYCDHMVLT-YNGPTQDA---------PGHTLGG---YSQQIVVNERYVLRItHPEAQLAAVAPLL 157
Cdd:cd08299    94 PQCGKCRACLNPESNLCLKNDLGkPQGLMQDGtsrftckgkPIHHFLGtstFSEYTVVDEIAVAKI-DAAAPLEKVCLIG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 158 CAGITTY-SPLRHWHVGPGKKVGV---VGIGGLGHMGIKLAHAmgAHVVAFTTSESKRNAARALGADDVVVSRNED---- 229
Cdd:cd08299   173 CGFSTGYgAAVNTAKVTPGSTCAVfglGGVGLSAIMGCKAAGA--SRIIAVDINKDKFAKAKELGATECINPQDYKkpiq 250

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1623245061 230 ----EM-AAHVK-SFDFI--LNTVAAphnldAFTTLLKRDGTMTLVGAPatphPSPEVFN----LIFRRRSIAGSMIGG 296
Cdd:cd08299   251 evltEMtDGGVDfSFEVIgrLDTMKA-----ALASCHEGYGVSVIVGVP----PSSQNLSinpmLLLTGRTWKGAVFGG 320
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 25-223 1.33e-07

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


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 52.37  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLhQARSEWAGTLY----PCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqceeca 100
Cdd:cd08244    25 PGPGQVRIAVAAAGVHFVDT-QLRSGWGPGPFppelPYVPGGEVAGVVDAVGPGVDPAWLGRRV---------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 101 eglenycdhmvltyNGPTQDAPGhtlgGYSQQIVVNERYVLRITHPEAQLAAVApLLCAGITTYSPLRHWHVGPGKKVGV 180
Cdd:cd08244    88 --------------VAHTGRAGG----GYAELAVADVDSLHPVPDGLDLEAAVA-VVHDGRTALGLLDLATLTPGDVVLV 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1623245061 181 VGIGGLghMG---IKLAHAMGAHVVAFTTSESKRNAARALGADDVV 223
Cdd:cd08244   149 TAAAGG--LGsllVQLAKAAGATVVGAAGGPAKTALVRALGADVAV 192
PLN02740 PLN02740
Alcohol dehydrogenase-like
 4-107 1.33e-07

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 52.88  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   4 NAIGTYSASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLhqarSEWAGT-----LYPCVPGHAIVGRVTAVGNAVSRY 78
Cdd:PLN02740   12 KAAVAWGPGEPLVMEEIRVDPPQKMEVRIKILYTSICHTDL----SAWKGEneaqrAYPRILGHEAAGIVESVGEGVEDL 87

                          90       100
                  ....*....|....*....|....*....
gi 1623245061  79 AVGDLVgVGCMVDSCQQCEECAEGLENYC 107
Cdd:PLN02740   88 KAGDHV-IPIFNGECGDCRYCKRDKTNLC 115
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 25-229 1.64e-07

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 52.42  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQA----------RSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCMVDScQ 94
Cdd:cd08246    40 LGPGEVLVAVMAAGVNYNNVWAAlgepvstfaaRQRRGRDEPYHIGGSDASGIVWAVGEGVKNWKVGDEVVVHCSVWD-G 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  95 QCEECAEGlenycDHMVltynGPTQDAPGH--TLGGYSQQIVVNERYVL----RITHPEAqlaavAPLLCAGITTYSPLR 168
Cdd:cd08246   119 NDPERAGG-----DPMF----DPSQRIWGYetNYGSFAQFALVQATQLMpkpkHLSWEEA-----AAYMLVGATAYRMLF 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1623245061 169 HWH---VGPGKKVGV-VGIGGLGHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNED 229
Cdd:cd08246   185 GWNpntVKPGDNVLIwGASGGLGSMAIQLARAAGANPVAVVSSEEKAEYCRALGAEGVINRRDFD 249
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 22-110 3.18e-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: 51.47  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  22 RRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCmVDSCQQCEECAE 101
Cdd:cd08285    19 IPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGDRVIVPA-ITPDWRSVAAQR 97


                  ....*....
gi 1623245061 102 GLENYCDHM 110
Cdd:cd08285    98 GYPSQSGGM 106
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 10-283 1.19e-06

