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Conserved domains on  [gi|1229749854|pdb|5VKT|B]
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Chain B, Cinnamyl alcohol dehydrogenases (SbCAD4)

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 11-351 6.14e-162

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: 456.57  E-value: 6.14e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       11 HGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDT 90
Cdd:cd05283   1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       91 VGVGYFVDSCRTCESCSTGHENYCPDLVLTSNGVDhhHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTV 170
Cdd:cd05283  81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKY--PDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      171 YSPMAQYALnEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDGI 250
Cdd:cd05283 159 YSPLKRNGV-GPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDAL-KLGADEFIATKDPEAMKKAAGSLDLI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      251 IDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMD 330
Cdd:cd05283 237 IDTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMD 316

                       330       340
                ....*....|....*....|.
5VKT_B      331 YVNTAIERLEKNDVRYRFVID 351
Cdd:cd05283 317 GINEALERLEKGDVRYRFVLD 337
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 11-351 6.14e-162

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: 456.57  E-value: 6.14e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       11 HGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDT 90
Cdd:cd05283   1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       91 VGVGYFVDSCRTCESCSTGHENYCPDLVLTSNGVDhhHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTV 170
Cdd:cd05283  81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKY--PDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      171 YSPMAQYALnEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDGI 250
Cdd:cd05283 159 YSPLKRNGV-GPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDAL-KLGADEFIATKDPEAMKKAAGSLDLI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      251 IDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMD 330
Cdd:cd05283 237 IDTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMD 316

                       330       340
                ....*....|....*....|.
5VKT_B      331 YVNTAIERLEKNDVRYRFVID 351
Cdd:cd05283 317 GINEALERLEKGDVRYRFVLD 337
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 10-355 4.88e-161

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 455.11  E-value: 4.88e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        10 AHGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGD 89
Cdd:PLN02586  13 AFGWAARDPSGVLSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        90 TVGVGYFVDSCRTCESCSTGHENYCPDLVLTSNGvdHHHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVT 169
Cdd:PLN02586  93 RVGVGVIVGSCKSCESCDQDLENYCPKMIFTYNS--IGHDGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGIT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       170 VYSPMAQYALNEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALGRLGADAFLVSHDAAQMKAAAATLDG 249
Cdd:PLN02586 171 VYSPMKYYGMTEPGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSFLVSTDPEKMKAAIGTMDY 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       250 IIDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQM 329
Cdd:PLN02586 251 IIDTVSAVHALGPLLGLLKVNGKLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRM 330

                        330       340
                 ....*....|....*....|....*.
5VKT_B       330 DYVNTAIERLEKNDVRYRFVIDVAGS 355
Cdd:PLN02586 331 DEINTAMERLAKSDVRYRFVIDVANS 356
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 11-351 1.32e-118

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 346.33  E-value: 1.32e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       11 HGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDT 90
Cdd:COG1064   2 KAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       91 VGVGyFVDSCRTCESCSTGHENYCPDLVLTsnGVDHHhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTV 170
Cdd:COG1064  82 VGVG-WVDSCGTCEYCRSGRENLCENGRFT--GYTTD-------GGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      171 YSPMAQYALnEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDA--AQMKAAAATLD 248
Cdd:COG1064 152 YRALRRAGV-GPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELAR-ELGADHVVNSSDEdpVEAVRELTGAD 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      249 GIIDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQ 328
Cdd:COG1064 230 VVIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIP 309

                       330       340
                ....*....|....*....|...
5VKT_B      329 MDYVNTAIERLEKNDVRYRFVID 351
Cdd:COG1064 310 LEEANEALERLRAGKVRGRAVLD 332
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 36-149 3.57e-29

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: 108.46  E-value: 3.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         36 DVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgYFVDSCRTCESCSTGHENYCP 115
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVV-EPLIPCGKCEYCREGRYNLCP 80

                          90       100       110
                  ....*....|....*....|....*....|....
5VKT_B        116 DLvltsngvdhHHHGATTKGGFSDVLVVSQDFVV 149
Cdd:pfam08240  81 NG---------RFLGYDRDGGFAEYVVVPERNLV 105
Rxyl_3153 TIGR03989
NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within ...
 33-277 2.36e-24

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


Pssm-ID: 274905 [Multi-domain]  Cd Length: 369  Bit Score: 102.39  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:TIGR03989  25 KAGEVLVKLVASGLCHSDEHLVTGDLPMPRYPILGGHEGAGVVTKVGPGVTGVKPGDHV-VLSFIPACGRCRYCSTGLQN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        113 YCpDL---VLT----SNGVDHHHHGATTK------GGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYAL 179
Cdd:TIGR03989 104 LC-DLgaaLLTgsqiSDGTYRFHADGQDVgqmcllGTFSEYTVVPEASVVKIDDDIPLDKACLVGCGVPTGWGSAVNIAD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        180 NEPGKHLGVVGLGGLGHMAVKFAKAFG-MTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAAT----LDGIIDTV 254
Cdd:TIGR03989 183 VRPGDTVVVMGIGGVGINAVQGAAVAGaRKVIAVDPVEFKREQAL-KFGATHAFASMEEAVQLVRELTngqgADKTIITV 261

                         250       260
                  ....*....|....*....|....*
5VKT_B        255 S--AGHQIVPLLALLKPMGQMVVVG 277
Cdd:TIGR03989 262 GevDGEHIAEALSATRKGGRVVVTG 286
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 63-224 9.34e-08

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 52.78  E-value: 9.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B          63 YPVVPGHEVVGVVTDVGHGVTKFKAGDTVGvgyfvdscrtcescstghenycpdlvltsngvdhhhhgATTKGGFSDVLV 142
Cdd:smart00829  22 GEAVLGGECAGVVTRVGPGVTGLAVGDRVM--------------------------------------GLAPGAFATRVV 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         143 VSQDFVVRVPESLPLDGAAPLLCAGVTVYspmaqYALNE-----PGKHlgvvglgGLGH--------MAVKFAKAFGMTV 209
Cdd:smart00829  64 TDARLVVPIPDGWSFEEAATVPVVFLTAY-----YALVDlarlrPGES-------VLIHaaaggvgqAAIQLARHLGAEV 131

                          170
                   ....*....|....*..
5VKT_B         210 TVISSSPGKRD--EALG 224
Cdd:smart00829 132 FATAGSPEKRDflRALG 148
 
Name Accession Description Interval E-value
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 11-351 6.14e-162

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: 456.57  E-value: 6.14e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       11 HGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDT 90
Cdd:cd05283   1 KGYAARDASGKLEPFTFERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGSKVTKFKVGDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       91 VGVGYFVDSCRTCESCSTGHENYCPDLVLTSNGVDhhHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTV 170
Cdd:cd05283  81 VGVGCQVDSCGTCEQCKSGEEQYCPKGVVTYNGKY--PDGTITQGGYADHIVVDERFVFKIPEGLDSAAAAPLLCAGITV 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      171 YSPMAQYALnEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDGI 250
Cdd:cd05283 159 YSPLKRNGV-GPGKRVGVVGIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDAL-KLGADEFIATKDPEAMKKAAGSLDLI 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      251 IDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMD 330
Cdd:cd05283 237 IDTVSASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAGSLIGGRKETQEMLDFAAEHGIKPWVEVIPMD 316

                       330       340
                ....*....|....*....|.
5VKT_B      331 YVNTAIERLEKNDVRYRFVID 351
Cdd:cd05283 317 GINEALERLEKGDVRYRFVLD 337
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 10-355 4.88e-161

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 455.11  E-value: 4.88e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        10 AHGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGD 89
Cdd:PLN02586  13 AFGWAARDPSGVLSPFHFSRRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGKNVKKFKEGD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        90 TVGVGYFVDSCRTCESCSTGHENYCPDLVLTSNGvdHHHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVT 169
Cdd:PLN02586  93 RVGVGVIVGSCKSCESCDQDLENYCPKMIFTYNS--IGHDGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGIT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       170 VYSPMAQYALNEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALGRLGADAFLVSHDAAQMKAAAATLDG 249
Cdd:PLN02586 171 VYSPMKYYGMTEPGKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSFLVSTDPEKMKAAIGTMDY 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       250 IIDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQM 329
Cdd:PLN02586 251 IIDTVSAVHALGPLLGLLKVNGKLITLGLPEKPLELPIFPLVLGRKLVGGSDIGGIKETQEMLDFCAKHNITADIELIRM 330

                        330       340
                 ....*....|....*....|....*.
5VKT_B       330 DYVNTAIERLEKNDVRYRFVIDVAGS 355
Cdd:PLN02586 331 DEINTAMERLAKSDVRYRFVIDVANS 356
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 8-359 1.03e-143

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 411.11  E-value: 1.03e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         8 KTAHGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKA 87
Cdd:PLN02514   8 KKTTGWAARDPSGHLSPYTYTLRKTGPEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        88 GDTVGVGYFVDSCRTCESCSTGHENYCPDLVLTSNGVDHHhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAG 167
Cdd:PLN02514  88 GDIVGVGVIVGCCGECSPCKSDLEQYCNKRIWSYNDVYTD--GKPTQGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAG 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       168 VTVYSPMAQYALNEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALGRLGADAFLVSHDAAQMKAAAATL 247
Cdd:PLN02514 166 VTVYSPLSHFGLKQSGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGADDYLVSSDAAEMQEAADSL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       248 DGIIDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVV 327
Cdd:PLN02514 246 DYIIDTVPVFHPLEPYLSLLKLDGKLILMGVINTPLQFVTPMLMLGRKVITGSFIGSMKETEEMLEFCKEKGLTSMIEVV 325

                        330       340       350
                 ....*....|....*....|....*....|..
5VKT_B       328 QMDYVNTAIERLEKNDVRYRFVIDVAGSKMEE 359
Cdd:PLN02514 326 KMDYVNTAFERLEKNDVRYRFVVDVAGSNLDA 357
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 10-362 2.03e-128

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 372.82  E-value: 2.03e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        10 AHGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGD 89
Cdd:PLN02178   7 AFGWAANDESGVLSPFHFSRRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVGKNVTKFKEGD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        90 TVGVGYFVDSCRTCESCSTGHENYCPDLVLTSNgvDHHHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVT 169
Cdd:PLN02178  87 RVGVGVIIGSCQSCESCNQDLENYCPKVVFTYN--SRSSDGTRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGIT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       170 VYSPMAQYAL-NEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALGRLGADAFLVSHDAAQMKAAAATLD 248
Cdd:PLN02178 165 VYSPMKYYGMtKESGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMD 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       249 GIIDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQ 328
Cdd:PLN02178 245 FIIDTVSAEHALLPLFSLLKVSGKLVALGLPEKPLDLPIFPLVLGRKMVGGSQIGGMKETQEMLEFCAKHKIVSDIELIK 324

                        330       340       350
                 ....*....|....*....|....*....|....
5VKT_B       329 MDYVNTAIERLEKNDVRYRFVIDVAGSKMEETVA 362
Cdd:PLN02178 325 MSDINSAMDRLAKSDVRYRFVIDVANSLLPESSA 358
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 11-351 1.32e-118

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 346.33  E-value: 1.32e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       11 HGWAARDASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDT 90
Cdd:COG1064   2 KAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGPGVTGFKVGDR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       91 VGVGyFVDSCRTCESCSTGHENYCPDLVLTsnGVDHHhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTV 170
Cdd:COG1064  82 VGVG-WVDSCGTCEYCRSGRENLCENGRFT--GYTTD-------GGYAEYVVVPARFLVKLPDGLDPAEAAPLLCAGITA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      171 YSPMAQYALnEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDA--AQMKAAAATLD 248
Cdd:COG1064 152 YRALRRAGV-GPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELAR-ELGADHVVNSSDEdpVEAVRELTGAD 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      249 GIIDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQ 328
Cdd:COG1064 230 VVIDTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPEVETIP 309

                       330       340
                ....*....|....*....|...
5VKT_B      329 MDYVNTAIERLEKNDVRYRFVID 351
Cdd:COG1064 310 LEEANEALERLRAGKVRGRAVLD 332
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 13-350 4.46e-110

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: 324.66  E-value: 4.46e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       13 WAARDAS--GHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDT 90
Cdd:cd08245   1 KAAVVHAagGPLEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       91 VGVGYFVDSCRTCESCSTGHENYCPDLVLTsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTV 170
Cdd:cd08245  81 VGVGWLVGSCGRCEYCRRGLENLCQKAVNT---------GYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITV 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      171 YSPMAQYALnEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDGI 250
Cdd:cd08245 152 YSALRDAGP-RPGERVAVLGIGGLGHLAVQYARAMGFETVAITRSPDKRELAR-KLGADEVVDSGAELDEQAAAGGADVI 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      251 IDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELP-AYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQM 329
Cdd:cd08245 230 LVTVVSGAAAEAALGGLRRGGRIVLVGLPESPPFSPdIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPMIETFPL 309

                       330       340
                ....*....|....*....|.
5VKT_B      330 DYVNTAIERLEKNDVRYRFVI 350
Cdd:cd08245 310 DQANEAYERMEKGDVRFRFVL 330
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 33-352 1.05e-71