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: 49.58  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  10 SASQPLESMAITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAG-TLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgc 88
Cdd:cd05282     9 PLPLVLELVSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSrPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRV---- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  89 mvdscqqceecaeglenycdhmvltyngptqdAPGHTLGGYSQQIVVNERYVLRIthPEA---QLAA---VAPLLCAGI- 161
Cdd:cd05282    85 --------------------------------LPLGGEGTWQEYVVAPADDLIPV--PDSisdEQAAmlyINPLTAWLMl 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 162 TTYSPLRH--W--------HVGpgkkvgvvgigglgHMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDeM 231
Cdd:cd05282   131 TEYLKLPPgdWviqnaansAVG--------------RMLIQLAKLLGFKTINVVRRDEQVEELKALGADEVIDSSPED-L 195

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1623245061 232 AAHVKSfdfILNTVAAPHNLDA-----FTTL---LKRDGTM----TLVGAPATPHPSPEVFNLI 283
Cdd:cd05282   196 AQRVKE---ATGGAGARLALDAvggesATRLarsLRPGGTLvnygLLSGEPVPFPRSVFIFKDI 256
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 57-298 1.39e-06

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


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 49.19  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  57 PCVPGHAIVGRVTAVGNAVSRYAVGDLVGVgcmvdscqqceecaeglenycdhmvltyngptqdapghtLGGYSQQIVVN 136
Cdd:cd08255    21 PLPPGYSSVGRVVEVGSGVTGFKPGDRVFC---------------------------------------FGPHAERVVVP 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 137 ERYVLRI-THPEAQLAAVAPLLCagiTTYSPLRHWHVGPGKKVGVVGIGGLGHMGIKLAHAMGA-HVVAFTTSESKRNAA 214
Cdd:cd08255    62 ANLLVPLpDGLPPERAALTALAA---TALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGArEVVGVDPDAARRELA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 215 RALGADDVVVSRNEDEMAAHVksFDFILNTVAAPHNLDAFTTLLKRDGTMTLVGAPAT-PHPSPEVFNliFRRRSIAGSM 293
Cdd:cd08255   139 EALGPADPVAADTADEIGGRG--ADVVIEASGSPSALETALRLLRDRGRVVLVGWYGLkPLLLGEEFH--FKRLPIRSSQ 214


                  ....*
gi 1623245061 294 IGGIP 298
Cdd:cd08255   215 VYGIG 219
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 8-286 4.77e-06

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 47.66  E-value: 4.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   8 TYSASQPLESMAITRRD---PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLV 84
Cdd:cd08271     5 VLPKPGAALQLTLEEIEipgPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKVGDRV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  85 GVgcmvdscqqceecaeglenycdHMVLTYNgptqdapghtlGGYSQQIVVNERYVLRItHPEAQLAAVAPLLCAGITTY 164
Cdd:cd08271    85 AY----------------------HASLARG-----------GSFAEYTVVDARAVLPL-PDSLSFEEAAALPCAGLTAY 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 165 SPLRH----------------WHVGpgkkvgvvgigglgHMGIKLAHAMGAHVvaFTTSeSKRN--AARALGADDVVVSR 226
Cdd:cd08271   131 QALFKklrieagrtilitggaGGVG--------------SFAVQLAKRAGLRV--ITTC-SKRNfeYVKSLGADHVIDYN 193

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1623245061 227 NEDEMAAHVKS-----FDFILNTVAAPHNlDAFTTLLKRDGtmTLVGAPATPHPSPEVFnliFRR 286
Cdd:cd08271   194 DEDVCERIKEItggrgVDAVLDTVGGETA-AALAPTLAFNG--HLVCIQGRPDASPDPP---FTR 252
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 25-249 7.54e-06

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: 47.04  E-value: 7.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAG-TLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVGVGCmvdscqqceecaegl 103
Cdd:cd08251     5 PGPGEVRIQVRAFSLNFGDLLCVRGLYPTmPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGT--------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 104 enycdhmvltyngptqdapGHTLGGYSQQIVVNERYVLR----ITHPEAqlaavAPLLCAGITTYSPLRHWHVGPGKKVG 179
Cdd:cd08251    70 -------------------GESMGGHATLVTVPEDQVVRkpasLSFEEA-----CALPVVFLTVIDAFARAGLAKGEHIL 125