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: 226.65  E-value: 1.05e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWG-NAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVDSCRTCESCSTGHE 111
Cdd:cd08297  25 GPGEVLVKLEASGVCHTDLHAALGDWPvKPKLPLIGGHEGAGVVVAVGPGVSGLKVGDRVGVKWLYDACGKCEYCRTGDE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 NYCPDLVLTSNGVDhhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSpmaqyALNE---------- 181
Cdd:cd08297 105 TLCPNQKNSGYTVD---------GTFAEYAIADARYVTPIPDGLSFEQAAPLLCAGVTVYK-----ALKKaglkpgdwvv 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      182 -PGkhlgvvGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFL-VSHDAAQMKAAAAT----LDGIIDTVS 255
Cdd:cd08297 171 iSG------AGGGLGHLGVQYAKAMGLRVIAIDVGDEKLELAK-ELGADAFVdFKKSDDVEAVKELTggggAHAVVVTAV 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      256 AGHQIVPLLALLKPMGQMVVVGAPST-PLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMDYVNT 334
Cdd:cd08297 244 SAAAYEQALDYLRPGGTLVCVGLPPGgFIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVKPHIQVVPLEDLNE 323

                       330
                ....*....|....*...
5VKT_B      335 AIERLEKNDVRYRFVIDV 352
Cdd:cd08297 324 VFEKMEEGKIAGRVVVDF 341
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 33-350 1.38e-66

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: 213.26  E-value: 1.38e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVDSCRTCESCSTGHEN 112
Cdd:cd08296  24 GPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVGVGWHGGHCGTCDACRRGDFV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDLVLTsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALnEPGKHLGVVGLG 192
Cdd:cd08296 104 HCENGKVT---------GVTRDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNALRNSGA-KPGDLVAVQGIG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      193 GLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDaAQMKAAAATLDG---IIDTVSAGHQIVPLLALLKP 269
Cdd:cd08296 174 GLGHLAVQYAAKMGFRTVAISRGSDKADLAR-KLGAHHYIDTSK-EDVAEALQELGGaklILATAPNAKAISALVGGLAP 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      270 MGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMDYVNTAIERLEKNDVRYRFV 349
Cdd:cd08296 252 RGKLLILGAAGEPVAVSPLQLIMGRKSIHGWPSGTALDSEDTLKFSALHGVRPMVETFPLEKANEAYDRMMSGKARFRVV 331


                .
5VKT_B      350 I 350
Cdd:cd08296 332 L 332
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 36-350 2.56e-61

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: 199.72  E-value: 2.56e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVDSCRTCESCSTGHENYCP 115
Cdd:cd08298  31 EVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGPGVTRFSVGDRVGVPWLGSTCGECRYCRSGRENLCD 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      116 DLVLTsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQyALNEPGKHLGVVGLGGLG 195
Cdd:cd08298 111 NARFT---------GYTVDGGYAEYMVADERFAYPIPEDYDDEEAAPLLCAGIIGYRALKL-AGLKPGQRLGLYGFGASA 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      196 HMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDaaqmkAAAATLDGIIDTVSAGHQIVPLLALLKPMGQMVV 275
Cdd:cd08298 181 HLALQIARYQGAEVFAFTRSGEHQELAR-ELGADWAGDSDD-----LPPEPLDAAIIFAPVGALVPAALRAVKKGGRVVL 254

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
5VKT_B      276 VGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMDYVNTAIERLEKNDVRYRFVI 350
Cdd:cd08298 255 AGIHMSDIPAFDYELLWGEKTIRSVANLTRQDGEEFLKLAAEIPIKPEVETYPLEEANEALQDLKEGRIRGAAVL 329
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 33-350 1.13e-52

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: 177.37  E-value: 1.13e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAM---YPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgYFVDSCRTCESCSTG 109
Cdd:cd05284  24 GPGQVLVRVGGAGVCHSDLHVIDGVWGGILpykLPFTLGHENAGWVEEVGSGVDGLKEGDPVVV-HPPWGCGTCRYCRRG 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      110 HENYCPDLVLTsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALN-EPGKHLGV 188
Cdd:cd05284 103 EENYCENARFP---------GIGTDGGFAEYLLVPSRRLVKLPRGLDPVEAAPLADAGLTAYHAVKKALPYlDPGSTVVV 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      189 VGLGGLGHMAVKFAKAF-GMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGHQIVPL 263
Cdd:cd05284 174 IGVGGLGHIAVQILRALtPATVIAVDRSEEALKLAE-RLGADHVLNASDDVVEEVRELTggrgADAVIDFVGSDETLALA 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      264 LALLKPMGQMVVVGAPSTpLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMDYVNTAIERLEKND 343
Cdd:cd05284 253 AKLLAKGGRYVIVGYGGH-GRLPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVKVEITKFPLEDANEALDRLREGR 331


                ....*..
5VKT_B      344 VRYRFVI 350
Cdd:cd05284 332 VTGRAVL 338
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 33-351 2.67e-44

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: 155.48  E-value: 2.67e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNE-WGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYfVDSCRTCESCSTGHE 111
Cdd:cd08254  25 GPGEVLVKVKAAGVCHSDLHILDGGvPTLTKLPLTLGHEIAGTVVEVGAGVTNFKVGDRVAVPA-VIPCGACALCRRGRG 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 NYCPDLVLTSNGVDhhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGL 191
Cdd:cd08254 104 NLCLNQGMPGLGID---------GGFAEYIVVPARALVPVPDGVPFAQAAVATDAVLTPYHAVVRAGEVKPGETVLVIGL 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      192 GGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDGIIDTVS--AGHQIVPLLA--LL 267
Cdd:cd08254 175 GGLGLNAVQIAKAMGAAVIAVDIKEEKLELAK-ELGADEVLNSLDDSPKDKKAAGLGGGFDVIFdfVGTQPTFEDAqkAV 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      268 KPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMDYVNTAIERLEKNDVRYR 347
Cdd:cd08254 254 KPGGRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQVETRPLDEIPEVLERLHKGKVKGR 333


                ....
5VKT_B      348 FVID 351
Cdd:cd08254 334 VVLV 337
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 36-314 9.19e-44

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


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 152.09  E-value: 9.19e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGNAM-YPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCSTGHENyc 114
Cdd:cd05188   1 EVLVRVEAAGLCGTDLHIRRGGYPPPPkLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNL-GCGTCELCRELCPG-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      115 pdlvltsngvdHHHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGLGGL 194
Cdd:cd05188  78 -----------GGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAALLPEPLATAYHALRRAGVLKPGDTVLVLGAGGV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      195 GHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGHQIVPLLALLKPM 270
Cdd:cd05188 147 GLLAAQLAKAAGARVIVTDRSDEKLELAK-ELGADHVIDYKEEDLEEELRLTggggADVVIDAVGGPETLAQALRLLRPG 225

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
5VKT_B      271 GQMVVVGAPSTPLELPA-YAIITGGKRVAGNGVGSVADCQAMLDF 314
Cdd:cd05188 226 GRIVVVGGTSGGPPLDDlRRLLFKELTIIGSTGGTREDFEEALDL 270
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 36-350 8.87e-42

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: 149.30  E-value: 8.87e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEW--GN----------AMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgYFVDSCRTC 103
Cdd:cd08240  27 EVLVKVTACGVCHSDLHIWDGGYdlGGgktmslddrgVKLPLVLGHEIVGEVVAVGPDAADVKVGDKVLV-YPWIGCGEC 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      104 ESCSTGHENYCPDLvltsngvdhHHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPG 183
Cdd:cd08240 106 PVCLAGDENLCAKG---------RALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACSGLTAYSAVKKLMPLVAD 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      184 KHLGVVGLGGLGHMAVKFAKAFGMT-VTVISSSPGKRDEALGRlGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGH 258
Cdd:cd08240 177 EPVVIIGAGGLGLMALALLKALGPAnIIVVDIDEAKLEAAKAA-GADVVVNGSDPDAAKRIIKAagggVDAVIDFVNNSA 255

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      259 QIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTA-DIEVVQMDYVNTAIE 337
Cdd:cd08240 256 TASLAFDILAKGGKLVLVGLFGGEATLPLPLLPLRALTIQGSYVGSLEELRELVALAKAGKLKPiPLTERPLSDVNDALD 335

                       330
                ....*....|...
5VKT_B      338 RLEKNDVRYRFVI 350
Cdd:cd08240 336 DLKAGKVVGRAVL 348
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 33-351 1.29e-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: 148.23  E-value: 1.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCSTGHEN 112
Cdd:cd08259  24 GPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGEGVERFKPGDRVILYYYI-PCGKCEYCLSGEEN 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDLVLtsngvdhhhHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYspmaqYALN----EPGKHLGV 188
Cdd:cd08259 103 LCRNRAE---------YGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVVGTAV-----HALKragvKKGDTVLV 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      189 VGLGGLGHM-AVKFAKAFGMTVTVISSSPGKRDEaLGRLGADAFLVSHDAAQMKAAAATLDGIIDTVsAGHQIVPLLALL 267
Cdd:cd08259 169 TGAGGGVGIhAIQLAKALGARVIAVTRSPEKLKI-LKELGADYVIDGSKFSEDVKKLGGADVVIELV-GSPTIEESLRSL 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      268 KPMGQMVVVG-APSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIE-VVQMDYVNTAIERLEKNDVR 345
Cdd:cd08259 247 NKGGRLVLIGnVTPDPAPLRPGLLILKEIRIIGSISATKADVEEALKLVKEGKIKPVIDrVVSLEDINEALEDLKSGKVV 326


                ....*.
5VKT_B      346 YRFVID 351
Cdd:cd08259 327 GRIVLK 332
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 39-351 3.68e-41

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 147.10  E-value: 3.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        39 IKVLFCGICHTDLHVIKNEWGNAMyPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVDSCRTCESCSTGHENYCPDlV 118
Cdd:PRK09422  30 VKMEYCGVCHTDLHVANGDFGDKT-GRILGHEGIGIVKEVGPGVTSLKVGDRVSIAWFFEGCGHCEYCTTGRETLCRS-V 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       119 LTSngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMaQYALNEPGKHLGVVGLGGLGHMA 198
Cdd:PRK09422 108 KNA--------GYTVDGGMAEQCIVTADYAVKVPEGLDPAQASSITCAGVTTYKAI-KVSGIKPGQWIAIYGAGGLGNLA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       199 VKFAK-AFGMTVTVISSSPGKRDEAlGRLGADAFLVSHDAAQMKAAAATLDG-----IIDTVS--AGHQIVpllALLKPM 270
Cdd:PRK09422 179 LQYAKnVFNAKVIAVDINDDKLALA-KEVGADLTINSKRVEDVAKIIQEKTGgahaaVVTAVAkaAFNQAV---DAVRAG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       271 GQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVVQMDYVNTAIERLEKNDVRYRFVI 350
Cdd:PRK09422 255 GRVVAVGLPPESMDLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKVVPKVQLRPLEDINDIFDEMEQGKIQGRMVI 334


                 .
5VKT_B       351 D 351
Cdd:PRK09422 335 D 335
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 33-314 6.81e-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: 138.73  E-value: 6.81e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:COG1063  23 GPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGEGVTGLKVGDRV-VVEPNIPCGECRYCRRGRYN 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDLVLTsnGVDHHHhgattkGGFSDVLVVSQDFVVRVPESLPLDGAA---PLLC-------AGVTVYS--------PM 174
Cdd:COG1063 102 LCENLQFL--GIAGRD------GGFAEYVRVPAANLVKVPDGLSDEAAAlvePLAValhaverAGVKPGDtvlvigagPI 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      175 AQyalnepgkhlgvvglgglghMAVKFAKAFG-MTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDG---- 249
Cdd:COG1063 174 GL--------------------LAALAARLAGaARVIVVDRNPERLELAR-ELGADAVVNPREEDLVEAVRELTGGrgad 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
5VKT_B      250 -IIDTVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDF 314
Cdd:COG1063 233 vVIEAVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALEL 298
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
33-305 8.30e-36

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 133.28  E-value: 8.30e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGnAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:COG1062  15 RPGEVLVRIVAAGLCHSDLHVRDGDLP-VPLPAVLGHEGAGVVEEVGPGVTGVAPGDHV-VLSFIPSCGHCRYCASGRPA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YC------------PD---LVLTSNGVDHHHHGATtkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLC------------ 165
Cdd:COG1062  93 LCeagaalngkgtlPDgtsRLSSADGEPVGHFFGQ--SSFAEYAVVPERSVVKVDKDVPLELAALLGCgvqtgagavlnt 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      166 AGVTVYSPMAQYA-----LNepgkhlgvvglgglghmAVKFAKAFG-MTVTVISSSPGKRDEALgRLGADAFLVSHDAAQ 239
Cdd:COG1062 171 AKVRPGDTVAVFGlggvgLS-----------------AVQGARIAGaSRIIAVDPVPEKLELAR-ELGATHTVNPADEDA 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
5VKT_B      240 MKAAAATLDG----IIDTVSAGHQIVPLLALLKPMGQMVVVG--APSTPLELPAYAIITGGKRVAGNGVGSV 305
Cdd:COG1062 233 VEAVRELTGGgvdyAFETTGNPAVIRQALEALRKGGTVVVVGlaPPGAEISLDPFQLLLTGRTIRGSYFGGA 304
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 33-314 8.55e-32

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


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 122.65  E-value: 8.55e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGnAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:cd08279  24 GPGEVLVRIAAAGLCHSDLHVVTGDLP-APLPAVLGHEGAGVVEEVGPGVTGVKPGDHV-VLSWIPACGTCRYCSRGQPN 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCpDLV--------------LTSNGVDHHHHGATtkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYA 178
Cdd:cd08279 102 LC-DLGagilggqlpdgtrrFTADGEPVGAMCGL--GTFAEYTVVPEASVVKIDDDIPLDRAALLGCGVTTGVGAVVNTA 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      179 LNEPGkhlgvvglgglGHMAVKFAKAFGM------------TVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAAT 246
Cdd:cd08279 179 RVRPG-----------DTVAVIGCGGVGLnaiqgariagasRIIAVDPVPEKLELAR-RFGATHTVNASEDDAVEAVRDL 246

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
5VKT_B      247 LDGI-----IDTVSAGHQIVPLLALLKPMGQMVVVG--APSTPLELPAYAIITGGKRVAGNGVGSvadCQAMLDF 314
Cdd:cd08279 247 TDGRgadyaFEAVGRAATIRQALAMTRKGGTAVVVGmgPPGETVSLPALELFLSEKRLQGSLYGS---ANPRRDI 318
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 36-351 6.62e-31

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


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 120.55  E-value: 6.62e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGNAMyPVVPGHEVVGVVTDVGHGVT---KFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:cd08263  27 EILIRVAACGVCHSDLHVLKGELPFPP-PFVLGHEISGEVVEVGPNVEnpyGLSVGDRV-VGSFIMPCGKCRYCARGKEN 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDLVLTSNGVDHHHHGAT-------------TKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYAL 179
Cdd:cd08263 105 LCEDFFAYNRLKGTLYDGTTrlfrldggpvymySMGGLAEYAVVPATALAPLPESLDYTESAVLGCAGFTAYGALKHAAD 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      180 NEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTV-ISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDG-----IIDT 253
Cdd:cd08263 185 VRPGETVAVIGVGGVGSSAIQLAKAFGASPIIaVDVRDEKLAKAK-ELGATHTVNAAKEDAVAAIREITGGrgvdvVVEA 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      254 VSAGHQIVPLLALLKPMGQMVVVG-APSTPL-ELPAYAIITGGKRVAGN-GVGSVADCQAMLDFA--GEHGVTADI-EVV 327
Cdd:cd08263 264 LGKPETFKLALDVVRDGGRAVVVGlAPGGATaEIPITRLVRRGIKIIGSyGARPRQDLPELVGLAasGKLDPEALVtHKY 343

                       330       340
                ....*....|....*....|....
5VKT_B      328 QMDYVNTAIERLEKNDVRYRFVID 351
Cdd:cd08263 344 KLEEINEAYENLRKGLIHGRAIVE 367
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 33-166 2.69e-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: 118.01  E-value: 2.69e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGnAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGvgyfVD---SCRTCESCSTG 109
Cdd:cd08234  23 GPDEVLIKVAACGICGTDLHIYEGEFG-AAPPLVPGHEFAGVVVAVGSKVTGFKVGDRVA----VDpniYCGECFYCRRG 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      110 HENYCPDLVLtsngvdhhhHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAA---PLLCA 166
Cdd:cd08234  98 RPNLCENLTA---------VGVTRNGGFAEYVVVPAKQVYKIPDNLSFEEAAlaePLSCA 148
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 33-353 1.41e-29

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


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 116.02  E-value: 1.41e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAM-YPVVPGHEVVGVVTDVGHGVTKFKAGDTVGvgyfvdscrtcescstghe 111
Cdd:COG0604  26 GPGEVLVRVKAAGVNPADLLIRRGLYPLPPgLPFIPGSDAAGVVVAVGEGVTGFKVGDRVA------------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 nycpdlvltsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTvyspmAQYALNE-----PGKHl 186
Cdd:COG0604  87 ------------------GLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAALPLAGLT-----AWQALFDrgrlkPGETv 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      187 gvvg-lgglgHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDA-----AQMKAAAATLDGIIDTVsAGHQI 260
Cdd:COG0604 144 lvhgaaggvgSAAVQLAKALGARVIATASSPEKAELLR-ALGADHVIDYREEdfaerVRALTGGRGVDVVLDTV-GGDTL 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      261 VPLLALLKPMGQMVVVGAPSTP-LELPAYAIITGGKRVAGNGVGSV------ADCQAMLDFAGEHGVTADI-EVVQMDYV 332
Cdd:COG0604 222 ARSLRALAPGGRLVSIGAASGApPPLDLAPLLLKGLTLTGFTLFARdpaerrAALAELARLLAAGKLRPVIdRVFPLEEA 301

                       330       340
                ....*....|....*....|.
5VKT_B      333 NTAIERLEKNDVRYRFVIDVA 353
Cdd:COG0604 302 AEAHRLLESGKHRGKVVLTVD 322
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 36-149 3.57e-29

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: 108.46  E-value: 3.57e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         36 DVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgYFVDSCRTCESCSTGHENYCP 115
Cdd:pfam08240   2 EVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVV-EPLIPCGKCEYCREGRYNLCP 80

                          90       100       110
                  ....*....|....*....|....*....|....
5VKT_B        116 DLvltsngvdhHHHGATTKGGFSDVLVVSQDFVV 149
Cdd:pfam08240  81 NG---------RFLGYDRDGGFAEYVVVPERNLV 105
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 33-341 4.62e-29

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 114.75  E-value: 4.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:PRK13771  24 GKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGENVKGFKPGDRV-ASLLYAPDGTCEYCRSGEEA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       113 YCPDLVLTSNGVDhhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNePGKHLGVVGLG 192
Cdd:PRK13771 103 YCKNRLGYGEELD---------GFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGLRRAGVK-KGETVLVTGAG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       193 GLGHM-AVKFAKAFGMTVTVISSSPGKRdEALGRLgADAFLVSHDAAQMKAAAATLDGIIDTVsAGHQIVPLLALLKPMG 271
Cdd:PRK13771 173 GGVGIhAIQVAKALGAKVIAVTSSESKA-KIVSKY-ADYVIVGSKFSEEVKKIGGADIVIETV-GTPTLEESLRSLNMGG 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
5VKT_B       272 QMVVVG--APSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEV-VQMDYVNTAIERLEK 341
Cdd:PRK13771 250 KIIQIGnvDPSPTYSLRLGYIILKDIEIIGHISATKRDVEEALKLVAEGKIKPVIGAeVSLSEIDKALEELKD 322
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 33-277 5.23e-29

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: 113.95  E-value: 5.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVDSCRTCESCSTGHEN 112
Cdd:cd08258  25 GPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGPDVEGWKVGDRVVSETTFSTCGRCPYCRRGDYN 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDLVLTSNGVDhhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAA---PLLCAgvtvYSPMAQYALNEPGKHLGVV 189
Cdd:cd08258 105 LCPHRKGIGTQAD---------GGFAEYVLVPEESLHELPENLSLEAAAltePLAVA----VHAVAERSGIRPGDTVVVF 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      190 GLGGLGHMAVKFAKAFGMTVTVISSSPGK-RDEALGRLGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGHQIVPLL 264
Cdd:cd08258 172 GPGPIGLLAAQVAKLQGATVVVVGTEKDEvRLDVAKELGADAVNGGEEDLAELVNEITdgdgADVVIECSGAVPALEQAL 251

                       250
                ....*....|...
5VKT_B      265 ALLKPMGQMVVVG 277
Cdd:cd08258 252 ELLRKGGRIVQVG 264
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 37-299 2.84e-26

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: 107.58  E-value: 2.84e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       37 VTIKVLFCGICHTDLHViKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYfvDSCRTCESCSTGHENYCPD 116
Cdd:cd08278  30 VLVRIVATGICHTDLVV-RDGGLPTPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLSF--ASCGECANCLSGHPAYCEN 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      117 LV-LTSNGVD------HHHHGATTKGG-------FSDVLVVSQDFVVRVPESLPLDGAAPLLC-----AGvTVyspmaqy 177
Cdd:cd08278 107 FFpLNFSGRRpdgstpLSLDDGTPVHGhffgqssFATYAVVHERNVVKVDKDVPLELLAPLGCgiqtgAG-AV------- 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      178 aLN----EPGkhlgvvglgglGHMAVKFAKAFGM------------TVTVISSSPGKRDEALgRLGADAFLVSHDAAQMK 241
Cdd:cd08278 179 -LNvlkpRPG-----------SSIAVFGAGAVGLaavmaakiagctTIIAVDIVDSRLELAK-ELGATHVINPKEEDLVA 245

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
5VKT_B      242 AAAATLDG----IIDTVSAGHQIVPLLALLKPMGQMVVVGAPS--TPLELPAYAIITGGKRVAG 299
Cdd:cd08278 246 AIREITGGgvdyALDTTGVPAVIEQAVDALAPRGTLALVGAPPpgAEVTLDVNDLLVSGKTIRG 309
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 33-286 7.04e-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: 106.16  E-value: 7.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWgNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCSTGHEN 112
Cdd:cd08236  23 GPGEVLVKVKACGICGSDIPRYLGTG-AYHPPLVLGHEFSGTVEEVGSGVDDLAVGDRVAVNPLL-PCGKCEYCKKGEYS 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDlvLTSNGVDHHhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAA---PLLCAGVTVYSPMAQyalnePGKHLGVV 189
Cdd:cd08236 101 LCSN--YDYIGSRRD-------GAFAEYVSVPARNLIKIPDHVDYEEAAmiePAAVALHAVRLAGIT-----LGDTVVVI 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      190 GLGGLGHMAVKFAKAFGMT-VTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGHQIVPLL 264
Cdd:cd08236 167 GAGTIGLLAIQWLKILGAKrVIAVDIDDEKLAVAR-ELGADDTINPKEEDVEKVRELTegrgADLVIEAAGSPATIEQAL 245

                       250       260
                ....*....|....*....|..
5VKT_B      265 ALLKPMGQMVVVGAPSTPLELP 286
Cdd:cd08236 246 ALARPGGKVVLVGIPYGDVTLS 267
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 36-183 7.22e-25

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: 103.67  E-value: 7.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWgNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHENYCP 115
Cdd:cd05279  27 EVRIKVVATGVCHTDLHVIDGKL-PTPLPVILGHEGAGIVESIGPGVTTLKPGDKV-IPLFGPQCGKCKQCLNPRPNLCS 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      116 DLV--------------LTSNGVDHHHHGATTKggFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNE 181
Cdd:cd05279 105 KSRgtngrglmsdgtsrFTCKGKPIHHFLGTST--FAEYTVVSEISLAKIDPDAPLEKVCLIGCGFSTGYGAAVNTAKVT 182


                ..
5VKT_B      182 PG 183
Cdd:cd05279 183 PG 184
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 33-277 2.28e-24

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: 101.91  E-value: 2.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGyFVDSCRTCESCSTGHEN 112
Cdd:cd08260  24 PPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGEDVSRWRVGDRVTVP-FVLGCGTCPYCRAGDSN 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDLVLTsngvdhhhhGATTKGGFSD-VLVVSQDF-VVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVG 190
Cdd:cd08260 103 VCEHQVQP---------GFTHPGSFAEyVAVPRADVnLVRLPDDVDFVTAAGLGCRFATAFRALVHQARVKPGEWVAVHG 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      191 LGGLGHMAVKFAKAFGMTVTVISSSPGKRDEAlGRLGADAFLVSHDAAQMKAAAATLDG-----IIDTVSAGHQIVPLLA 265
Cdd:cd08260 174 CGGVGLSAVMIASALGARVIAVDIDDDKLELA-RELGAVATVNASEVEDVAAAVRDLTGggahvSVDALGIPETCRNSVA 252

                       250
                ....*....|..
5VKT_B      266 LLKPMGQMVVVG 277
Cdd:cd08260 253 SLRKRGRHVQVG 264
Rxyl_3153 TIGR03989
NDMA-dependent alcohol dehydrogenase, Rxyl_3153 family; This model describes a clade within ...
 33-277 2.36e-24