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1623245061 180 VVGIGGLGH-MGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNED------EMAAHvKSFDFILNTVAAPH 249
Cdd:cd08251   126 IQTATGGTGlMAVQLARLKGAEIYATASSDDKLEYLKQLGVPHVINYVEEDfeeeimRLTGG-RGVDVVINTLSGEA 201
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 25-302 1.10e-05

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: 46.81  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAI--AYCGVCHSDLHQARSEWAGTlYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgVGCMvdscqqceecaeg 102
Cdd:cd08249    22 PKPGPDEVLVkvKAVALNPVDWKHQDYGFIPS-YPAILGCDFAGTVVEVGSGVTRFKVGDRV-AGFV------------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 103 lenycdHMVLTYNGPTqdapghtlGGYSQQIVVNERYVLRIthPEA---QLAAVAPLlcAGITTYSPLRHWHVGPGKKVG 179
Cdd:cd08249    87 ------HGGNPNDPRN--------GAFQEYVVADADLTAKI--PDNisfEEAATLPV--GLVTAALALFQKLGLPLPPPK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 180 VVGIGGLGH------------MGIKLAHAMGAHVVafTTSeSKRNAA--RALGADDVV----VSRNEDEMAAHVKSFDFI 241
Cdd:cd08249   149 PSPASKGKPvliwggsssvgtLAIQLAKLAGYKVI--TTA-SPKNFDlvKSLGADAVFdyhdPDVVEDIRAATGGKLRYA 225

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1623245061 242 LNTVAAPHNLDAFTTLLKRDGT---MTLVGAPATPHPSPEVfnliFRRRSIAGSMIGGIPETQE 302
Cdd:cd08249   226 LDCISTPESAQLCAEALGRSGGgklVSLLPVPEETEPRKGV----KVKFVLGYTVFGEIPEDRE 285
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 25-273 1.64e-05

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 45.98  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqceecaegle 104
Cdd:cd08252    28 PGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGSEVTLFKVGDEV-------------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 105 nYcdhmvltYNG-PTQDapghtlGGYSQQIVVNERYVLR----ITHPEAqlAAVaPLlcAGITTYSPL-RHWHVGPGKKV 178
Cdd:cd08252    88 -Y-------YAGdITRP------GSNAEYQLVDERIVGHkpksLSFAEA--AAL-PL--TSLTAWEALfDRLGISEDAEN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 179 GVVGIGGLG------HMGIKLA-HAMGAHVVAfTTS--ESkRNAARALGADDVVVSRN--EDEMAA-HVKSFDFILNTVA 246
Cdd:cd08252   149 EGKTLLIIGgaggvgSIAIQLAkQLTGLTVIA-TASrpES-IAWVKELGADHVINHHQdlAEQLEAlGIEPVDYIFCLTD 226

                         250       260
                  ....*....|....*....|....*..
gi 1623245061 247 APHNLDAFTTLLKRDGTMTLVGAPATP 273
Cdd:cd08252   227 TDQHWDAMAELIAPQGHICLIVDPQEP 253
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 29-264 6.82e-05

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: 44.10  E-value: 6.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  29 DVQIAIAYCGVCHSDLHQARSEWAGTlyPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqceecaeglenycd 108
Cdd:cd05195     2 EVEVEVKAAGLNFRDVLVALGLLPGD--ETPLGLECSGIVTRVGSGVTGLKVGDRV------------------------ 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 109 hMVLTyngptqdapghtLGGYSQQIVVNERYVLRI----THPEAqlaavAPLLCAGITTYSPLRH-WHVGPgkkvgvvgi 183
Cdd:cd05195    56 -MGLA------------PGAFATHVRVDARLVVKIpdslSFEEA-----ATLPVAYLTAYYALVDlARLQK--------- 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 184 gglghmG----------------IKLAHAMGAHVvaFTT--SESKRNAARALG--ADDVVVSRN---EDEM--AAHVKSF 238
Cdd:cd05195   109 ------GesvlihaaaggvgqaaIQLAQHLGAEV--FATvgSEEKREFLRELGgpVDHIFSSRDlsfADGIlrATGGRGV 180

                         250       260
                  ....*....|....*....|....*.
gi 1623245061 239 DFILNTVAAPHnLDAFTTLLKRDGTM 264
Cdd:cd05195   181 DVVLNSLSGEL-LRASWRCLAPFGRF 205
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 32-264 1.07e-04