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


Pssm-ID: 274905 [Multi-domain]  Cd Length: 369  Bit Score: 102.39  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:TIGR03989  25 KAGEVLVKLVASGLCHSDEHLVTGDLPMPRYPILGGHEGAGVVTKVGPGVTGVKPGDHV-VLSFIPACGRCRYCSTGLQN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        113 YCpDL---VLT----SNGVDHHHHGATTK------GGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYAL 179
Cdd:TIGR03989 104 LC-DLgaaLLTgsqiSDGTYRFHADGQDVgqmcllGTFSEYTVVPEASVVKIDDDIPLDKACLVGCGVPTGWGSAVNIAD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        180 NEPGKHLGVVGLGGLGHMAVKFAKAFG-MTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAAT----LDGIIDTV 254
Cdd:TIGR03989 183 VRPGDTVVVMGIGGVGINAVQGAAVAGaRKVIAVDPVEFKREQAL-KFGATHAFASMEEAVQLVRELTngqgADKTIITV 261

                         250       260
                  ....*....|....*....|....*
5VKT_B        255 S--AGHQIVPLLALLKPMGQMVVVG 277
Cdd:TIGR03989 262 GevDGEHIAEALSATRKGGRVVVTG 286
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 33-166 4.24e-24

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: 101.13  E-value: 4.24e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCSTGHEN 112
Cdd:cd08235  23 GPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDRVFVAPHV-PCGECHYCLRGNEN 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
5VKT_B      113 YCPDLVLTSNGVDhhhhgattkGGFSDVLVV-----SQDFVVRVPESLPLDGAA---PLLCA 166
Cdd:cd08235 102 MCPNYKKFGNLYD---------GGFAEYVRVpawavKRGGVLKLPDNVSFEEAAlvePLACC 154
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 36-183 7.51e-24

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: 100.88  E-value: 7.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKnEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHENYCP 115
Cdd:cd08277  29 EVRIKMLATSVCHTDILAIE-GFKATLFPVILGHEGAGIVESVGEGVTNLKPGDKV-IPLFIGQCGECSNCRSGKTNLCQ 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      116 DLVLTSNGVD--------------HHHHGATTkggFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNE 181
Cdd:cd08277 107 KYRANESGLMpdgtsrftckgkkiYHFLGTST---FSQYTVVDENYVAKIDPAAPLEHVCLLGCGFSTGYGAAWNTAKVE 183


                ..
5VKT_B      182 PG 183
Cdd:cd08277 184 PG 185
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 36-161 1.09e-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: 100.31  E-value: 1.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLH-------VIKNE----WGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgYFVDSCRTCE 104
Cdd:cd08233  26 EVKIKVAWCGICGSDLHeyldgpiFIPTEghphLTGETAPVTLGHEFSGVVVEVGSGVTGFKVGDRVVV-EPTIKCGTCG 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
5VKT_B      105 SCSTGHENYCPDLVLTSNGVDHhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAA 161
Cdd:cd08233 105 ACKRGLYNLCDSLGFIGLGGGG--------GGFAEYVVVPAYHVHKLPDNVPLEEAA 153
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 14-304 1.36e-23

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: 100.14  E-value: 1.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       14 AARDASGHLSPYSFSARIQ---------GDADVTIKVLFCGICHTDLHVIKNEWGNAMyPVVPGHEVVGVVTDVGHGVTK 84
Cdd:cd08281   4 AVLRETGAPTPYADSRPLVieeveldppGPGEVLVKIAAAGLCHSDLSVINGDRPRPL-PMALGHEAAGVVVEVGEGVTD 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       85 FKAGDTVgVGYFVDSCRTCESCSTGHENYCP--------------DLVLTSNGVDHHHHgaTTKGGFSDVLVVSQDFVVR 150
Cdd:cd08281  83 LEVGDHV-VLVFVPSCGHCRPCAEGRPALCEpgaaangagtllsgGRRLRLRGGEINHH--LGVSAFAEYAVVSRRSVVK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      151 VPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGLGGLGHMAVKFAKAFGMT-VTVISSSPGKRDEALgRLGA- 228
Cdd:cd08281 160 IDKDVPLEIAALFGCAVLTGVGAVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASqVVAVDLNEDKLALAR-ELGAt 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      229 DAFLVSHDAAQMKAAAATLDGI---IDTVSAGHQIVPLLALLKPMGQMVVVG--APSTPLELPAYAIITGGKRVAGNGVG 303
Cdd:cd08281 239 ATVNAGDPNAVEQVRELTGGGVdyaFEMAGSVPALETAYEITRRGGTTVTAGlpDPEARLSVPALSLVAEERTLKGSYMG 318


                .
5VKT_B      304 S 304
Cdd:cd08281 319 S 319
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 33-350 2.83e-23

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


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 98.40  E-value: 2.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMY---PVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFvdscrtcescstg 109
Cdd:cd05289  26 GPGEVLVKVHAAGVNPVDLKIREGLLKAAFPltlPLIPGHDVAGVVVAVGPGVTGFKVGDEV-FGMT------------- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      110 henycpdlvltsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHlgvv 189
Cdd:cd05289  92 --------------------PFTRGGAYAEYVVVPADELALKPANLSFEEAAALPLAGLTAWQALFELGGLKAGQTvlih 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      190 g-lgglgHMAVKFAKAFGMTVTVISSSPGKrdEALGRLGADAFLVSHDAAQMKAAAAT-LDGIIDTVSaGHQIVPLLALL 267
Cdd:cd05289 152 gaaggvgSFAVQLAKARGARVIATASAANA--DFLRSLGADEVIDYTKGDFERAAAPGgVDAVLDTVG-GETLARSLALV 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      268 KPMGQMV-VVGAPSTPLELPAYAIITGGKRVAGNGvgsvADCQAMLDFAGEHGVTADI-EVVQMDYVNTAIERLEKNDVR 345
Cdd:cd05289 229 KPGGRLVsIAGPPPAEQAAKRRGVRAGFVFVEPDG----EQLAELAELVEAGKLRPVVdRVFPLEDAAEAHERLESGHAR 304


                ....*
5VKT_B      346 YRFVI 350
Cdd:cd05289 305 GKVVL 309
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 33-323 3.54e-22

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: 95.85  E-value: 3.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYP-VVPGHEVVGVVTDVGHGVTKFKAGDTVGVgYFVDSCRTCESCSTGHE 111
Cdd:cd08239  23 GPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQgVIPGHEPAGVVVAVGPGVTHFRVGDRVMV-YHYVGCGACRNCRRGWM 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 NYCpDLVLTSNGVDHHhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSpmAQYALNEPGKHLGVVGL 191
Cdd:cd08239 102 QLC-TSKRAAYGWNRD-------GGHAEYMLVPEKTLIPLPDDLSFADGALLLCGIGTAYH--ALRRVGVSGRDTVLVVG 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      192 GGLGHMAV-KFAKAFGMT-VTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGHQIVPLLA 265
Cdd:cd08239 172 AGPVGLGAlMLARALGAEdVIGVDPSPERLELAK-ALGADFVINSGQDDVQEIRELTsgagADVAIECSGNTAARRLALE 250

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
5VKT_B      266 LLKPMGQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTAD 323
Cdd:cd08239 251 AVRPWGRLVLVGEGGELTIEVSNDLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVD 308
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 33-318 3.97e-21

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: 93.09  E-value: 3.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFV-----DSCRTCESCS 107
Cdd:cd08231  24 EPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTDVAGEPLKVGDRVtwsvgAPCGRCYRCL 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      108 TGHENYCPdlVLTSNGVDHHHHGATTKGGFSDVLVVSQDF-VVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHL 186
Cdd:cd08231 104 VGDPTKCE--NRKKYGHEASCDDPHLSGGYAEHIYLPPGTaIVRVPDNVPDEVAAPANCALATVLAALDRAGPVGAGDTV 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      187 GVVGLGGLGHMAVKFAKAFG-MTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLD--------------GII 251
Cdd:cd08231 182 VVQGAGPLGLYAVAAAKLAGaRRVIVIDGSPERLELAR-EFGADATIDIDELPDPQRRAIVRDitggrgadvvieasGHP 260

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
5VKT_B      252 DTVSAGhqivplLALLKPMGQMVVVG--APSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEH 318
Cdd:cd08231 261 AAVPEG------LELLRRGGTYVLVGsvAPAGTVPLDPERIVRKNLTIIGVHNYDPSHLYRAVRFLERT 323
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 33-161 7.35e-21

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


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 91.87  E-value: 7.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKnewGN---AMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTG 109
Cdd:cd08261  23 GAGEVLVRVKRVGICGSDLHIYH---GRnpfASYPRILGHELSGEVVEVGEGVAGLKVGDRV-VVDPYISCGECYACRKG 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
5VKT_B      110 HENYCPDL-VLtsnGVDhhhhgatTKGGFSDVLVVSQDFVVrVPESLPLDGAA 161
Cdd:cd08261  99 RPNCCENLqVL---GVH-------RDGGFAEYIVVPADALL-VPEGLSLDQAA 140
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 33-278 6.93e-20

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: 88.95  E-value: 6.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMyPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgYFVDSCRTCESCSTGHEN 112
Cdd:cd08264  25 GPGEVLIRVKMAGVNPVDYNVINAVKVKPM-PHIPGAEFAGVVEEVGDHVKGVKKGDRVVV-YNRVFDGTCDMCLSGNEM 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCpdlvltSNGvdhHHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSpMAQYALNEPGKHLGVVGLG 192
Cdd:cd08264 103 LC------RNG---GIIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTAYH-ALKTAGLGPGETVVVFGAS 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      193 GLGHM-AVKFAKAFGMTVTVISsspgkRDEALGRLGADaFLVSHDAAQMKAAAAT--LDGIIDtvSAGHQIVPL-LALLK 268
Cdd:cd08264 173 GNTGIfAVQLAKMMGAEVIAVS-----RKDWLKEFGAD-EVVDYDEVEEKVKEITkmADVVIN--SLGSSFWDLsLSVLG 244

                       250
                ....*....|
5VKT_B      269 PMGQMVVVGA 278
Cdd:cd08264 245 RGGRLVTFGT 254
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 36-183 4.78e-19

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: 87.37  E-value: 4.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGnAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHENYCP 115
Cdd:cd08299  34 EVRIKIVATGICRSDDHVVSGKLV-TPFPVILGHEAAGIVESVGEGVTTVKPGDKV-IPLFVPQCGKCRACLNPESNLCL 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      116 DLVL--------------TSNGVDHHHHGATtkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNE 181
Cdd:cd08299 112 KNDLgkpqglmqdgtsrfTCKGKPIHHFLGT--STFSEYTVVDEIAVAKIDAAAPLEKVCLIGCGFSTGYGAAVNTAKVT 189


                ..
5VKT_B      182 PG 183
Cdd:cd08299 190 PG 191
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 33-285 7.76e-19

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: 86.13  E-value: 7.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIK-NEW--GNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGV-GYFVdsCRTCESCST 108
Cdd:cd05281  24 GPGEVLIKVLAASICGTDVHIYEwDEWaqSRIKPPLIFGHEFAGEVVEVGEGVTRVKVGDYVSAeTHIV--CGKCYQCRT 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      109 GHENYCPDLVLTsnGVDhhhhgatTKGGFSDVLVVSQDFVVRVPESLPLDGAA---PLLCAGVTVyspmaqYALNEPGKH 185
Cdd:cd05281 102 GNYHVCQNTKIL--GVD-------TDGCFAEYVVVPEENLWKNDKDIPPEIASiqePLGNAVHTV------LAGDVSGKS 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      186 LGVVGLGGLGHMAVKFAKAFGmTVTVISSSPGKRDEALGR-LGAD-AFLVSHDAAQMKAAAATLDGiIDTV--SAGHQ-- 259
Cdd:cd05281 167 VLITGCGPIGLMAIAVAKAAG-ASLVIASDPNPYRLELAKkMGADvVINPREEDVVEVKSVTDGTG-VDVVleMSGNPka 244

                       250       260
                ....*....|....*....|....*.
5VKT_B      260 IVPLLALLKPMGQMVVVGAPSTPLEL 285
Cdd:cd05281 245 IEQGLKALTPGGRVSILGLPPGPVDI 270
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
196-315 8.83e-19

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 81.50  E-value: 8.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        196 HMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKA-----AAATLDGIIDTVSAGHQIVPLLALLKPM 270
Cdd:pfam00107   4 LAAIQLAKAAGAKVIAVDGSEEKLELAK-ELGADHVINPKETDLVEEikeltGGKGVDVVFDCVGSPATLEQALKLLRPG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
5VKT_B        271 GQMVVVGAPSTPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFA 315
Cdd:pfam00107  83 GRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLL 127
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 33-161 2.24e-18

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 84.88  E-value: 2.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        33 GDADVTIKVLFCGICHTDLHVIK-NEWGNAMYPV--VPGHEVVGVVTDVGHGVTKFKAGDTV-GVGYFVdsCRTCESCST 108
Cdd:PRK05396  24 GPNDVLIKVKKTAICGTDVHIYNwDEWAQKTIPVpmVVGHEFVGEVVEVGSEVTGFKVGDRVsGEGHIV--CGHCRNCRA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
5VKT_B       109 GHENYCPDLVltsnGVdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAA 161
Cdd:PRK05396 102 GRRHLCRNTK----GV-----GVNRPGAFAEYLVIPAFNVWKIPDDIPDDLAA 145
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 37-169 6.48e-18

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: 83.82  E-value: 6.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       37 VTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHENYC-- 114
Cdd:cd08300  30 VRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVGEGVTSVKPGDHV-IPLYTPECGECKFCKSGKTNLCqk 108

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VKT_B      115 ----------PDLV--LTSNGVD-HHHHGATTkggFSDVLVVSQDFVVRVPESLPLDGAAPLLCaGVT 169
Cdd:cd08300 109 iratqgkglmPDGTsrFSCKGKPiYHFMGTST---FSEYTVVAEISVAKINPEAPLDKVCLLGC-GVT 172
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 36-169 2.63e-17

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: 81.96  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHENYCP 115
Cdd:cd08301  29 EVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHEAAGIVESVGEGVTDLKPGDHV-LPVFTGECKECRHCKSEKSNMCD 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
5VKT_B      116 DLVL---------------TSNGVDHHHHGATTKggFSDVLVVSQDFVVRVPESLPLDGAAPLLCaGVT 169
Cdd:cd08301 108 LLRIntdrgvmindgksrfSINGKPIYHFVGTST--FSEYTVVHVGCVAKINPEAPLDKVCLLSC-GVS 173
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 37-280 5.34e-17

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: 80.62  E-value: 5.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       37 VTIKVLFCGICHTDLHVIKNEWGNAM-YPVVPGHEVVGVVTDVGHGVTKFKAGDTVgvgyfvdscrtcescstghenycp 115
Cdd:cd08241  30 VRIRVEAAGVNFPDLLMIQGKYQVKPpLPFVPGSEVAGVVEAVGEGVTGFKVGDRV------------------------ 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      116 dlvltsngvdhhhHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHlgvvglgGLG 195
Cdd:cd08241  86 -------------VALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAAALPVTYGTAYHALVRRARLQPGET-------VLV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      196 H--------MAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDG-----IIDTVsAGHQIVP 262
Cdd:cd08241 146 LgaaggvglAAVQLAKALGARVIAAASSEEKLALAR-ALGADHVIDYRDPDLRERVKALTGGrgvdvVYDPV-GGDVFEA 223

                       250
                ....*....|....*...
5VKT_B      263 LLALLKPMGQMVVVGAPS 280
Cdd:cd08241 224 SLRSLAWGGRLLVIGFAS 241
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 33-161 6.14e-17

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: 80.74  E-value: 6.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIkNEWGNAMY----PVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCST 108
Cdd:cd08232  20 GPGEVRVRVAAGGICGSDLHYY-QHGGFGTVrlrePMVLGHEVSGVVEAVGPGVTGLAPGQRVAVNPSR-PCGTCDYCRA 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
5VKT_B      109 GHENYCPDLVLTSNGVDHHHhgatTKGGFSDVLVVSQDFVVRVPESLPLDGAA 161
Cdd:cd08232  98 GRPNLCLNMRFLGSAMRFPH----VQGGFREYLVVDASQCVPLPDGLSLRRAA 146
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 31-313 1.11e-16

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


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 80.01  E-value: 1.11e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       31 IQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGyFVDSCRTCESCSTGH 110
Cdd:cd05278  22 IQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGDRVSVP-CITFCGRCRFCRRGY 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      111 ENYCPDlvlTSNGVDhhhHGATTKGGFSD-VLVVSQDF-VVRVPESLPLDGAAPLLCAGVTVYSPmAQYALNEPGKHLGV 188
Cdd:cd05278 101 HAHCEN---GLWGWK---LGNRIDGGQAEyVRVPYADMnLAKIPDGLPDEDALMLSDILPTGFHG-AELAGIKPGSTVAV 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      189 VGLGGLGHMAVKFAKAFGMT-VTVISSSPGKRDEALGRLGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGHQIVPL 263
Cdd:cd05278 174 IGAGPVGLCAVAGARLLGAArIIAVDSNPERLDLAKEAGATDIINPKNGDIVEQILELTggrgVDCVIEAVGFEETFEQA 253

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
5VKT_B      264 LALLKPMGQMVVVGAPSTPLELPAYAIITG-GKRVAGNGVGSVADCQAMLD 313
Cdd:cd05278 254 VKVVRPGGTIANVGVYGKPDPLPLLGEWFGkNLTFKTGLVPVRARMPELLD 304
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 63-282 2.71e-15

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 75.71  E-value: 2.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       63 YPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFvdscrtcescstghenycpdlvltsngvdhhhHGATTKGGFSDVLV 142
Cdd:cd08268  57 LPARLGYEAAGVVEAVGAGVTGFAVGDRVSVIPA--------------------------------ADLGQYGTYAEYAL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      143 VSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGLGGLG-HMAVKFAKAFGMTVTVISSSPGKRDE 221
Cdd:cd08268 105 VPAAAVVKLPDGLSFVEAAALWMQYLTAYGALVELAGLRPGDSVLITAASSSVgLAAIQIANAAGATVIATTRTSEKRDA 184

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
5VKT_B      222 ALgRLGADAFLVSHDAAQMKAAAATLDG-----IIDTVsAGHQIVPLLALLKPMGQMVVVGAPSTP 282
Cdd:cd08268 185 LL-ALGAAHVIVTDEEDLVAEVLRITGGkgvdvVFDPV-GGPQFAKLADALAPGGTLVVYGALSGE 248
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 33-352 5.15e-15

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


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 74.99  E-value: 5.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWG-NAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHE 111
Cdd:cd08266  26 GPDEVLVRVKAAALNHLDLWVRRGMPGiKLPLPHILGSDGAGVVEAVGPGVTNVKPGQRV-VIYPGISCGRCEYCLAGRE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 NYCPDLVLtsngvdhhhHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHL-GVVG 190
Cdd:cd08266 105 NLCAQYGI---------LGEHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAAPLTFLTAWHMLVTRARLRPGETVlVHGA 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      191 LGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAfLVSHDAAQMKAAAATL------DGIIDTVSAGHQIVPLL 264
Cdd:cd08266 176 GSGVGSAAIQIAKLFGATVIATAGSEDKLERAK-ELGADY-VIDYRKEDFVREVRELtgkrgvDVVVEHVGAATWEKSLK 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      265 AlLKPMGQMVVVGA---PSTPLELpaYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIE-VVQMDYVNTAIERLE 340
Cdd:cd08266 254 S-LARGGRLVTCGAttgYEAPIDL--RHVFWRQLSILGSTMGTKAELDEALRLVFRGKLKPVIDsVFPLEEAAEAHRRLE 330

                       330
                ....*....|..
5VKT_B      341 KNDVRYRFVIDV 352
Cdd:cd08266 331 SREQFGKIVLTP 342
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 33-327 6.20e-15

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 74.88  E-value: 6.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAM-YPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFvdscrtcescSTGHE 111
Cdd:cd08276  26 GPGEVLVRVHAVSLNYRDLLILNGRYPPPVkDPLIPLSDGAGEVVAVGEGVTRFKVGDRV-VPTF----------FPNWL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 NYCPDLVLTSNGVdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGL 191
Cdd:cd08276  95 DGPPTAEDEASAL-----GGPIDGVLAEYVVLPEEGLVRAPDHLSFEEAATLPCAGLTAWNALFGLGPLKPGDTVLVQGT 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      192 GGLGHMAVKFAKAFGMTVTVISSSPGKRdEALGRLGADAFLVSHDAAQMKAAAATL------DGIIDTVSAGHQIVPLLA 265
Cdd:cd08276 170 GGVSLFALQFAKAAGARVIATSSSDEKL-ERAKALGADHVINYRTTPDWGEEVLKLtggrgvDHVVEVGGPGTLAQSIKA 248

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
5VKT_B      266 lLKPMGQMVVVGAPS-TPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADIEVV 327
Cdd:cd08276 249 -VAPGGVISLIGFLSgFEAPVLLLPLLTKGATLRGIAVGSRAQFEAMNRAIEAHRIRPVIDRV 310
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 36-341 7.12e-15

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 74.56  E-value: 7.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGNAM---YPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFvdscrtcescstghen 112
Cdd:cd08267  28 EVLVKVHAASVNPVDWKLRRGPPKLLLgrpFPPIPGMDFAGEVVAVGSGVTRFKVGDEV-FGRL---------------- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 ycpdlvltsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHlgvvg-l 191
Cdd:cd08267  91 -----------------PPKGGGALAEYVVAPESGLAKKPEGVSFEEAAALPVAGLTALQALRDAGKVKPGQRvlingas 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      192 gglgHMAVKFAKAFGMTVTVIsSSPGKRDEALGrLGADAFL--VSHDAAQMKAAAATLDGIIDTVSAGHQIVP-LLALLK 268
Cdd:cd08267 154 ggvgTFAVQIAKALGAHVTGV-CSTRNAELVRS-LGADEVIdyTTEDFVALTAGGEKYDVIFDAVGNSPFSLYrASLALK 231

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5VKT_B      269 PMGQMVVVGAPS-----TPLELPAYAIITGGKRVAGNGVGSVADCQAMLDFAGEHGVTADI-EVVQMDYVNTAIERLEK 341
Cdd:cd08267 232 PGGRYVSVGGGPsglllVLLLLPLTLGGGGRRLKFFLAKPNAEDLEQLAELVEEGKLKPVIdSVYPLEDAPEAYRRLKS 310
PRK10083 PRK10083
putative oxidoreductase; Provisional
 36-161 9.60e-15

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 74.39  E-value: 9.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        36 DVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYfVDSCRTCESCSTGHENYCP 115
Cdd:PRK10083  26 EVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVDAARIGERVAVDP-VISCGHCYPCSIGKPNVCT 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
5VKT_B       116 DLVLTsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAA 161
Cdd:PRK10083 105 SLVVL---------GVHRDGGFSEYAVVPAKNAHRIPDAIADQYAV 141
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 33-288 2.18e-14

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 73.08  E-value: 2.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgyfvdscrtcescstghen 112
Cdd:cd08271  26 GAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTGWKVGDRVAY------------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 ycpdlvltsngvdhhHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHL-GVVGL 191
Cdd:cd08271  87 ---------------HASLARGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQALFKKLRIEAGRTIlITGGA 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      192 GGLGHMAVKFAKAFGMTVTVISSSPGKrdEALGRLGADAFLVSHDAAQMKAAAATLDG-----IIDTVSAGHQIVpLLAL 266
Cdd:cd08271 152 GGVGSFAVQLAKRAGLRVITTCSKRNF--EYVKSLGADHVIDYNDEDVCERIKEITGGrgvdaVLDTVGGETAAA-LAPT 228

                       250       260
                ....*....|....*....|..
5VKT_B      267 LKPMGQMVVVGAPSTPLELPAY 288
Cdd:cd08271 229 LAFNGHLVCIQGRPDASPDPPF 250
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 30-282 2.42e-14

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: 73.06  E-value: 2.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       30 RIQGDADVTIKVLFCGICHTDLHVIKNEWGNAmYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTG 109
Cdd:cd08284  21 QIQDPTDAIVKVTAAAICGSDLHIYRGHIPST-PGFVLGHEFVGEVVEVGPEVRTLKVGDRV-VSPFTIACGECFYCRRG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      110 HENYCPdlvltsNGVDHHHHGATT-KGGFSD-VLVVSQDF-VVRVPESLPLDGAapLLCAGV--TVYSpMAQYALNEPGK 184
Cdd:cd08284  99 QSGRCA------KGGLFGYAGSPNlDGAQAEyVRVPFADGtLLKLPDGLSDEAA--LLLGDIlpTGYF-GAKRAQVRPGD 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      185 HLGVVGLGGLGHMAVKFAKAFGM-TVTVISSSPGKRDEAlGRLGADAFLVSHDAAQMKAAAAT----LDGIIDTVSAGHQ 259
Cdd:cd08284 170 TVAVIGCGPVGLCAVLSAQVLGAaRVFAVDPVPERLERA-AALGAEPINFEDAEPVERVREATegrgADVVLEAVGGAAA 248

                       250       260
                ....*....|....*....|...
5VKT_B      260 IVPLLALLKPMGQMVVVGAPSTP 282
Cdd:cd08284 249 LDLAFDLVRPGGVISSVGVHTAE 271
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
31-287 3.69e-14

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 72.56  E-value: 3.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        31 IQGDADVTIKVLFCGICHTDL-HVIKNewGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCSTG 109
Cdd:PRK10309  22 IKHQDDVLVKVASSGLCGSDIpRIFKN--GAHYYPITLGHEFSGYVEAVGSGVDDLHPGDAVACVPLL-PCFTCPECLRG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       110 HENYCPdlvltsngvDHHHHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAplLCAGVTVYSPMAQYALNEPGKHLGVV 189
Cdd:PRK10309  99 FYSLCA---------KYDFIGSRRDGGNAEYIVVKRKNLFALPTDMPIEDGA--FIEPITVGLHAFHLAQGCEGKNVIII 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       190 GLGGLGHMAVKFAKAFGM-TVTVISSSPGKRDEALGrLGADAFL----VSHDAAQMKAAAATLDGIIDTVSAGHQIVPL- 263
Cdd:PRK10309 168 GAGTIGLLAIQCAVALGAkSVTAIDINSEKLALAKS-LGAMQTFnsreMSAPQIQSVLRELRFDQLILETAGVPQTVELa 246