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 43.53  E-value: 1.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061   32 IAIAYCGVCHSDLHQARsewaGTL-YPCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqceecaeglenycdhM 110
Cdd:smart00829   1 IEVRAAGLNFRDVLIAL----GLYpGEAVLGGECAGVVTRVGPGVTGLAVGDRV-------------------------M 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  111 VLTyngptqdapghtLGGYSQQIVVNERYVLRI----THPEAqlaavAPLLCAGITTYSPLRHW-----------H---- 171
Cdd:smart00829  52 GLA------------PGAFATRVVTDARLVVPIpdgwSFEEA-----ATVPVVFLTAYYALVDLarlrpgesvliHaaag 114

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  172 -VGpgkkvgvvgigglgHMGIKLAHAMGAHVvaFTT--SESKRNAARALG--ADDVVVSRNEDeMAAHVKS------FDF 240
Cdd:smart00829 115 gVG--------------QAAIQLARHLGAEV--FATagSPEKRDFLRALGipDDHIFSSRDLS-FADEILRatggrgVDV 177

                          250       260
                   ....*....|....*....|....
gi 1623245061  241 ILNTVAAPHnLDAFTTLLKRDGTM 264
Cdd:smart00829 178 VLNSLSGEF-LDASLRCLAPGGRF 200
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 25-229 1.17e-04

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 43.40  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQDVQIAIAYCGVCHSDLHQARSEWAGTLYPcvP---GHAIVGRVTAVGNAVSRYAVGDLVGvgcmvdscqqceecae 101
Cdd:cd08250    28 PGPGEVLVKNRFVGINASDINFTAGRYDPGVKP--PfdcGFEGVGEVVAVGEGVTDFKVGDAVA---------------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 102 glenycdhmvltyngpTQdapghTLGGYSQQIVVNERYVLRIthPEAQlAAVAPLLCAGITTYSPLRHwhVGPGKKVGVV 181
Cdd:cd08250    90 ----------------TM-----SFGAFAEYQVVPARHAVPV--PELK-PEVLPLLVSGLTASIALEE--VGEMKSGETV 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1623245061 182 GIGGLG----HMGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNED 229
Cdd:cd08250   144 LVTAAAggtgQFAVQLAKLAGCHVIGTCSSDEKAEFLKSLGCDRPINYKTED 195
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 25-269 2.07e-04

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 42.57  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  25 PGPQD--VQIAIAYCGVCHSDLHqARSewaGtLY------PCVPGHAIVGRVTAVGNAVSRYAVGDLVgvgcmvdscqqc 96
Cdd:cd08275    22 PEPSSgeVRVRVEACGLNFADLM-ARQ---G-LYdsapkpPFVPGFECAGTVEAVGEGVKDFKVGDRV------------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  97 eecaeglenycdhMVLTYNgptqdapghtlGGYSQQIVVNERYVLRI----THPEAqlaavAPLLCAGITTYSPLRHW-H 171
Cdd:cd08275    85 -------------MGLTRF-----------GGYAEVVNVPADQVFPLpdgmSFEEA-----AAFPVNYLTAYYALFELgN 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 172 VGPgkkvgvvGIGGLGHM-----GIKLAHAMGA--HVVAF-TTSESKRNAARALGADDVVVSRNED------EMAAhvKS 237
Cdd:cd08275   136 LRP-------GQSVLVHSaaggvGLAAGQLCKTvpNVTVVgTASASKHEALKENGVTHVIDYRTQDyveevkKISP--EG 206

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1623245061 238 FDFILNTVAAPHNLDAFtTLLKRDGTMTLVGA 269
Cdd:cd08275   207 VDIVLDALGGEDTRKSY-DLLKPMGRLVVYGA 237
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 189-343 2.71e-04

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


Pssm-ID: 176183 [Multi-domain]  Cd Length: 325  Bit Score: 42.14  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 189 MGIKLAHAMGAHVVAFTTSESKRNAARALGADDvVVSRNE----DEMAAHVKSFDFILNTVAAPHnLDAFTTLLKRDGTM 264
Cdd:cd05280   162 IAVAILAKLGYTVVALTGKEEQADYLKSLGASE-VLDREDlldeSKKPLLKARWAGAIDTVGGDV-LANLLKQTKYGGVV 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 265 TLVGAPATPHPSPEVFNLIFRRRSIAG--SMIGGIPETQE-------MLDFCAEHGIVADIELirgDEINEAWERMVKGD 335
Cdd:cd05280   240 ASCGNAAGPELTTTVLPFILRGVSLLGidSVNCPMELRKQvwqklatEWKPDLLEIVVREISL---EELPEAIDRLLAGK 316