                        250       260
                 ....*....|....*....|....
5VKT_B       264 LALLKPMGQMVVVGAPSTPLELPA 287
Cdd:PRK10309 247 IEIAGPRAQLALVGTLHHDLHLTS 270
PLN02827 PLN02827
Alcohol dehydrogenase-like
 7-165 5.89e-14

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 72.24  E-value: 5.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         7 CKTAHGWAARDAsghLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEwgnAMYPVVPGHEVVGVVTDVGHGVTKFK 86
Cdd:PLN02827  13 CRAAVAWGAGEA---LVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWESQ---ALFPRIFGHEASGIVESIGEGVTEFE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        87 AGDTVgVGYFVDSCRTCESCSTGHENYCPDLVLTSNGVDH--------------HHHGATTKggFSDVLVVSQDFVVRVP 152
Cdd:PLN02827  87 KGDHV-LTVFTGECGSCRHCISGKSNMCQVLGLERKGVMHsdqktrfsikgkpvYHYCAVSS--FSEYTVVHSGCAVKVD 163

                        170
                 ....*....|...
5VKT_B       153 ESLPLDGAAPLLC 165
Cdd:PLN02827 164 PLAPLHKICLLSC 176
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 33-286 1.02e-13

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: 71.37  E-value: 1.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEwGNAMY----PVVPGHEVVGVVTDVGHGVTKFKAGDTV----GVgyfvdSCRTCE 104
Cdd:cd05285  21 GPGEVLVRVRAVGICGSDVHYYKHG-RIGDFvvkePMVLGHESAGTVVAVGSGVTHLKVGDRVaiepGV-----PCRTCE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      105 SCSTGHENYCPDLVLTSNGVDHhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSpmAQYALNEPGK 184
Cdd:cd05285  95 FCKSGRYNLCPDMRFAATPPVD--------GTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHA--CRRAGVRPGD 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      185 HLGVVGLGGLGHMAVKFAKAFGMTVTVIS-SSPGKRDEALgRLGADAFLVSHDAAQMKAAAATL--------DGIIDTVS 255
Cdd:cd05285 165 TVLVFGAGPIGLLTAAVAKAFGATKVVVTdIDPSRLEFAK-ELGATHTVNVRTEDTPESAEKIAellggkgpDVVIECTG 243

                       250       260       270
                ....*....|....*....|....*....|.
5VKT_B      256 AGHQIVPLLALLKPMGQMVVVGAPSTPLELP 286
Cdd:cd05285 244 AESCIQTAIYATRPGGTVVLVGMGKPEVTLP 274
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 33-286 3.82e-13

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: 69.53  E-value: 3.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGnAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYfvdscrtcescSTGHEN 112
Cdd:cd08249  25 GPDEVLVKVKAVALNPVDWKHQDYGFI-PSYPAILGCDFAGTVVEVGSGVTRFKVGDRV-AGF-----------VHGGNP 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCPDlvltsngvdhhhhgattKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYspMAQYALNEPGKHLGVVGLG 192
Cdd:cd08249  92 NDPR-----------------NGAFQEYVVADADLTAKIPDNISFEEAATLPVGLVTAA--LALFQKLGLPLPPPKPSPA 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      193 GLGH-------------MAVKFAKAFGMTVTVISSSpgKRDEALGRLGADAFLVSHDAAQM----KAAAATLDGIIDTVS 255
Cdd:cd08249 153 SKGKpvliwggsssvgtLAIQLAKLAGYKVITTASP--KNFDLVKSLGADAVFDYHDPDVVedirAATGGKLRYALDCIS 230

                       250       260       270
                ....*....|....*....|....*....|...
5VKT_B      256 AGHQIVPLLALLKPM--GQMVVVGAPSTPLELP 286
Cdd:cd08249 231 TPESAQLCAEALGRSggGKLVSLLPVPEETEPR 263
PLN02740 PLN02740
Alcohol dehydrogenase-like
 36-114 4.63e-13

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 69.44  E-value: 4.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        36 DVTIKVLFCGICHTDLHVIKNEwgNAM---YPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTGHEN 112
Cdd:PLN02740  37 EVRIKILYTSICHTDLSAWKGE--NEAqraYPRILGHEAAGIVESVGEGVEDLKAGDHV-IPIFNGECGDCRYCKRDKTN 113


                 ..
5VKT_B       113 YC 114
Cdd:PLN02740 114 LC 115
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 36-305 1.17e-12

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: 68.02  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGNAmyP-----VVPGHEVVGVVTDVGHGvTKFKAGDTVgVGYFVDSCRTCESCSTGH 110
Cdd:cd08230  27 EVLVRTLEVGVCGTDREIVAGEYGTA--PpgedfLVLGHEALGVVEEVGDG-SGLSPGDLV-VPTVRRPPGKCLNCRIGR 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      111 ENYCPDlvltsnGvDHHHHGATTKGGF-SDVLVVSQDFVVRVPESL--------PLDGAAPLLCAGVTVYSPMAQYalne 181
Cdd:cd08230 103 PDFCET------G-EYTERGIKGLHGFmREYFVDDPEYLVKVPPSLadvgvllePLSVVEKAIEQAEAVQKRLPTW---- 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      182 PGKHLGVVGLGGLGHMAVKFAKAFGMTVTVIS--SSPGKRDEALGRLGADAFLVSHDAAQMKAAAATLDGIIDTVSAGHQ 259
Cdd:cd08230 172 NPRRALVLGAGPIGLLAALLLRLRGFEVYVLNrrDPPDPKADIVEELGATYVNSSKTPVAEVKLVGEFDLIIEATGVPPL 251

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
5VKT_B      260 IVPLLALLKPMGQMVVVGAPST--PLELPAYAIITGgkRVAGNG--VGSV 305
Cdd:cd08230 252 AFEALPALAPNGVVILFGVPGGgrEFEVDGGELNRD--LVLGNKalVGSV 299
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 33-161 2.76e-12

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: 66.95  E-value: 2.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLH-------VIKNEWGNAMY----PVVPGHEVVGVVTDVGHGV-TKFKAGDTVGVGYFVdSC 100
Cdd:cd08262  22 GPGQVLVKVLACGICGSDLHatahpeaMVDDAGGPSLMdlgaDIVLGHEFCGEVVDYGPGTeRKLKVGTRVTSLPLL-LC 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
5VKT_B      101 RTCESCSTGhenycpdlvltsngvdhhhHGATTKGGFSDVLVVSQDFVVRVPESLPLDGAA 161
Cdd:cd08262 101 GQGASCGIG-------------------LSPEAPGGYAEYMLLSEALLLRVPDGLSMEDAA 142
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 33-279 1.68e-11

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


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 64.30  E-value: 1.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKN---EWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgvgyfvdscrtcescstg 109
Cdd:cd08269  18 GPGQVLVRVEGCGVCGSDLPAFNQgrpWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRV------------------ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      110 henycpdLVLTSngvdhhhhgattkGGFSDVLVVSQDFVVRVPESLPlDGAAPLLCAGVTVYspMAQYALNEPGKHLGVV 189
Cdd:cd08269  80 -------AGLSG-------------GAFAEYDLADADHAVPLPSLLD-GQAFPGEPLGCALN--VFRRGWIRAGKTVAVI 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      190 GLGGLGHMAVKFAKAFGM-TVTVISSSPGKRDEAlGRLGADAfLVSHDAAQMKAAAATLDG------IIDTVsaGHQIVP 262
Cdd:cd08269 137 GAGFIGLLFLQLAAAAGArRVIAIDRRPARLALA-RELGATE-VVTDDSEAIVERVRELTGgagadvVIEAV--GHQWPL 212

                       250
                ....*....|....*....
5VKT_B      263 LLA--LLKPMGQMVVVGAP 279
Cdd:cd08269 213 DLAgeLVAERGRLVIFGYH 231
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 36-114 1.68e-11

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: 64.92  E-value: 1.68e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEWGnAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCSTGHENYC 114
Cdd:cd08282  27 DAIVRITTTAICGSDLHMYRGRTG-AEPGLVLGHEAMGEVEEVGSAVESLKVGDRVVVPFNV-ACGRCRNCKRGLTGVC 103
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 31-114 2.25e-11

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: 64.19  E-value: 2.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       31 IQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYfVDSCRTCESCSTGH 110
Cdd:cd08286  22 IQEPTDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGSAVTNFKVGDRVLISC-ISSCGTCGYCRKGL 100


                ....
5VKT_B      111 ENYC 114
Cdd:cd08286 101 YSHC 104
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 33-227 4.94e-11

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


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 62.83  E-value: 4.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEW-GNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYfvdscrtcescstghe 111
Cdd:cd08251   6 GPGEVRIQVRAFSLNFGDLLCVRGLYpTMPPYPFTPGFEASGVVRAVGPHVTRLAVGDEVIAGT---------------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 nycpdlvltsngvdhhhhgATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALnEPGKHLGVVGL 191
Cdd:cd08251  70 -------------------GESMGGHATLVTVPEDQVVRKPASLSFEEACALPVVFLTVIDAFARAGL-AKGEHILIQTA 129

                       170       180       190
                ....*....|....*....|....*....|....*..
5VKT_B      192 GGLGH-MAVKFAKAFGMTVTVISSSPGKRdEALGRLG 227
Cdd:cd08251 130 TGGTGlMAVQLARLKGAEIYATASSDDKL-EYLKQLG 165
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 33-166 8.98e-11

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: 62.43  E-value: 8.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDL---HVIKNEWGNAMY------PVVPGHEVVGVVTDVGHGVTK--FKAGDTVGVGYFVdSCR 101
Cdd:cd08256  23 GPGEILVKVEACGICAGDIkcyHGAPSFWGDENQppyvkpPMIPGHEFVGRVVELGEGAEErgVKVGDRVISEQIV-PCW 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5VKT_B      102 TCESCSTGHENYCPdlvltsngvDHHHHG--ATTKGGFSDVLVVSQDFVV-RVPESLPLDGAA---PLLCA 166
Cdd:cd08256 102 NCRFCNRGQYWMCQ---------KHDLYGfqNNVNGGMAEYMRFPKEAIVhKVPDDIPPEDAIliePLACA 163
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 30-109 2.57e-10

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: 61.40  E-value: 2.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       30 RIQGDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCSTG 109
Cdd:cd08283  21 KIEDPTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGPEVRNLKVGDRV-VVPFTIACGECFYCKRG 99
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 37-296 3.52e-10

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 60.68  E-value: 3.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       37 VTIKVLFCGICHTDLHVIKNEWGNAM-YPVVPGHEVVGVVTDVGHGVTKFKAGDTV-GVGYFvdscrtcescstghenyc 114
Cdd:cd08275  29 VRVRVEACGLNFADLMARQGLYDSAPkPPFVPGFECAGTVEAVGEGVKDFKVGDRVmGLTRF------------------ 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      115 pdlvltsngvdhhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYspmaqYALNE-----PGKHlgvv 189
Cdd:cd08275  91 --------------------GGYAEVVNVPADQVFPLPDGMSFEEAAAFPVNYLTAY-----YALFElgnlrPGQS---- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      190 glgGLGHMA--------VKFAKAFGMTVTVISSSPGKRdEALGRLGADaflvshdaaqmkaaaATLD-GIIDTVSAGHQI 260
Cdd:cd08275 142 ---VLVHSAaggvglaaGQLCKTVPNVTVVGTASASKH-EALKENGVT---------------HVIDyRTQDYVEEVKKI 202

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
5VKT_B      261 VP-----------------LLALLKPMGQMVVVGAPStplelpayaIITGGKR 296
Cdd:cd08275 203 SPegvdivldalggedtrkSYDLLKPMGRLVVYGAAN---------LVTGEKR 246
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 33-230 7.40e-10

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 59.79  E-value: 7.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        33 GDADVTIKVLFCGICHTDLHVIKnEWGNAMY----PVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSCRTCESCST 108
Cdd:PLN02702  40 GPHDVRVRMKAVGICGSDVHYLK-TMRCADFvvkePMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGI-SCWRCNLCKE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       109 GHENYCPDLVLTSNGVDHhhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAplLCAGVTVYSPMAQYALNEPGKHLGV 188
Cdd:PLN02702 118 GRYNLCPEMKFFATPPVH--------GSLANQVVHPADLCFKLPENVSLEEGA--MCEPLSVGVHACRRANIGPETNVLV 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
5VKT_B       189 VGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEALGRLGADA 230
Cdd:PLN02702 188 MGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADE 229
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 64-292 7.53e-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: 59.52  E-value: 7.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       64 PVVPGHEVVGVVTDVGHGVTKFKAGDTVgvgyfvdscrtcescstghenycpdlVLTSNGVDHHHhgattkGGFSDVLVV 143
Cdd:cd08253  58 PYVPGSDGAGVVEAVGEGVDGLKVGDRV--------------------------WLTNLGWGRRQ------GTAAEYVVV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      144 SQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGK----HLGVVGLGglgHMAVKFAKAFGMTVTVISSSPGKR 219
Cdd:cd08253 106 PADQLVPLPDGVSFEQGAALGIPALTAYRALFHRAGAKAGEtvlvHGGSGAVG---HAAVQLARWAGARVIATASSAEGA 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
5VKT_B      220 DEALgRLGADAFLVSHDAAQMKAAAATLDG-----IIDtVSAGHQIVPLLALLKPMGQMVVVGAPSTPLELPAYAIIT 292
Cdd:cd08253 183 ELVR-QAGADAVFNYRAEDLADRILAATAGqgvdvIIE-VLANVNLAKDLDVLAPGGRIVVYGSGGLRGTIPINPLMA 258
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 29-125 9.73e-10

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: 59.24  E-value: 9.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       29 ARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAmYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYFVDSCRTCESCST 108
Cdd:cd08287  20 PVIEEPTDAVIRVVATCVCGSDLWPYRGVSPTR-APAPIGHEFVGVVEEVGSEVTSVKPGDFV-IAPFAISDGTCPFCRA 97

                        90
                ....*....|....*..
5VKT_B      109 GHENYCPDLVLTSNGVD 125
Cdd:cd08287  98 GFTTSCVHGGFWGAFVD 114
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 28-148 1.43e-09

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: 59.07  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       28 SARIQGDADVTIKVLFCGICHTDLHVIK-NEWGNAMY------PVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYFVdSC 100
Cdd:cd08265  45 PVPNLKPDEILIRVKACGICGSDIHLYEtDKDGYILYpgltefPVVIGHEFSGVVEKTGKNVKNFEKGDPVTAEEMM-WC 123

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
5VKT_B      101 RTCESCSTGHENYCPDLVLTsngvdhhhhGATTKGGFSDVLVVSQDFV 148
Cdd:cd08265 124 GMCRACRSGSPNHCKNLKEL---------GFSADGAFAEYIAVNARYA 162
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 36-350 1.52e-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: 58.43  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHV-IKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGvgyfvdscrtcescstghenyc 114
Cdd:cd08273  29 EVVVKVEASGVSFADVQMrRGLYPDQPPLPFTPGYDLVGRVDALGSGVTGFEVGDRVA---------------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      115 pdlvltsngvdhhhhgATTK-GGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGLGG 193
Cdd:cd08273  87 ----------------ALTRvGGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNYVTAYQMLHRAAKVLTGQRVLIHGASG 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      194 LGHMAV-KFAKAFGmtVTVISSSPGKRDEALGRLGADAFLVS-HDAAQMKAAAATLDGIIDTVSAGHqIVPLLALLKPMG 271
Cdd:cd08273 151 GVGQALlELALLAG--AEVYGTASERNHAALRELGATPIDYRtKDWLPAMLTPGGVDVVFDGVGGES-YEESYAALAPGG 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      272 QMVVVGAPST----PLELPAYAI----------ITGGKRVAGNGVGSV---------ADCQAMLDFAGEHGVTADI-EVV 327
Cdd:cd08273 228 TLVCYGGNSSllqgRRSLAALGSllarlaklklLPTGRRATFYYVWRDraedpklfrQDLTELLDLLAKGKIRPKIaKRL 307

                       330       340
                ....*....|....*....|...
5VKT_B      328 QMDYVNTAIERLEKNDVRYRFVI 350
Cdd:cd08273 308 PLSEVAEAHRLLESGKVVGKIVL 330
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 36-277 2.20e-09

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: 57.96  E-value: 2.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTDLHVIKNEwgNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVgVGYfvdscrtcescstghenycp 115
Cdd:cd05195   2 EVEVEVKAAGLNFRDVLVALGL--LPGDETPLGLECSGIVTRVGSGVTGLKVGDRV-MGL-------------------- 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      116 dlvltsngvdhhhhgatTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYspmaqYALNE-----PGK----Hl 186
Cdd:cd05195  59 -----------------APGAFATHVRVDARLVVKIPDSLSFEEAATLPVAYLTAY-----YALVDlarlqKGEsvliH- 115

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      187 gvVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDeALGRLG--ADAFLVSHDAAQMKAAAATLDG-----IIDTVSaGHQ 259
Cdd:cd05195 116 --AAAGGVGQAAIQLAQHLGAEVFATVGSEEKRE-FLRELGgpVDHIFSSRDLSFADGILRATGGrgvdvVLNSLS-GEL 191

                       250
                ....*....|....*...
5VKT_B      260 IVPLLALLKPMGQMVVVG 277
Cdd:cd05195 192 LRASWRCLAPFGRFVEIG 209
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 39-163 2.93e-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: 57.64  E-value: 2.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       39 IKVLFCGICHTDLHVIKNEWGnamYPVVPGHEVVGVVTDVGhgvtkfkAGDTVG---VGYFVDSCRTCESCSTGHENYCP 115
Cdd:cd08242  29 VRVLLAGICNTDLEIYKGYYP---FPGVPGHEFVGIVEEGP-------EAELVGkrvVGEINIACGRCEYCRRGLYTHCP 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
5VKT_B      116 DL-VLtsnGVDHHHhgattkGGFSDVLVVSQDFVVRVPESLPLDGAA---PL 163
Cdd:cd08242  99 NRtVL---GIVDRD------GAFAEYLTLPLENLHVVPDLVPDEQAVfaePL 141
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 33-285 1.66e-08

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 55.38  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHV-------------------IKNEWGNAM-YPVVPGHEVVGVVTDVGHGVTKFKAGDTVG 92
Cdd:cd08274  27 APGEVLIRVGACGVNNTDINTregwystevdgatdstgagEAGWWGGTLsFPRIQGADIVGRVVAVGEGVDTARIGERVL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       93 VgyfvdscRTCESCSTGHENYCPDLVltsngvdhhhhGATTKGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYS 172
Cdd:cd08274 107 V-------DPSIRDPPEDDPADIDYI-----------GSERDGGFAEYTVVPAENAYPVNSPLSDVELATFPCSYSTAEN 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      173 PMAQYALNEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVIsSSPGKRDEALGrLGADAFL---VSHDAAQMKAAAATLDG 249
Cdd:cd08274 169 MLERAGVGAGETVLVTGASGGVGSALVQLAKRRGAIVIAV-AGAAKEEAVRA-LGADTVIlrdAPLLADAKALGGEPVDV 246

                       250       260       270
                ....*....|....*....|....*....|....*....
5VKT_B      250 IIDTVsAGHQIVPLLALLKPMGQMVVVGA---PSTPLEL 285
Cdd:cd08274 247 VADVV-GGPLFPDLLRLLRPGGRYVTAGAiagPVVELDL 284
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 64-282 2.22e-08

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


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 54.75  E-value: 2.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       64 PVVPGHEVVGVVTDVGHGVTKFKAGDTVGvgyfvdscrtcescstghenYCpdlvltsngvdhhhhgaTTKGGFSDVLVV 143
Cdd:cd05286  55 PFVLGVEGAGVVEAVGPGVTGFKVGDRVA--------------------YA-----------------GPPGAYAEYRVV 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      144 SQDFVVRVPESLPLDGAAPLLCAGVTvyspmAQYALNE-----PGkhlgvvgLGGLGH--------MAVKFAKAFGMTV- 209
Cdd:cd05286  98 PASRLVKLPDGISDETAAALLLQGLT-----AHYLLREtypvkPG-------DTVLVHaaaggvglLLTQWAKALGATVi 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      210 -TVisSSPGKRDEALgRLGADAFLVSHDAAQMKAAA---------ATLDGI-IDTVSAGhqivplLALLKPMGQMVVVGA 278
Cdd:cd05286 166 gTV--SSEEKAELAR-AAGADHVINYRDEDFVERVReitggrgvdVVYDGVgKDTFEGS------LDSLRPRGTLVSFGN 236


                ....
5VKT_B      279 PSTP 282
Cdd:cd05286 237 ASGP 240
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 18-299 4.28e-08

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: 54.21  E-value: 4.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       18 ASGHLSPYSFSARIQGDADVTIKVLFCGICHTDLHVIKNEWGNAM-YPVVPGHEVVGVVTDVGHGVTKFKAGDTVgvgyf 96
Cdd:cd05282  10 LPLVLELVSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSRPpLPAVPGNEGVGVVVEVGSGVSGLLVGQRV----- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       97 vdscrtcescstghenycpdLVLTSNGvdhhhhgattkgGFSDVLVVSQDFVVRVPESLPLDGAA-----PLlcagvTVY 171
Cdd:cd05282  85 --------------------LPLGGEG------------TWQEYVVAPADDLIPVPDSISDEQAAmlyinPL-----TAW 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      172 SPMAQYALNEPGKHLGVVGLGGLG-HMAVKFAKAFGMTVTVISSSPGKRDEaLGRLGADAFLVSHDAA-----QMKAAAA 245
Cdd:cd05282 128 LMLTEYLKLPPGDWVIQNAANSAVgRMLIQLAKLLGFKTINVVRRDEQVEE-LKALGADEVIDSSPEDlaqrvKEATGGA 206

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
5VKT_B      246 TLDGIIDTVsAGHQIVPLLALLKPMGQMVVVGAPST-PLELPAYAIITGGKRVAG 299
Cdd:cd05282 207 GARLALDAV-GGESATRLARSLRPGGTLVNYGLLSGePVPFPRSVFIFKDITVRG 260
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 33-277 5.04e-08

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: 53.98  E-value: 5.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNewgnaMYPV------VPGHEVVGVVTDVGHGVTKFKAGDTVgvgyfvdscrtcesC 106
Cdd:cd05276  26 GPGEVLIRVAAAGVNRADLLQRQG-----LYPPppgasdILGLEVAGVVVAVGPGVTGWKVGDRV--------------C 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      107 StghenycpdLVltsngvdhhhHGattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKhl 186
Cdd:cd05276  87 A---------LL----------AG----GGYAEYVVVPAGQLLPVPEGLSLVEAAALPEVFFTAWQNLFQLGGLKAGE-- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      187 gvvglGGLGH--------MAVKFAKAFGMTVTVISSSPGKRDEALgRLGADAFLVSHDAAQMKAAAATLDG-----IIDT 253
Cdd:cd05276 142 -----TVLIHggasgvgtAAIQLAKALGARVIATAGSEEKLEACR-ALGADVAINYRTEDFAEEVKEATGGrgvdvILDM 215

                       250       260
                ....*....|....*....|....
5VKT_B      254 VSAGHqIVPLLALLKPMGQMVVVG 277
Cdd:cd05276 216 VGGDY-LARNLRALAPDGRLVLIG 238
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 63-224 9.34e-08

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 52.78  E-value: 9.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B          63 YPVVPGHEVVGVVTDVGHGVTKFKAGDTVGvgyfvdscrtcescstghenycpdlvltsngvdhhhhgATTKGGFSDVLV 142
Cdd:smart00829  22 GEAVLGGECAGVVTRVGPGVTGLAVGDRVM--------------------------------------GLAPGAFATRVV 63

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         143 VSQDFVVRVPESLPLDGAAPLLCAGVTVYspmaqYALNE-----PGKHlgvvglgGLGH--------MAVKFAKAFGMTV 209
Cdd:smart00829  64 TDARLVVPIPDGWSFEEAATVPVVFLTAY-----YALVDlarlrPGES-------VLIHaaaggvgqAAIQLARHLGAEV 131

                          170
                   ....*....|....*..
5VKT_B         210 TVISSSPGKRD--EALG 224
Cdd:smart00829 132 FATAGSPEKRDflRALG 148
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 34-291 1.42e-07

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 52.77  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        34 DADVTIKVLFCGICHTDLHVIKN-EWGNAM--YPVVPGHEVVGVVTDVGHgvTKFKAGDTVGVGYfVDSCRTCESCSTGH 110
Cdd:PRK09880  27 NNGTLVQITRGGICGSDLHYYQEgKVGNFVikAPMVLGHEVIGKIVHSDS--SGLKEGQTVAINP-SKPCGHCKYCLSHN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       111 ENYCPDLVLTSNGVDHHHhgatTKGGFSDVLVVSQDFVVRVPESLPLDG---AAPLlcaGVTVYSpmAQYALNEPGKHLG 187
Cdd:PRK09880 104 ENQCTTMRFFGSAMYFPH----VDGGFTRYKVVDTAQCIPYPEKADEKVmafAEPL---AVAIHA--AHQAGDLQGKRVF 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       188 VVGLGGLGHMAVKFAKAFGMTVTVISS-SPGKRDEALgRLGADAFLVSHDAAQMKAAAATldGIIDTV--SAGH--QIVP 262
Cdd:PRK09880 175 VSGVGPIGCLIVAAVKTLGAAEIVCADvSPRSLSLAR-EMGADKLVNPQNDDLDHYKAEK--GYFDVSfeVSGHpsSINT 251

                        250       260
                 ....*....|....*....|....*....
5VKT_B       263 LLALLKPMGQMVVVGAPSTPLELPAYAII 291
Cdd:PRK09880 252 CLEVTRAKGVMVQVGMGGAPPEFPMMTLI 280
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 64-277 3.26e-07

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: 51.12  E-value: 3.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       64 PVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYfvdscrtcescstGHenycpdlvltsngvdhhhhgattkggfSDVLVV 143
Cdd:cd08255  21 PLPPGYSSVGRVVEVGSGVTGFKPGDRVFCFG-------------PH---------------------------AERVVV 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      144 SQDFVVRVPESLPLDGAAPLlcagvtvysPMAQYALN-------EPGKHLGVVGLGGLGHMAVKFAKAFG-MTVTVISSS 215
Cdd:cd08255  61 PANLLVPLPDGLPPERAALT---------ALAATALNgvrdaepRLGERVAVVGLGLVGLLAAQLAKAAGaREVVGVDPD 131

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
5VKT_B      216 PGKRD--EALGRLGADAFLVSHDAAQMKAaaatlDGIIDTVSAGHQIVPLLALLKPMGQMVVVG 277
Cdd:cd08255 132 AARRElaEALGPADPVAADTADEIGGRGA-----DVVIEASGSPSALETALRLLRDRGRVVLVG 190
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 33-229 1.57e-06

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


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 49.18  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPvvP---GHEVVGVVTDVGHGVTKFKAGDTVGVgyfvdscrtcescstg 109
Cdd:cd08250  29 GPGEVLVKNRFVGINASDINFTAGRYDPGVKP--PfdcGFEGVGEVVAVGEGVTDFKVGDAVAT---------------- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      110 henycpdlvltsngvdhhhhgaTTKGGFSDVLVVSQDFVVRVPESLPLdgAAPLLCAGVTvyspmAQYALNEPGKHLGVV 189
Cdd:cd08250  91 ----------------------MSFGAFAEYQVVPARHAVPVPELKPE--VLPLLVSGLT-----ASIALEEVGEMKSGE 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
5VKT_B      190 GLGGLG------HMAVKFAKAFGMTVTVISSSPGKrDEALGRLGAD 229
Cdd:cd08250 142 TVLVTAaaggtgQFAVQLAKLAGCHVIGTCSSDEK-AEFLKSLGCD 186
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 48-279 2.64e-06

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


Pssm-ID: 176210 [Multi-domain]  Cd Length: 350  Bit Score: 48.76  E-value: 2.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       48 HTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVgyfvdscrtcescstghenycpdlvltsnGVDHH 127
Cdd:cd08248  58 NKKRKPQSCKYSGIEFPLTLGRDCSGVVVDIGSGVKSFEIGDEVWG-----------------------------AVPPW 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      128 HHGAttkggFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYA-LNEPGKHL----GVVGLGGLGHMAVKFA 202
Cdd:cd08248 109 SQGT-----HAEYVVVPENEVSKKPKNLSHEEAASLPYAGLTAWSALVNVGgLNPKNAAGkrvlILGGSGGVGTFAIQLL 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      203 KAFGMTVTVISSSpgKRDEALGRLGADaFLVSHDAAQMKAAAATLDG---IIDTVsAGHQIVPLLALLKPMGQMVVVGAP 279
Cdd:cd08248 184 KAWGAHVTTTCST--DAIPLVKSLGAD-DVIDYNNEDFEEELTERGKfdvILDTV-GGDTEKWALKLLKKGGTYVTLVSP 259
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 33-91 6.84e-06

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


Pssm-ID: 176250 [Multi-domain]  Cd Length: 341  Bit Score: 47.21  E-value: 6.84e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIknewgNAMYPV----------VPGHEVVGVVTDVGHGVTKFKAGDTV 91
Cdd:cd08290  28 PPNEVLVKMLAAPINPADINQI-----QGVYPIkppttpeppaVGGNEGVGEVVKVGSGVKSLKPGDWV 91
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 64-230 1.54e-05

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 46.40  E-value: 1.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       64 PVVPGHEVVGVVTDVGHGVTKFKAGDTVgvgYfvdscrtcescstghenYCPdlvltsNGVDHHHhgattkGGFSDVLVV 143
Cdd:cd08272  58 PAILGCDVAGVVEAVGEGVTRFRVGDEV---Y-----------------GCA------GGLGGLQ------GSLAEYAVV 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      144 SQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGLGGLG-HMAVKFAKAFGMTVTViSSSPGKRdEA 222
Cdd:cd08272 106 DARLLALKPANLSMREAAALPLVGITAWEGLVDRAAVQAGQTVLIHGGAGGVgHVAVQLAKAAGARVYA-TASSEKA-AF 183


                ....*...
5VKT_B      223 LGRLGADA 230
Cdd:cd08272 184 ARSLGADP 191
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
 34-229 3.97e-05

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 45.01  E-value: 3.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       34 DADVTIKVLFCGICHTDLHVIKneWGNAM---YPVVPGHEVVGVVTDVGHgvTKFKAGDTVGVgyfvdscrtcescsTGH 110
Cdd:cd08289  27 EGDVLIRVAYSSVNYKDGLASI--PGGKIvkrYPFIPGIDLAGTVVESND--PRFKPGDEVIV--------------TSY 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      111 EnycpdlvltsNGVDHHhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTvySPMAQYALN------EPGK 184
Cdd:cd08289  89 D----------LGVSHH-------GGYSEYARVPAEWVVPLPKGLTLKEAMILGTAGFT--AALSIHRLEengltpEQGP 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
5VKT_B      185 HLGVVGLGGLGHMAVKFAKAFGMTVTvisSSPGKRDEA--LGRLGAD 229
Cdd:cd08289 150 VLVTGATGGVGSLAVSILAKLGYEVV---ASTGKADAAdyLKKLGAK 193
MDR_yhdh cd08288
Yhdh putative quinone oxidoreductases; Yhdh putative quinone oxidoreductases (QOR). QOR ...
 33-169 1.14e-04

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


Pssm-ID: 176248 [Multi-domain]  Cd Length: 324  Bit Score: 43.68  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAM-YPVVPGHEVVGVVTDVGHGvtKFKAGDTVgvgyfvdscrtcescstghe 111
Cdd:cd08288  26 PEGDVTVEVHYSTLNYKDGLAITGKGGIVRtFPLVPGIDLAGTVVESSSP--RFKPGDRV-------------------- 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
5VKT_B      112 nycpdlVLTSNGVDHHHHgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVT 169
Cdd:cd08288  84 ------VLTGWGVGERHW-----GGYAQRARVKADWLVPLPEGLSARQAMAIGTAGFT 130
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 135-352 2.03e-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: 42.74  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      135 GGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTvyspmAQYALNEPG-----KHLGVVGLGGLGHMAVKFAKAFGMTV 209
Cdd:cd08270  86 GAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVT-----ALRALRRGGpllgrRVLVTGASGGVGRFAVQLAALAGAHV 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      210 TVISSSPgKRDEALGRLGADAFLVSHDaaqmKAAAATLDGIIDTVsAGHQIVPLLALLKPMGQMVVVGAPS---TPLELP 286
Cdd:cd08270 161 VAVVGSP-ARAEGLRELGAAEVVVGGS----ELSGAPVDLVVDSV-GGPQLARALELLAPGGTVVSVGSSSgepAVFNPA 234

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
5VKT_B      287 AYAIITGGKRVAG----NGVGSVADCQAMLDFAGEHGVTADIEV-VQMDYVNTAIERLEKNDVRYRFVIDV 352
Cdd:cd08270 235 AFVGGGGGRRLYTfflyDGEPLAADLARLLGLVAAGRLDPRIGWrGSWTEIDEAAEALLARRFRGKAVLDV 305
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 36-299 2.54e-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: 42.53  E-value: 2.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       36 DVTIKVLFCGICHTD-LHVIKNewGNAM--YPVVPGHEVVGVVtdVGHGVTKFKAGDTVGV-GYfvdscrtcescstghe 111
Cdd:cd05280  29 DVLIRVHYSSLNYKDaLAATGN--GGVTrnYPHTPGIDAAGTV--VSSDDPRFREGDEVLVtGY---------------- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      112 nycpDLvltsnGVDHHhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVT----VYsPMAQYALN-EPGKHL 186
Cdd:cd05280  89 ----DL-----GMNTD-------GGFAEYVRVPADWVVPLPEGLSLREAMILGTAGFTaalsVH-RLEDNGQTpEDGPVL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      187 GVVGLGGLGHMAVKFAKAFGMTVTVISsspGKRDEA--LGRLGADAFLVSHDAAQMKA---AAATLDGIIDTVsAGHQIV 261
Cdd:cd05280 152 VTGATGGVGSIAVAILAKLGYTVVALT---GKEEQAdyLKSLGASEVLDREDLLDESKkplLKARWAGAIDTV-GGDVLA 227

                       250       260       270
                ....*....|....*....|....*....|....*....
5VKT_B      262 PLLALLKPMGQMVVVG-APSTPLELPAYAIITGGKRVAG 299
Cdd:cd05280 228 NLLKQTKYGGVVASCGnAAGPELTTTVLPFILRGVSLLG 266
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 33-229 3.86e-04

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: 41.84  E-value: 3.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       33 GDADVTIKVLFCGICHTDLHVIKNEWGNAMYPVVPGHEVVGVVTDVGHGVTKFKAGDTVGVGYfVDSCRTCESCSTGHEN 112
Cdd:cd08285  23 GPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGSEVKDFKPGDRVIVPA-ITPDWRSVAAQRGYPS 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      113 YCpdlvltSNGVDHHHHGATTKGGFSDVLVV--SQDFVVRVPESLPLDgAAPLLCAGVTVYSPMAQYALNEPGKHLGVVG 190
Cdd:cd08285 102 QS------GGMLGGWKFSNFKDGVFAEYFHVndADANLAPLPDGLTDE-QAVMLPDMMSTGFHGAELANIKLGDTVAVFG 174

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
5VKT_B      191 LGGLGHMAVKFAKAFGMT-VTVISSSPgKRDEALGRLGAD 229
Cdd:cd08285 175 IGPVGLMAVAGARLRGAGrIIAVGSRP-NRVELAKEYGAT 213
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 36-352 1.99e-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: 39.85  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B         36 DVTIKVLFCGICHTDLHVIKNEwGNAM--YPVVPGHEVVGVVtdVGHGVTKFKAGDTVGV-GYfvdscrtcescstghen 112
Cdd:TIGR02823  28 DVLIKVAYSSLNYKDALAITGK-GGVVrsYPMIPGIDAAGTV--VSSEDPRFREGDEVIVtGY----------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        113 ycpDLvltsnGVDHHhhgattkGGFSDVLVVSQDFVVRVPESLPLDGAAPLLCAGVTvySPMAQYALN------EPGKHL 186
Cdd:TIGR02823  88 ---GL-----GVSHD-------GGYSQYARVPADWLVPLPEGLSLREAMALGTAGFT--AALSVMALErngltpEDGPVL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        187 GVVGLGGLGHMAVKFAKAFGMTVTVISsspGKRDEA--LGRLGADAFLVSHDAAQMK--AAAATLDGIIDTVsAGHQIVP 262
Cdd:TIGR02823 151 VTGATGGVGSLAVAILSKLGYEVVAST---GKAEEEdyLKELGASEVIDREDLSPPGkpLEKERWAGAVDTV-GGHTLAN 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B        263 LLALLKPMGQMVVVGAPSTPlELPA--YAIITGGkrVAGNGVGSV----ADCQA-------MLDFAGEHGVTadiEVVQM 329
Cdd:TIGR02823 227 VLAQLKYGGAVAACGLAGGP-DLPTtvLPFILRG--VSLLGIDSVycpmALREAawqrlatDLKPRNLESIT---REITL 300

                         330       340
                  ....*....|....*....|...
5VKT_B        330 DYVNTAIERLEKNDVRYRFVIDV 352
Cdd:TIGR02823 301 EELPEALEQILAGQHRGRTVVDV 323
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 64-230 6.24e-03

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: 38.12  E-value: 6.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B       64 PVVPGHEVVGVVTDVGHGVtkfkagDTVGVGYFVDScrtcescstghenycpdlvltsngvdhhHHGATTkGGFSDVLVV 143
Cdd:cd08244  60 PYVPGGEVAGVVDAVGPGV------DPAWLGRRVVA----------------------------HTGRAG-GGYAELAVA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5VKT_B      144 SQDFVVRVPESLPLDGAAPLLCAGVTVYSPMAQYALNEPGKHLGVVGLGGLGHMAVKFAKAFGMTVTVISSSPGKRDEAL 223
Cdd:cd08244 105 DVDSLHPVPDGLDLEAAVAVVHDGRTALGLLDLATLTPGDVVLVTAAAGGLGSLLVQLAKAAGATVVGAAGGPAKTALVR 184


                ....*..
5VKT_B      224 gRLGADA 230
Cdd:cd08244 185 -ALGADV 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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