                  ....*...
gi 1623245061 336 VKYRFVID 343
Cdd:cd05280   317 HRGRTVVK 324
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 116-280 4.24e-04

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 41.59  E-value: 4.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 116 GPTQDAPGHTL---GGYSQQIVVNERYVLRIThPEAQLAAVAPLLCAGITTYSPLRHwhVGPGKKVGVVGIGGLGHMG-- 190
Cdd:cd08270    72 GPAVGARVVGLgamGAWAELVAVPTGWLAVLP-DGVSFAQAATLPVAGVTALRALRR--GGPLLGRRVLVTGASGGVGrf 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 191 -IKLAHAMGAHVVAFTTSESKRNAARALGADDVVVSRNEDEMAahvkSFDFILNTVAAPhNLDAFTTLLKRDGTMTLVGA 269
Cdd:cd08270   149 aVQLAALAGAHVVAVVGSPARAEGLRELGAAEVVVGGSELSGA----PVDLVVDSVGGP-QLARALELLAPGGTVVSVGS 223

                         170
                  ....*....|....*
gi 1623245061 270 ----PATPHPSPEVF 280
Cdd:cd08270   224 ssgePAVFNPAAFVG 238
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 191-248 1.21e-03

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 38.64  E-value: 1.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1623245061  191 IKLAHAMGAHVVAFTTS-ESKRNAARALGADDVVVSRNEDEMAAHVKSFDFILNTVAAP 248
Cdd:smart01002  36 AATAKGLGAEVTVLDVRpARLRQLESLLGARFTTLYSQAELLEEAVKEADLVIGAVLIP 94
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 189-343 3.22e-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: 39.08  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 189 MGIKLAHAMGAHVVAFTTSESKRNAARALGADDVVvsrNEDEMAAHVKS-----FDFILNTVAAPHnLDAFTTLLKRDGT 263
Cdd:TIGR02823 161 LAVAILSKLGYEVVASTGKAEEEDYLKELGASEVI---DREDLSPPGKPlekerWAGAVDTVGGHT-LANVLAQLKYGGA 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 264 MTLVGAPATPHPSPEVFNLIFRRRSIAG--SMIGGIPETQE-------MLDFCAEHGIVADIELirgDEINEAWERMVKG 334
Cdd:TIGR02823 237 VAACGLAGGPDLPTTVLPFILRGVSLLGidSVYCPMALREAawqrlatDLKPRNLESITREITL---EELPEALEQILAG 313


                  ....*....
gi 1623245061 335 DVKYRFVID 343
Cdd:TIGR02823 314 QHRGRTVVD 322
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 20-271 4.98e-03

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: 38.36  E-value: 4.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  20 ITRRDPGPQDVQIAIAYCGVCHSDLHQARSEWAGtlYP-----CVPGHAIVGRVTAVGNAvSRYAVGDLVgVGCMVDSCQ 94
Cdd:cd08230    18 IPEPEPTPGEVLVRTLEVGVCGTDREIVAGEYGT--APpgedfLVLGHEALGVVEEVGDG-SGLSPGDLV-VPTVRRPPG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061  95 QCEECAEGLENYCDhmvltyNGPTQDAPGHTLGGY-SQQIVVNERYVLRITHPEAQLAAVA-PLLCA------GITTYSP 166
Cdd:cd08230    94 KCLNCRIGRPDFCE------TGEYTERGIKGLHGFmREYFVDDPEYLVKVPPSLADVGVLLePLSVVekaieqAEAVQKR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1623245061 167 LRHWH--------VGPgkkvgvvgigglghmgIKLAHAMGAHVVAFTT--------SESKRNAARALGADDVVVSRNEDE 230
Cdd:cd08230   168 LPTWNprralvlgAGP----------------IGLLAALLLRLRGFEVyvlnrrdpPDPKADIVEELGATYVNSSKTPVA 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1623245061 231 MAAHVKSFDFILNTVAAPHNLDAFTTLLKRDGTMTLVGAPA 271
Cdd:cd08230   232 EVKLVGEFDLIIEATGVPPLAFEALPALAPNGVVILFGVPG 272
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH