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Conserved domains on  [gi|519047159|ref|WP_020203034|]
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L-threonine 3-dehydrogenase [Cupriavidus sp. WS]

Protein Classification

L-threonine 3-dehydrogenase( domain architecture ID 11480837)

L-threonine 3-dehydrogenase (TDH) catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate; belongs to the medium chain dehydrogenase/reductase (MDR) family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
1-341 0e+00

L-threonine 3-dehydrogenase; Validated


:

Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 711.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:PRK05396   1 MKALVKLKAEPGLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHIYNWDEWAQKTIPVPMVVGHEFVGEVVEVGSEVTGFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF 160
Cdd:PRK05396  81 VGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAFNVWKIPDDIPDDLAAIFDPFGNAVHTALSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 161 NLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMS 240
Cdd:PRK05396 161 DLVGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAKEDLRDVMAELGMTEGFDVGLEMS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 241 GVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREMFETWYKMVAMLQSGLDLTPMITHRFGVDD 320
Cdd:PRK05396 241 GAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWNKVIFKGLTIKGIYGREMFETWYKMSALLQSGLDLSPIITHRFPIDD 320
                        330       340
                 ....*....|....*....|.
gi 519047159 321 FQAGFAAMLSGNSGKVVLDWT 341
Cdd:PRK05396 321 FQKGFEAMRSGQSGKVILDWD 341
 
Name Accession Description Interval E-value
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
1-341 0e+00

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 711.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:PRK05396   1 MKALVKLKAEPGLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHIYNWDEWAQKTIPVPMVVGHEFVGEVVEVGSEVTGFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF 160
Cdd:PRK05396  81 VGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAFNVWKIPDDIPDDLAAIFDPFGNAVHTALSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 161 NLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMS 240
Cdd:PRK05396 161 DLVGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAKEDLRDVMAELGMTEGFDVGLEMS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 241 GVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREMFETWYKMVAMLQSGLDLTPMITHRFGVDD 320
Cdd:PRK05396 241 GAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWNKVIFKGLTIKGIYGREMFETWYKMSALLQSGLDLSPIITHRFPIDD 320
                        330       340
                 ....*....|....*....|.
gi 519047159 321 FQAGFAAMLSGNSGKVVLDWT 341
Cdd:PRK05396 321 FQKGFEAMRSGQSGKVILDWD 341
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
3-340 0e+00

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


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 517.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159    3 ALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIG 82
Cdd:TIGR00692   1 ALMKTKPGYGAELTEVPVPEPGPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   83 DRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSFNL 162
Cdd:TIGR00692  81 DYVSVETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  163 VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGV 242
Cdd:TIGR00692 161 SGKSVLVTGAGPIGLMAIAVAKASGAYPVIVSDPNEYRLELAKKMGATYVVNPFKEDVVKEVADLTDGEGVDVFLEMSGA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  243 PSAFATMLGHMNHGGKIAMLGIPPSQMAIDW-NQIIFKGLEIKGIYGREMFETWYKMVAMLQSG-LDLTPMITHRFGVDD 320
Cdd:TIGR00692 241 PKALEQGLQAVTPGGRVSLLGLPPGKVTIDFtNKVIFKGLTIYGITGRHMFETWYTVSRLIQSGkLDLDPIITHKFKFDK 320
                         330       340
                  ....*....|....*....|
gi 519047159  321 FQAGFAAMLSGNSGKVVLDW 340
Cdd:TIGR00692 321 FEKGFELMRSGQTGKVILSL 340
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-339 1.74e-160

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: 452.84  E-value: 1.74e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:cd05281    1 MKAIVKTKAGPGAELVEVPVPKPGPGEVLIKVLAASICGTDVHIYEWDEWAQSRIKPPLIFGHEFAGEVVEVGEGVTRVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF 160
Cdd:cd05281   81 VGDYVSAETHIVCGKCYQCRTGNYHVCQNTKILGVDTDGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVLAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 161 NLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTeGFDVGMEMS 240
Cdd:cd05281  161 DVSGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGADVVINPREEDVVEVKSVTDGT-GVDVVLEMS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 241 GVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDW-NQIIFKGLEIKGIYGREMFETWYKMVAMLQSG-LDLTPMITHRFGV 318
Cdd:cd05281  240 GNPKAIEQGLKALTPGGRVSILGLPPGPVDIDLnNLVIFKGLTVQGITGRKMFETWYQVSALLKSGkVDLSPVITHKLPL 319
                        330       340
                 ....*....|....*....|.
gi 519047159 319 DDFQAGFAAMLSGNSGKVVLD 339
Cdd:cd05281  320 EDFEEAFELMRSGKCGKVVLY 340
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-341 9.01e-138

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: 395.28  E-value: 9.01e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTErAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:COG1063    1 MKALVLHG-PGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRG---GYPFVRPPLVLGHEFVGEVVEVGEGVTGLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGV-NRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALS 159
Cdd:COG1063   77 VGDRVVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVER 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 160 FNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGME 238
Cdd:COG1063  157 AGVkPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPREEDLVEAVRELTGGRGADVVIE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 239 MSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREMfETWYKMVAMLQSG-LDLTPMITHRFG 317
Cdd:COG1063  237 AVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTR-EDFPEALELLASGrIDLEPLITHRFP 315
                        330       340
                 ....*....|....*....|....*.
gi 519047159 318 VDDFQAGFAAMLSGNSG--KVVLDWT 341
Cdd:COG1063  316 LDDAPEAFEAAADRADGaiKVVLDPD 341
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
26-133 6.67e-39

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: 133.89  E-value: 6.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   26 NDVMIRIRQTAICGTDIHIWKWDEWaqhTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHITCGFCRNCRAGRRH 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNP---PVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77
                          90       100
                  ....*....|....*....|....*...
gi 519047159  106 LCRNSVGVGVNRPGAFAEYLVIPAFNAF 133
Cdd:pfam08240  78 LCPNGRFLGYDRDGGFAEYVVVPERNLV 105
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
55-189 1.06e-12

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 67.80  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159    55 IPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeghitCGFCrncragrrhlcrnsvgvgvnrPGAFAEYLVIPAFNAFR 134
Cdd:smart00829  20 YPGEAVLGGECAGVVTRVGPGVTGLAVGDRV-------MGLA---------------------PGAFATRVVTDARLVVP 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519047159   135 IPDDIPDEIAA-IFDPFGNATHtALsFNLV----GEDVLI-TGAGPIGIMAAAIARHVGAR 189
Cdd:smart00829  72 IPDGWSFEEAAtVPVVFLTAYY-AL-VDLArlrpGESVLIhAAAGGVGQAAIQLARHLGAE 130
 
Name Accession Description Interval E-value
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
1-341 0e+00

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 711.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:PRK05396   1 MKALVKLKAEPGLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHIYNWDEWAQKTIPVPMVVGHEFVGEVVEVGSEVTGFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF 160
Cdd:PRK05396  81 VGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAFNVWKIPDDIPDDLAAIFDPFGNAVHTALSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 161 NLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMS 240
Cdd:PRK05396 161 DLVGEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAKEDLRDVMAELGMTEGFDVGLEMS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 241 GVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREMFETWYKMVAMLQSGLDLTPMITHRFGVDD 320
Cdd:PRK05396 241 GAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWNKVIFKGLTIKGIYGREMFETWYKMSALLQSGLDLSPIITHRFPIDD 320
                        330       340
                 ....*....|....*....|.
gi 519047159 321 FQAGFAAMLSGNSGKVVLDWT 341
Cdd:PRK05396 321 FQKGFEAMRSGQSGKVILDWD 341
tdh TIGR00692
L-threonine 3-dehydrogenase; This protein is a tetrameric, zinc-binding, NAD-dependent enzyme ...
3-340 0e+00

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


Pssm-ID: 129775 [Multi-domain]  Cd Length: 340  Bit Score: 517.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159    3 ALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIG 82
Cdd:TIGR00692   1 ALMKTKPGYGAELTEVPVPEPGPGEVLIKVLATSICGTDVHIYNWDEWAQSRIKPPQVVGHEVAGEVVGIGPGVEGIKVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   83 DRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSFNL 162
Cdd:TIGR00692  81 DYVSVETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGCFAEYAVVPAQNIWKNPKSIPPEYATIQEPLGNAVHTVLAGPI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  163 VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGV 242
Cdd:TIGR00692 161 SGKSVLVTGAGPIGLMAIAVAKASGAYPVIVSDPNEYRLELAKKMGATYVVNPFKEDVVKEVADLTDGEGVDVFLEMSGA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  243 PSAFATMLGHMNHGGKIAMLGIPPSQMAIDW-NQIIFKGLEIKGIYGREMFETWYKMVAMLQSG-LDLTPMITHRFGVDD 320
Cdd:TIGR00692 241 PKALEQGLQAVTPGGRVSLLGLPPGKVTIDFtNKVIFKGLTIYGITGRHMFETWYTVSRLIQSGkLDLDPIITHKFKFDK 320
                         330       340
                  ....*....|....*....|
gi 519047159  321 FQAGFAAMLSGNSGKVVLDW 340
Cdd:TIGR00692 321 FEKGFELMRSGQTGKVILSL 340
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-339 1.74e-160

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: 452.84  E-value: 1.74e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:cd05281    1 MKAIVKTKAGPGAELVEVPVPKPGPGEVLIKVLAASICGTDVHIYEWDEWAQSRIKPPLIFGHEFAGEVVEVGEGVTRVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF 160
Cdd:cd05281   81 VGDYVSAETHIVCGKCYQCRTGNYHVCQNTKILGVDTDGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVLAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 161 NLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTeGFDVGMEMS 240
Cdd:cd05281  161 DVSGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGADVVINPREEDVVEVKSVTDGT-GVDVVLEMS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 241 GVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDW-NQIIFKGLEIKGIYGREMFETWYKMVAMLQSG-LDLTPMITHRFGV 318
Cdd:cd05281  240 GNPKAIEQGLKALTPGGRVSILGLPPGPVDIDLnNLVIFKGLTVQGITGRKMFETWYQVSALLKSGkVDLSPVITHKLPL 319
                        330       340
                 ....*....|....*....|.
gi 519047159 319 DDFQAGFAAMLSGNSGKVVLD 339
Cdd:cd05281  320 EDFEEAFELMRSGKCGKVVLY 340
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
1-341 9.01e-138

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: 395.28  E-value: 9.01e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTErAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:COG1063    1 MKALVLHG-PGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRG---GYPFVRPPLVLGHEFVGEVVEVGEGVTGLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGV-NRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALS 159
Cdd:COG1063   77 VGDRVVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVER 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 160 FNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGME 238
Cdd:COG1063  157 AGVkPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPREEDLVEAVRELTGGRGADVVIE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 239 MSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREMfETWYKMVAMLQSG-LDLTPMITHRFG 317
Cdd:COG1063  237 AVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTR-EDFPEALELLASGrIDLEPLITHRFP 315
                        330       340
                 ....*....|....*....|....*.
gi 519047159 318 VDDFQAGFAAMLSGNSG--KVVLDWT 341
Cdd:COG1063  316 LDDAPEAFEAAADRADGaiKVVLDPD 341
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
1-337 1.70e-92

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: 279.80  E-value: 1.70e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTerAPG-LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAqhTIP-VPmqvGHEYVGEIVALGQEVRG 78
Cdd:cd08234    1 MKALVYE--GPGeLEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFGA--APPlVP---GHEFAGVVVAVGSKVTG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  79 LAIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTAL 158
Cdd:cd08234   74 FKVGDRVAVDPNIYCGECFYCRRGRPNLCENLTAVGVTRNGGFAEYVVVPAKQVYKIPDNLSFEEAALAEPLSCAVHGLD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 SFNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENlgDVAAELHMTEGFDVGM 237
Cdd:cd08234  154 LLGIkPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPSRED--PEAQKEDNPYGFDVVI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 238 EMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQ--IIFKGLEIKGIYgREMFeTWYKMVAMLQSG-LDLTPMITH 314
Cdd:cd08234  232 EATGVPKTLEQAIEYARRGGTVLVFGVYAPDARVSISPfeIFQKELTIIGSF-INPY-TFPRAIALLESGkIDVKGLVSH 309
                        330       340
                 ....*....|....*....|...
gi 519047159 315 RFGVDDFQAGFAAMLSGNSGKVV 337
Cdd:cd08234  310 RLPLEEVPEALEGMRSGGALKVV 332
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
1-339 4.07e-85

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 260.81  E-value: 4.07e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwDEWAQHTIP-VPmqvGHEYVGEIVALGQEVRGL 79
Cdd:COG1064    1 MKAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAE-GEWPVPKLPlVP---GHEIVGRVVAVGPGVTGF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAA-IFDPFGNATHTAL 158
Cdd:COG1064   77 KVGDRVGVGWVDSCGTCEYCRSGRENLCENGRFTGYTTDGGYAEYVVVPARFLVKLPDGLDPAEAApLLCAGITAYRALR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 SFNLV-GEDVLITGAGPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHEnlgDVAAELHMTEGFDVGM 237
Cdd:COG1064  157 RAGVGpGDRVAVIGAGGLGHLAVQIAKALGAE-VIAVDRSPEKLELARELGADHVVNSSDE---DPVEAVRELTGADVVI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 238 EMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKG--IYGREMFEtwyKMVAMLQSGlDLTPMItHR 315
Cdd:COG1064  233 DTVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGslIGTRADLQ---EMLDLAAEG-KIKPEV-ET 307
                        330       340
                 ....*....|....*....|....*
gi 519047159 316 FGVDDFQAGFAAMLSGN-SGKVVLD 339
Cdd:COG1064  308 IPLEEANEALERLRAGKvRGRAVLD 332
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
1-338 9.18e-85

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: 260.24  E-value: 9.18e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTEraPG-LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwDEWAQHtipVPMQVGHEYVGEIVALGQEVRGL 79
Cdd:cd08236    1 MKALVLTG--PGdLRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYL-GTGAYH---PPLVLGHEFSGTVEEVGSGVDDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALS 159
Cdd:cd08236   75 AVGDRVAVNPLLPCGKCEYCKKGEYSLCSNYDYIGSRRDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAAVALHAVRL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 160 FNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHmTEGFDVGME 238
Cdd:cd08236  155 AGItLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTINPKEEDVEKVRELTE-GRGADLVIE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 239 MSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAI---DWNQIIFKGLEIKGIY--------GREmfetWYKMVAMLQSG-L 306
Cdd:cd08236  234 AAGSPATIEQALALARPGGKVVLVGIPYGDVTLseeAFEKILRKELTIQGSWnsysapfpGDE----WRTALDLLASGkI 309
                        330       340       350
                 ....*....|....*....|....*....|....
gi 519047159 307 DLTPMITHRFGVDDFQAGFAAMLSGN--SGKVVL 338
Cdd:cd08236  310 KVEPLITHRLPLEDGPAAFERLADREefSGKVLL 343
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
1-338 3.27e-83

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: 256.37  E-value: 3.27e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKAlAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdewAQHTIPV-PMQVGHEYVGEIVALGQEVRGL 79
Cdd:cd08235    1 MKA-AVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKIR----GGHTDLKpPRILGHEIAGEIVEVGDGVTGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNA-----FRIPDDIPDEIAAIFDPFGNAT 154
Cdd:cd08235   76 KVGDRVFVAPHVPCGECHYCLRGNENMCPNYKKFGNLYDGGFAEYVRVPAWAVkrggvLKLPDNVSFEEAALVEPLACCI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 155 HTALSFNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGF 233
Cdd:cd08235  156 NAQRKAGIkPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEKVRELTDGRGA 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 234 DVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPP--SQMAIDWNQIIFKGLEIKGIYG--REMFEtwyKMVAMLQSG-LDL 308
Cdd:cd08235  236 DVVIVATGSPEAQAQALELVRKGGRILFFGGLPkgSTVNIDPNLIHYREITITGSYAasPEDYK---EALELIASGkIDV 312
                        330       340       350
                 ....*....|....*....|....*....|
gi 519047159 309 TPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:cd08235  313 KDLITHRFPLEDIEEAFELAADGKSLKIVI 342
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
1-340 4.79e-77

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: 240.17  E-value: 4.79e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALakTERAPG-LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEwaqhtipvPMQV-----GHEYVGEIVALGQ 74
Cdd:cd08261    1 MKAL--VCEKPGrLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRN--------PFASyprilGHELSGEVVEVGE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  75 EVRGLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAfNAFRIPDDIPDEIAAIFDPFGNAT 154
Cdd:cd08261   71 GVAGLKVGDRVVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPA-DALLVPEGLSLDQAALVEPLAIGA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 155 HTALSFNLV-GEDVLITGAGPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGF 233
Cdd:cd08261  150 HAVRRAGVTaGDTVLVVGAGPIGLGVIQVAKARGAR-VIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTDGEGA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 234 DVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKG--IYGREMFETwykMVAMLQSG-LDLTP 310
Cdd:cd08261  229 DVVIDATGNPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGsrNATREDFPD---VIDLLESGkVDPEA 305
                        330       340       350
                 ....*....|....*....|....*....|..
gi 519047159 311 MITHRFGVDDFQAGFAAMLSGNSG--KVVLDW 340
Cdd:cd08261  306 LITHRFPFEDVPEAFDLWEAPPGGviKVLIEF 337
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
1-305 6.18e-77

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: 239.14  E-value: 6.18e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPG-LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWaqhTIPVPMQVGHEYVGEIVALGQEVRGL 79
Cdd:cd08258    1 MKALVKTGPGPGnVELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYD---PVETPVVLGHEFSGTIVEVGPDVEGW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVSGEG-HITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTAL 158
Cdd:cd08258   78 KVGDRVVSETtFSTCGRCPYCRRGDYNLCPHRKGIGTQADGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAVHAVA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 SFNLV--GEDVLITGAGPIGIMAAAIARHVGARNVVITDVND-YRLALARRMGATrAVNVQHENLGDVAAELHMTEGFDV 235
Cdd:cd08258  158 ERSGIrpGDTVVVFGPGPIGLLAAQVAKLQGATVVVVGTEKDeVRLDVAKELGAD-AVNGGEEDLAELVNEITDGDGADV 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519047159 236 GMEMSGVPSAFATMLGHMNHGGKIAMLGI-PPSQMAIDWNQIIFKGLEIKGIYGREmFETWYKMVAMLQSG 305
Cdd:cd08258  237 VIECSGAVPALEQALELLRKGGRIVQVGIfGPLAASIDVERIIQKELSVIGSRSST-PASWETALRLLASG 306
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
13-339 1.37e-73

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: 231.61  E-value: 1.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHIT 92
Cdd:cd05285   10 LRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKHGRIGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVGDRVAIEPGVP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 CGFCRNCRAGRRHLCRN-----SVGVgvnrPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSFNLV-GED 166
Cdd:cd05285   90 CRTCEFCKSGRYNLCPDmrfaaTPPV----DGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRRAGVRpGDT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 167 VLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHM---TEGFDVGMEMSGVP 243
Cdd:cd05285  166 VLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNVRTEDTPESAEKIAEllgGKGPDVVIECTGAE 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 244 SAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGI--YGRemfeTWYKMVAMLQSGL-DLTPMITHRFGVDD 320
Cdd:cd05285  246 SCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVfrYAN----TYPTAIELLASGKvDVKPLITHRFPLED 321
                        330       340
                 ....*....|....*....|.
gi 519047159 321 FQAGFAAMLSGNSG--KVVLD 339
Cdd:cd05285  322 AVEAFETAAKGKKGviKVVIE 342
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
9-339 9.60e-71

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: 224.04  E-value: 9.60e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   9 RAPG-LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSG 87
Cdd:cd08232    4 HAAGdLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYQHGGFGTVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRVAV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  88 EGHITCGFCRNCRAGRRHLCRNS--VGVGVNRP---GAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTA-LSFN 161
Cdd:cd08232   84 NPSRPCGTCDYCRAGRPNLCLNMrfLGSAMRFPhvqGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVnRAGD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 162 LVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAElhmTEGFDVGMEMSG 241
Cdd:cd08232  164 LAGKRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADETVNLARDPLAAYAAD---KGDFDVVFEASG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 242 VPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYgreMFETWYKM-VAMLQSG-LDLTPMITHRFGVD 319
Cdd:cd08232  241 APAALASALRVVRPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSF---RFDDEFAEaVRLLAAGrIDVRPLITAVFPLE 317
                        330       340
                 ....*....|....*....|.
gi 519047159 320 DFQAGFA-AMLSGNSGKVVLD 339
Cdd:cd08232  318 EAAEAFAlAADRTRSVKVQLS 338
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
16-336 5.88e-70

(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: 222.42  E-value: 5.88e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  16 TDVPVPEVGHNDVMIRIRQTAICGTDIHiwkwdEWAQ---------------HTIPVPMqvGHEYVGEIVALGQEVRGLA 80
Cdd:cd08233   15 EEVPEPPVKPGEVKIKVAWCGICGSDLH-----EYLDgpifipteghphltgETAPVTL--GHEFSGVVVEVGSGVTGFK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRP-GAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTA-L 158
Cdd:cd08233   88 VGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFIGLGGGgGGFAEYVVVPAYHVHKLPDNVPLEEAALVEPLAVAWHAVrR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 SFNLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGME 238
Cdd:cd08233  168 SGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVLDPTEVDVVAEVRKLTGGGGVDVSFD 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 239 MSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGI--YGREMFEtwyKMVAMLQSG-LDLTPMITHR 315
Cdd:cd08233  248 CAGVQATLDTAIDALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGSicYTREDFE---EVIDLLASGkIDAEPLITSR 324
                        330       340
                 ....*....|....*....|..
gi 519047159 316 FGVDD-FQAGFAAMLSGNSGKV 336
Cdd:cd08233  325 IPLEDiVEKGFEELINDKEQHV 346
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
27-302 2.19e-68

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: 216.03  E-value: 2.19e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  27 DVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMqvGHEYVGEIVALGQEVRGLAIGDRVSGEGHITCGFCRNCragrRHL 106
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGYPPPPKLPLIL--GHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELC----REL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 107 CRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAA-IFDPFGNATHTALSFNLV--GEDVLITGAGPIGIMAAAIA 183
Cdd:cd05188   75 CPGGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEAAlLPEPLATAYHALRRAGVLkpGDTVLVLGAGGVGLLAAQLA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 184 RHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHmTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLG 263
Cdd:cd05188  155 KAAGAR-VIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTG-GGGADVVIDAVGGPETLAQALRLLRPGGRIVVVG 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 519047159 264 IPP-SQMAIDWNQIIFKGLEIKGIYGREMFEtWYKMVAML 302
Cdd:cd05188  233 GTSgGPPLDDLRRLLFKELTIIGSTGGTRED-FEEALDLL 271
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
2-339 1.31e-66

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: 214.43  E-value: 1.31e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   2 KALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDewaQHTIPVPMQVGHEYVGEIVALGQEVR---- 77
Cdd:cd08231    2 RAAVLTGPGKPLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGR---RPRVPLPIILGHEGVGRVVALGGGVTtdva 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  78 --GLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRP-------GAFAEYLVIPAFNAF-RIPDDIPDEIAAif 147
Cdd:cd08231   79 gePLKVGDRVTWSVGAPCGRCYRCLVGDPTKCENRKKYGHEAScddphlsGGYAEHIYLPPGTAIvRVPDNVPDEVAA-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 148 dPFGNATHTAL------SFNLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLG 221
Cdd:cd08231  157 -PANCALATVLaaldraGPVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADATIDIDELPDP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 222 DVAA---ELHMTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGI--PPSQMAIDWNQIIFKGLEIKGIYGREmFETWY 296
Cdd:cd08231  236 QRRAivrDITGGRGADVVIEASGHPAAVPEGLELLRRGGTYVLVGSvaPAGTVPLDPERIVRKNLTIIGVHNYD-PSHLY 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 519047159 297 KMVAMLQSGLDLTP---MITHRFGVDDFQAGFAAMLSGNSGKVVLD 339
Cdd:cd08231  315 RAVRFLERTQDRFPfaeLVTHRYPLEDINEALELAESGTALKVVID 360
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
17-340 1.46e-62

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: 202.94  E-value: 1.46e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  17 DVPVPEVGHNDVMIRIRQTAICGTDIHIWkWDEWAQHTIPvPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHITCGFC 96
Cdd:cd08239   16 EFPVPVPGPGEVLLRVKASGLCGSDLHYY-YHGHRAPAYQ-GVIPGHEPAGVVVAVGPGVTHFRVGDRVMVYHYVGCGAC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  97 RNCRAGRRHLCRNS-VGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAA-IFDPFGNATHTALSFNLVG-EDVLITGAG 173
Cdd:cd08239   94 RNCRRGWMQLCTSKrAAYGWNRDGGHAEYMLVPEKTLIPLPDDLSFADGAlLLCGIGTAYHALRRVGVSGrDTVLVVGAG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 174 PIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVaAELHMTEGFDVGMEMSGVPSAFATMLGHM 253
Cdd:cd08239  174 PVGLGALMLARALGAEDVIGVDPSPERLELAKALGADFVINSGQDDVQEI-RELTSGAGADVAIECSGNTAARRLALEAV 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 254 NHGGKIAMLGIPPSQMAIDWNQIIFKGleiKGIYGREMFETWYKMVA---MLQSGLDLTPMITHRFGVDDFQAGFAAMLS 330
Cdd:cd08239  253 RPWGRLVLVGEGGELTIEVSNDLIRKQ---RTLIGSWYFSVPDMEECaefLARHKLEVDRLVTHRFGLDQAPEAYALFAQ 329
                        330
                 ....*....|
gi 519047159 331 GNSGKVVLDW 340
Cdd:cd08239  330 GESGKVVFVF 339
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
13-338 2.28e-61

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 200.31  E-value: 2.28e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDewaqHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHIT 92
Cdd:COG1062    4 LEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVRDGD----LPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 CGFCRNCRAGRRHLCRNsvGVGVNRPG------------------------AFAEYLVIPAFNAFRIPDDIPDEIAAIF- 147
Cdd:COG1062   80 CGHCRYCASGRPALCEA--GAALNGKGtlpdgtsrlssadgepvghffgqsSFAEYAVVPERSVVKVDKDVPLELAALLg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 148 ----DPFGNATHTAlsfNL-VGEDVLITGAGPIG---IMAAAIArhvGARNVVITDVNDYRLALARRMGATRAVNVQHEN 219
Cdd:COG1062  158 cgvqTGAGAVLNTA---KVrPGDTVAVFGLGGVGlsaVQGARIA---GASRIIAVDPVPEKLELARELGATHTVNPADED 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 220 LGDVAAELhmTE-GFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPP--SQMAIDWNQIIFKGLEIKGIY-----GREM 291
Cdd:COG1062  232 AVEAVREL--TGgGVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPpgAEISLDPFQLLLTGRTIRGSYfggavPRRD 309
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 519047159 292 FEtwyKMVAMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:COG1062  310 IP---RLVDLYRAGrLPLDELITRRYPLDEINEAFDDLRSGEVIRPVI 354
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
1-339 6.52e-58

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: 190.92  E-value: 6.52e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPG-LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHtiPVPMQVGHEYVGEIVALGQEVRGL 79
Cdd:cd08254    1 MKAWRFHKGSKGlLVLEEVPVPEPGPGEVLVKVKAAGVCHSDLHILDGGVPTLT--KLPLTLGHEIAGTVVEVGAGVTNF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIfdpfgnAT----- 154
Cdd:cd08254   79 KVGDRVAVPAVIPCGACALCRRGRGNLCLNQGMPGLGIDGGFAEYIVVPARALVPVPDGVPFAQAAV------ATdavlt 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 155 --HTALSFNLV--GEDVLITGAGPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELhMT 230
Cdd:cd08254  153 pyHAVVRAGEVkpGETVLVIGLGGLGLNAVQIAKAMGAA-VIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAG-LG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 231 EGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYG--REMFETWYKMVAmlqSGLdL 308
Cdd:cd08254  231 GGFDVIFDFVGTQPTFEDAQKAVKPGGRIVVVGLGRDKLTVDLSDLIARELRIIGSFGgtPEDLPEVLDLIA---KGK-L 306
                        330       340       350
                 ....*....|....*....|....*....|..
gi 519047159 309 TPMITHRfGVDDFQAGFAAMLSGN-SGKVVLD 339
Cdd:cd08254  307 DPQVETR-PLDEIPEVLERLHKGKvKGRVVLV 337
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
1-338 1.28e-55

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: 185.82  E-value: 1.28e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDewaqHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:cd08279    1 MRAAVLHEVGKPLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGD----LPAPLPAVLGHEGAGVVEEVGPGVTGVK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRP--------------------GAFAEYLVIPAFNAFRIPDDIP 140
Cdd:cd08279   77 PGDHVVLSWIPACGTCRYCSRGQPNLCDLGAGILGGQLpdgtrrftadgepvgamcglGTFAEYTVVPEASVVKIDDDIP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 141 DEIAAIF-----DPFGNATHTALsfnlV--GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAV 213
Cdd:cd08279  157 LDRAALLgcgvtTGVGAVVNTAR----VrpGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGATHTV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 214 NVQHENLGDVAAELHMTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEiKGIYGremfe 293
Cdd:cd08279  233 NASEDDAVEAVRDLTDGRGADYAFEAVGRAATIRQALAMTRKGGTAVVVGMGPPGETVSLPALELFLSE-KRLQG----- 306
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 519047159 294 TWY----------KMVAMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:cd08279  307 SLYgsanprrdipRLLDLYRAGrLKLDELVTRRYSLDEINEAFADMLAGENARGVI 362
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-339 1.98e-54

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: 181.75  E-value: 1.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:cd08259    1 MKAAILHKPNKPLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKG---FFPRGKYPLILGHEIVGTVEEVGEGVERFK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDE-IAAIFDPFGNATHTALS 159
Cdd:cd08259   78 PGDRVILYYYIPCGKCEYCLSGEENLCRNRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDEsAALAACVVGTAVHALKR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 160 FNLV-GEDVLITGA-GPIGIMAAAIARHVGARNVVITDvNDYRLALARRMGATraVNVQHENLGDVAAELHmteGFDVGM 237
Cdd:cd08259  158 AGVKkGDTVLVTGAgGGVGIHAIQLAKALGARVIAVTR-SPEKLKILKELGAD--YVIDGSKFSEDVKKLG---GADVVI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 238 EMSGVPSaFATMLGHMNHGGKIAMLG-IPPSQMAIDWNQIIFKGLEIKGIYG---REMFETwykmVAMLQSGLdLTPMIT 313
Cdd:cd08259  232 ELVGSPT-IEESLRSLNKGGRLVLIGnVTPDPAPLRPGLLILKEIRIIGSISatkADVEEA----LKLVKEGK-IKPVID 305
                        330       340
                 ....*....|....*....|....*..
gi 519047159 314 HRFGVDDFQAGFAAMLSGNS-GKVVLD 339
Cdd:cd08259  306 RVVSLEDINEALEDLKSGKVvGRIVLK 332
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
16-339 1.00e-53

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


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 180.04  E-value: 1.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  16 TDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDeWAQHTIPvPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeGHI---- 91
Cdd:cd08297   17 KDVPVPEPGPGEVLVKLEASGVCHTDLHAALGD-WPVKPKL-PLIGGHEGAGVVVAVGPGVSGLKVGDRV---GVKwlyd 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  92 TCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAifdPF---GNATHTAL--SFNLVGED 166
Cdd:cd08297   92 ACGKCEYCRTGDETLCPNQKNSGYTVDGTFAEYAIADARYVTPIPDGLSFEQAA---PLlcaGVTVYKALkkAGLKPGDW 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 167 VLITGA-GPIGIMAAAIARHVGARNVVItDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGVPSA 245
Cdd:cd08297  169 VVISGAgGGLGHLGVQYAKAMGLRVIAI-DVGDEKLELAKELGADAFVDFKKSDDVEAVKELTGGGGAHAVVVTAVSAAA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 246 FATMLGHMNHGGKIAMLGIPPSQMA-IDWNQIIFKGLEIKGIY-G-----REMFEtwykMVAMlqsGLdLTPMIThRFGV 318
Cdd:cd08297  248 YEQALDYLRPGGTLVCVGLPPGGFIpLDPFDLVLRGITIVGSLvGtrqdlQEALE----FAAR---GK-VKPHIQ-VVPL 318
                        330       340
                 ....*....|....*....|..
gi 519047159 319 DDFQAGFAAMLSGN-SGKVVLD 339
Cdd:cd08297  319 EDLNEVFEKMEEGKiAGRVVVD 340
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-339 2.82e-53

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: 179.33  E-value: 2.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKW-DEWaqhtIPVPMQVGHEYVGEIVALGQEVRGL 79
Cdd:cd08260    1 MRAAVYEEFGEPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGhDPD----VTLPHVPGHEFAGVVVEVGEDVSRW 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPA--FNAFRIPDDIPDEIAAIFD-PFGNATHT 156
Cdd:cd08260   77 RVGDRVTVPFVLGCGTCPYCRAGDSNVCEHQVQPGFTHPGSFAEYVAVPRadVNLVRLPDDVDFVTAAGLGcRFATAFRA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 157 ALSFNLV--GEDVLITGAGPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENlgDVAAELH--MTEG 232
Cdd:cd08260  157 LVHQARVkpGEWVAVHGCGGVGLSAVMIASALGAR-VIAVDIDDDKLELARELGAVATVNASEVE--DVAAAVRdlTGGG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 233 FDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQ---MAIDWNQIIFKGLEIKGIYGreMFETWY-KMVAMLQSG-LD 307
Cdd:cd08260  234 AHVSVDALGIPETCRNSVASLRKRGRHVQVGLTLGEeagVALPMDRVVARELEIVGSHG--MPAHRYdAMLALIASGkLD 311
                        330       340       350
                 ....*....|....*....|....*....|...
gi 519047159 308 LTPMITHRFGVDDFQAGFAAMLS-GNSGKVVLD 339
Cdd:cd08260  312 PEPLVGRTISLDEAPDALAAMDDyATAGITVIT 344
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
1-339 3.63e-53

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: 179.01  E-value: 3.63e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKteRAPG-LAMTDVPVPEVGH-NDVMIRIRQTAICGTDIHIWKwdewaQHTI--PVPMQVGHEYVGEIVALGQEV 76
Cdd:cd05278    1 MKALVY--LGPGkIGLEEVPDPKIQGpHDAIVRVTATSICGSDLHIYR-----GGVPgaKHGMILGHEFVGEVVEVGSDV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  77 RGLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNsVGVGV---NR-PGAFAEYLVIPA--FNAFRIPDDIPDEIA-AIFDP 149
Cdd:cd05278   74 KRLKPGDRVSVPCITFCGRCRFCRRGYHAHCEN-GLWGWklgNRiDGGQAEYVRVPYadMNLAKIPDGLPDEDAlMLSDI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 150 FGNATHTALSFNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELH 228
Cdd:cd05278  153 LPTGFHGAELAGIkPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKNGDIVEQILELT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 229 MTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGI-------PPSQMAIDWNQIIFKGLEIKGIYGREMFEtwykmvaM 301
Cdd:cd05278  233 GGRGVDCVIEAVGFEETFEQAVKVVRPGGTIANVGVygkpdplPLLGEWFGKNLTFKTGLVPVRARMPELLD-------L 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 519047159 302 LQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSG--KVVLD 339
Cdd:cd05278  306 IEEGkIDPSKLITHRFPLDDILKAYRLFDNKPDGciKVVIR 346
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
18-338 8.92e-53

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: 177.98  E-value: 8.92e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  18 VPVPEVGHNDVMIRIRQTAICGTDIHIWK-----W-DEWAQHTIPVPMQVGHEYVGEIVALGQEV--RGLAIGDRVSGEG 89
Cdd:cd08256   17 VPVPRPGPGEILVKVEACGICAGDIKCYHgapsfWgDENQPPYVKPPMIPGHEFVGRVVELGEGAeeRGVKVGDRVISEQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  90 HITCGFCRNCRAGRRHLCR--NSVGVGVNRPGAFAEYLVIP--AFNaFRIPDDIPDEIAAIFDPFGNATHTALSFNLVGE 165
Cdd:cd08256   97 IVPCWNCRFCNRGQYWMCQkhDLYGFQNNVNGGMAEYMRFPkeAIV-HKVPDDIPPEDAILIEPLACALHAVDRANIKFD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 166 D-VLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENlgDVAAELHMTEGF--DVGMEMSGV 242
Cdd:cd08256  176 DvVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALARKFGADVVLNPPEVD--VVEKIKELTGGYgcDIYIEATGH 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 243 PSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNqII--FKGLEIKGIY-GREMFEtwyKMVAMLQSG-LDLTPMITHRFGV 318
Cdd:cd08256  254 PSAVEQGLNMIRKLGRFVEFSVFGDPVTVDWS-IIgdRKELDVLGSHlGPYCYP---IAIDLIASGrLPTDGIVTHQFPL 329
                        330       340
                 ....*....|....*....|.
gi 519047159 319 DDFQAGFAAMLSG-NSGKVVL 338
Cdd:cd08256  330 EDFEEAFELMARGdDSIKVVL 350
PLN02702 PLN02702
L-idonate 5-dehydrogenase
20-317 5.71e-52

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 176.51  E-value: 5.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  20 VPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHITCGFCRNC 99
Cdd:PLN02702  36 LPPLGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGSEVKHLVVGDRVALEPGISCWRCNLC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 100 RAGRRHLCRNSVGVG---VNrpGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSFNLVGE-DVLITGAGPI 175
Cdd:PLN02702 116 KEGRYNLCPEMKFFAtppVH--GSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRANIGPEtNVLVMGAGPI 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 176 GIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQhENLGDVAAELH-----MTEGFDVGMEMSGVPSAFATML 250
Cdd:PLN02702 194 GLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIVLVS-TNIEDVESEVEeiqkaMGGGIDVSFDCVGFNKTMSTAL 272
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519047159 251 GHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREmfETWYKMVAMLQSG-LDLTPMITHRFG 317
Cdd:PLN02702 273 EATRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFRYR--NTWPLCLEFLRSGkIDVKPLITHRFG 338
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
17-339 1.63e-51

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: 174.37  E-value: 1.63e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  17 DVPVPEVGH-NDVMIRIRQTAICGTDIHIWKWDEwaqhTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHITCGF 95
Cdd:cd08284   16 EVPIPQIQDpTDAIVKVTAAAICGSDLHIYRGHI----PSTPGFVLGHEFVGEVVEVGPEVRTLKVGDRVVSPFTIACGE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  96 CRNCRAGRRHLCRNSVGVG----VNRPGAFAEYLVIPA--FNAFRIPDDIPDEiAAIF--DPFGNATHTALSFNLVGED- 166
Cdd:cd08284   92 CFYCRRGQSGRCAKGGLFGyagsPNLDGAQAEYVRVPFadGTLLKLPDGLSDE-AALLlgDILPTGYFGAKRAQVRPGDt 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 167 VLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATrAVNVQHENLGDVAAELHMTEGFDVGMEMSGVPSAF 246
Cdd:cd08284  171 VAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAALGAE-PINFEDAEPVERVREATEGRGADVVLEAVGGAAAL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 247 ATMLGHMNHGGKIAMLGIP-PSQMAIDWNQIIFKGLEIKgiYGR-EMFETWYKMVAMLQSG-LDLTPMITHRFGVDDFQA 323
Cdd:cd08284  250 DLAFDLVRPGGVISSVGVHtAEEFPFPGLDAYNKNLTLR--FGRcPVRSLFPELLPLLESGrLDLEFLIDHRMPLEEAPE 327
                        330
                 ....*....|....*.
gi 519047159 324 GFAAMLSGNSGKVVLD 339
Cdd:cd08284  328 AYRLFDKRKVLKVVLD 343
PRK10083 PRK10083
putative oxidoreductase; Provisional
8-340 1.12e-49

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 169.54  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   8 ERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKW-DEWAQHtipvPMQVGHEYVGEIVALGQEVRGLAIGDRVS 86
Cdd:PRK10083   7 EKPNSLAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGhNPFAKY----PRVIGHEFFGVIDAVGEGVDAARIGERVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  87 GEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPF---GNATHTAlsfNLV 163
Cdd:PRK10083  83 VDPVISCGHCYPCSIGKPNVCTSLVVLGVHRDGGFSEYAVVPAKNAHRIPDAIADQYAVMVEPFtiaANVTGRT---GPT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 164 GEDV-LITGAGPIGIMAAAIARHV-GARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHM--TEGFDVgmem 239
Cdd:PRK10083 160 EQDVaLIYGAGPVGLTIVQVLKGVyNVKAVIVADRIDERLALAKESGADWVINNAQEPLGEALEEKGIkpTLIIDA---- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 240 SGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEI-KGIYGREMFETwykMVAMLQSGL-DLTPMITHRFG 317
Cdd:PRK10083 236 ACHPSILEEAVTLASPAARIVLMGFSSEPSEIVQQGITGKELSIfSSRLNANKFPV---VIDWLSKGLiDPEKLITHTFD 312
                        330       340
                 ....*....|....*....|....*
gi 519047159 318 VDDFQAGFAAMLS--GNSGKVVLDW 340
Cdd:PRK10083 313 FQHVADAIELFEKdqRHCCKVLLTF 337
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
1-331 1.20e-49

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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: 170.24  E-value: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEwaqhTIPVPMQVGHEYVGEIVALGQEV---R 77
Cdd:cd08263    1 MKAAVLKGPNPPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGEL----PFPPPFVLGHEISGEVVEVGPNVenpY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  78 GLAIGDRVSGEGHITCGFCRNCRAGRRHLC----------------------RNSVGVGVNRPGAFAEYLVIPAFNAFRI 135
Cdd:cd08263   77 GLSVGDRVVGSFIMPCGKCRYCARGKENLCedffaynrlkgtlydgttrlfrLDGGPVYMYSMGGLAEYAVVPATALAPL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 136 PDDIP-DEIA----AIFDPFGnATHTALSFNlVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGAT 210
Cdd:cd08263  157 PESLDyTESAvlgcAGFTAYG-ALKHAADVR-PGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAKELGAT 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 211 RAVNVQHENLGDVAAELHMTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPP--SQMAIDWNQIIFKGLEIKGIYG 288
Cdd:cd08263  235 HTVNAAKEDAVAAIREITGGRGVDVVVEALGKPETFKLALDVVRDGGRAVVVGLAPggATAEIPITRLVRRGIKIIGSYG 314
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 519047159 289 REMFETWYKMVAMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSG 331
Cdd:cd08263  315 ARPRQDLPELVGLAASGkLDPEALVTHKYKLEEINEAYENLRKG 358
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
1-264 1.38e-48

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: 166.58  E-value: 1.38e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:cd05284    1 MKAARLYEYGKPLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGGILPYKLPFTLGHENAGWVEEVGSGVDGLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDI-PDEIAAIFD----PFgNATH 155
Cdd:cd05284   81 EGDPVVVHPPWGCGTCRYCRRGEENYCENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLdPVEAAPLADagltAY-HAVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 156 TALSFNLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQhENLGDVAAELHMTEGFDV 235
Cdd:cd05284  160 KALPYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERLGADHVLNAS-DDVVEEVRELTGGRGADA 238
                        250       260
                 ....*....|....*....|....*....
gi 519047159 236 GMEMSGVPSAFATMLGHMNHGGKIAMLGI 264
Cdd:cd05284  239 VIDFVGSDETLALAAKLLAKGGRYVIVGY 267
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
5-338 9.84e-47

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: 163.07  E-value: 9.84e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   5 AKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIP----VPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:cd08265   31 SKVWRYPELRVEDVPVPNLKPDEILIRVKACGICGSDIHLYETDKDGYILYPglteFPVVIGHEFSGVVEKTGKNVKNFE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIpDDIPD--------EIAAIFDPfgn 152
Cdd:cd08265  111 KGDPVTAEEMMWCGMCRACRSGSPNHCKNLKELGFSADGAFAEYIAVNARYAWEI-NELREiysedkafEAGALVEP--- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 153 athTALSFNLV---------GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVN---VQHENL 220
Cdd:cd08265  187 ---TSVAYNGLfirgggfrpGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYVFNptkMRDCLS 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 221 GDVAAELHMTEGFDVGMEMSGVPSA-FATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREMFETWYKMV 299
Cdd:cd08265  264 GEKVMEVTKGWGADIQVEAAGAPPAtIPQMEKSIAINGKIVYIGRAATTVPLHLEVLQVRRAQIVGAQGHSGHGIFPSVI 343
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 519047159 300 AMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:cd08265  344 KLMASGkIDMTKIITARFPLEGIMEAIKAASERTDGKITI 383
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
1-339 2.21e-45

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: 158.57  E-value: 2.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTEraPG-LAMTDVPVPEVGHN-DVMIRIRQTAICGTDIHIWKWD--EWAQHTIpvpmqVGHEYVGEIVALGQEV 76
Cdd:cd08286    1 MKALVYHG--PGkISWEDRPKPTIQEPtDAIVKMLKTTICGTDLHILKGDvpTVTPGRI-----LGHEGVGVVEEVGSAV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  77 RGLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNS---VGVGVNrpGAFAEYLVIP--AFNAFRIPDDIPDEIAAIFdpfG 151
Cdd:cd08286   74 TNFKVGDRVLISCISSCGTCGYCRKGLYSHCESGgwiLGNLID--GTQAEYVRIPhaDNSLYKLPEGVDEEAAVML---S 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 152 NATHTALSFNLV------GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAA 225
Cdd:cd08286  149 DILPTGYECGVLngkvkpGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHTVNSAKGDAIEQVL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 226 ELHMTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIK-GIYGREMFETWYKMVAmlQS 304
Cdd:cd08286  229 ELTDGRGVDVVIEAVGIPATFELCQELVAPGGHIANVGVHGKPVDLHLEKLWIKNITITtGLVDTNTTPMLLKLVS--SG 306
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 519047159 305 GLDLTPMITHRFGVDDFQA---GFAAMLSGNSGKVVLD 339
Cdd:cd08286  307 KLDPSKLVTHRFKLSEIEKaydTFSAAAKHKALKVIID 344
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
1-339 3.07e-45

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


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 157.62  E-value: 3.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAP--GLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdEWAQHTIPVPMQVGHEYVGEIVALGQEVRG 78
Cdd:COG0604    1 MKAIVITEFGGpeVLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRR--GLYPLPPGLPFIPGSDAAGVVVAVGEGVTG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  79 LAIGDRVsgeghitcgfcrncragrrhlcrnsvgVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIfdpFGNATHTAL 158
Cdd:COG0604   79 FKVGDRV---------------------------AGLGRGGGYAEYVVVPADQLVPLPDGLSFEEAAA---LPLAGLTAW 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 sFNLV-------GEDVLITGA-GPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMT 230
Cdd:COG0604  129 -QALFdrgrlkpGETVLVHGAaGGVGSAAVQLAKALGAR-VIATASSPEKAELLRALGADHVIDYREEDFAERVRALTGG 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 231 EGFDVGMEMSGvPSAFATMLGHMNHGGKIAMLGIPPSQMA-IDWNQIIFKGLEIKGIYGREMF-----ETWYKMVAMLQS 304
Cdd:COG0604  207 RGVDVVLDTVG-GDTLARSLRALAPGGRLVSIGAASGAPPpLDLAPLLLKGLTLTGFTLFARDpaerrAALAELARLLAA 285
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 519047159 305 GlDLTPMITHRFGVDDFQAGFAAMLSGNS-GKVVLD 339
Cdd:COG0604  286 G-KLRPVIDRVFPLEEAAEAHRLLESGKHrGKVVLT 320
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
13-339 6.08e-45

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: 157.08  E-value: 6.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQV--------GHEYVGEIVALGQEVRG-LAIGD 83
Cdd:cd08262   11 LVVRDVPDPEPGPGQVLVKVLACGICGSDLHATAHPEAMVDDAGGPSLMdlgadivlGHEFCGEVVDYGPGTERkLKVGT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  84 RVSGEGHITCGFCRNCragrrhlcrnSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSFNLV 163
Cdd:cd08262   91 RVTSLPLLLCGQGASC----------GIGLSPEAPGGYAEYMLLSEALLLRVPDGLSMEDAALTEPLAVGLHAVRRARLT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 164 -GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDV-AAELHMTEGF--DVGMEM 239
Cdd:cd08262  161 pGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGADIVVDPAADSPFAAwAAELARAGGPkpAVIFEC 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 240 SGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREMFEtWYKMVAMLQSG-LDLTPMITHRFGV 318
Cdd:cd08262  241 VGAPGLIQQIIEGAPPGGRIVVVGVCMESDNIEPALAIRKELTLQFSLGYTPEE-FADALDALAEGkVDVAPMVTGTVGL 319
                        330       340
                 ....*....|....*....|..
gi 519047159 319 DDFQAGFAAMLSGNS-GKVVLD 339
Cdd:cd08262  320 DGVPDAFEALRDPEHhCKILVD 341
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
13-331 8.67e-44

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: 154.02  E-value: 8.67e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwDEWAQhtIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsGEGHI- 91
Cdd:cd08245   12 LEPEEVPVPEPGPGEVLIKIEACGVCHTDLHAAE-GDWGG--SKYPLVPGHEIVGEVVEVGAGVEGRKVGDRV-GVGWLv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  92 -TCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSFN--LVGEDVL 168
Cdd:cd08245   88 gSCGRCEYCRRGLENLCQKAVNTGYTTQGGYAEYMVADAEYTVLLPDGLPLAQAAPLLCAGITVYSALRDAgpRPGERVA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 169 ITGAGPIGIMAAAIARHVGARNVVITDVNDYRlALARRMGATRAVNVQHENLGDVAAelhmtEGFDVGMEMSGVPSAFAT 248
Cdd:cd08245  168 VLGIGGLGHLAVQYARAMGFETVAITRSPDKR-ELARKLGADEVVDSGAELDEQAAA-----GGADVILVTVVSGAAAEA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 249 MLGHMNHGGKIAMLGIPPS-QMAIDWNQIIFKGLEIKGIY--GRemfetwykmvAMLQSGLDL------TPMItHRFGVD 319
Cdd:cd08245  242 ALGGLRRGGRIVLVGLPESpPFSPDIFPLIMKRQSIAGSThgGR----------ADLQEALDFaaegkvKPMI-ETFPLD 310
                        330
                 ....*....|..
gi 519047159 320 DFQAGFAAMLSG 331
Cdd:cd08245  311 QANEAYERMEKG 322
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
13-339 2.19e-43

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: 153.18  E-value: 2.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIhiWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHIT 92
Cdd:cd08266   15 LEYGDLPEPEPGPDEVLVRVKAAALNHLDL--WVRRGMPGIKLPLPHILGSDGAGVVEAVGPGVTNVKPGQRVVIYPGIS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 CGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFdP--FGNATHTALSFNLV--GEDVL 168
Cdd:cd08266   93 CGRCEYCLAGRENLCAQYGILGEHVDGGYAEYVAVPARNLLPIPDNLSFEEAAAA-PltFLTAWHMLVTRARLrpGETVL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 169 ITGAGP-IGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGVpSAFA 247
Cdd:cd08266  172 VHGAGSgVGSAAIQIAKLFGAT-VIATAGSEDKLERAKELGADYVIDYRKEDFVREVRELTGKRGVDVVVEHVGA-ATWE 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 248 TMLGHMNHGGKIAMLGIPPSQMA-IDWNQIIFKGLEIKGIYG---REMFEtwykMVAMLQSGlDLTPMITHRFGVDDFQA 323
Cdd:cd08266  250 KSLKSLARGGRLVTCGATTGYEApIDLRHVFWRQLSILGSTMgtkAELDE----ALRLVFRG-KLKPVIDSVFPLEEAAE 324
                        330
                 ....*....|....*..
gi 519047159 324 GFAAMLSGNS-GKVVLD 339
Cdd:cd08266  325 AHRRLESREQfGKIVLT 341
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
1-339 6.68e-42

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: 150.38  E-value: 6.68e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALakTERAPG-LAMTDVPVPEVGH-NDVMIRIRQTAICGTDIHIWkwdewaQHTIPvPMQV----GHEYVGEIVALGQ 74
Cdd:cd08283    1 MKAL--VWHGKGdVRVEEVPDPKIEDpTDAIVRVTATAICGSDLHLY------HGYIP-GMKKgdilGHEFMGVVEEVGP 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  75 EVRGLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNS------VGVGVNRPGAF--------------AEYLVIP--AFNA 132
Cdd:cd08283   72 EVRNLKVGDRVVVPFTIACGECFYCKRGLYSQCDNTnpsaemAKLYGHAGAGIfgyshltggyaggqAEYVRVPfaDVGP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 133 FRIPDDIPDEiAAIF--DPFGNATHTALSFNLVGEDVL-ITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGA 209
Cdd:cd08283  152 FKIPDDLSDE-KALFlsDILPTGYHAAELAEVKPGDTVaVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 210 TRAVNvqHENLGDVAAEL-HMTEG------FD-VGMEMSGVPSAFA------------TMLGHMNH----GGKIAMLGIP 265
Cdd:cd08283  231 AETIN--FEEVDDVVEALrELTGGrgpdvcIDaVGMEAHGSPLHKAeqallkletdrpDALREAIQavrkGGTVSIIGVY 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 266 PSQM-AIDWNQIIFKGLEIKG------IYGREMFEtwykmvaMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSG--K 335
Cdd:cd08283  309 GGTVnKFPIGAAMNKGLTLRMgqthvqRYLPRLLE-------LIESGeLDPSFIITHRLPLEDAPEAYKIFDKKEDGciK 381

                 ....
gi 519047159 336 VVLD 339
Cdd:cd08283  382 VVLK 385
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
1-339 7.34e-42

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 149.03  E-value: 7.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:PRK13771   1 MKAVILPGFKQGYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQG---FYPRMKYPVILGHEVVGTVEEVGENVKGFK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF 160
Cdd:PRK13771  78 PGDRVASLLYAPDGTCEYCRSGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVYRGLRR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 161 NLV--GEDVLITGA-GPIGIMAAAIARHVGARNVVITDVNDYRLAL---ARRMGATRAVNVQHENLGDVaaelhmtegfD 234
Cdd:PRK13771 158 AGVkkGETVLVTGAgGGVGIHAIQVAKALGAKVIAVTSSESKAKIVskyADYVIVGSKFSEEVKKIGGA----------D 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 235 VGMEMSGVPSaFATMLGHMNHGGKIAMLG-IPPSQ-MAIDWNQIIFKGLEIKGIYG---REMFETwykmVAMLQSGlDLT 309
Cdd:PRK13771 228 IVIETVGTPT-LEESLRSLNMGGKIIQIGnVDPSPtYSLRLGYIILKDIEIIGHISatkRDVEEA----LKLVAEG-KIK 301
                        330       340       350
                 ....*....|....*....|....*....|.
gi 519047159 310 PMITHRFGVDDFQAGFAAMLSGNS-GKVVLD 339
Cdd:PRK13771 302 PVIGAEVSLSEIDKALEELKDKSRiGKILVK 332
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
1-314 7.42e-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: 7.42e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIW---------KWDEWAQHTIPVPMQVGHEYVGEIVA 71
Cdd:cd08240    1 MKAAAVVEPGKPLEEVEIDTPKPPGTEVLVKVTACGVCHSDLHIWdggydlgggKTMSLDDRGVKLPLVLGHEIVGEVVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  72 LGQEVRGLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFG 151
Cdd:cd08240   81 VGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAATLACSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 152 NATHTALS--FNLVGED-VLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNvqHENLGDVAAELH 228
Cdd:cd08240  161 LTAYSAVKklMPLVADEpVVIIGAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADVVVN--GSDPDAAKRIIK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 229 MTEG-FDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIY-GR--EMFEtwykMVAMLQS 304
Cdd:cd08240  239 AAGGgVDAVIDFVNNSATASLAFDILAKGGKLVLVGLFGGEATLPLPLLPLRALTIQGSYvGSleELRE----LVALAKA 314
                        330
                 ....*....|.
gi 519047159 305 G-LDLTPMITH 314
Cdd:cd08240  315 GkLKPIPLTER 325
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
9-329 3.99e-41

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


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 146.35  E-value: 3.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   9 RAPGLA-MTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSG 87
Cdd:cd08269    2 TGPGRFeVEEHPRPTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  88 EGHitcgfcrncragrrhlcrnsvgvgvnrpGAFAEYLVIPAFNAFRIPDDIPDEiAAIFDPFGNATHTA-LSFNLVGED 166
Cdd:cd08269   82 LSG----------------------------GAFAEYDLADADHAVPLPSLLDGQ-AFPGEPLGCALNVFrRGWIRAGKT 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 167 VLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSG--VPS 244
Cdd:cd08269  133 VAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALARELGATEVVTDDSEAIVERVRELTGGAGADVVIEAVGhqWPL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 245 AFATMLghMNHGGKIAMLGIP---PSQMAI-DWNqiiFKGLEIKGIYGR---EMFETWYKMVAMLQSG-LDLTPMITHRF 316
Cdd:cd08269  213 DLAGEL--VAERGRLVIFGYHqdgPRPVPFqTWN---WKGIDLINAVERdprIGLEGMREAVKLIADGrLDLGSLLTHEF 287
                        330
                 ....*....|...
gi 519047159 317 GVDDFQAGFAAML 329
Cdd:cd08269  288 PLEELGDAFEAAR 300
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
13-338 1.90e-40

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: 145.98  E-value: 1.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEwaqhTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHIT 92
Cdd:cd08281   21 LVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDR----PRPLPMALGHEAAGVVVEVGEGVTDLEVGDHVVLVFVPS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 CGFCRNCRAGRRHLCRNSVGVGVN-----------RPG----------AFAEYLVIPAFNAFRIPDDIPDEIAAIFdpfG 151
Cdd:cd08281   97 CGHCRPCAEGRPALCEPGAAANGAgtllsggrrlrLRGgeinhhlgvsAFAEYAVVSRRSVVKIDKDVPLEIAALF---G 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 152 NATHTALS--FNLV----GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAA 225
Cdd:cd08281  174 CAVLTGVGavVNTAgvrpGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARELGATATVNAGDPNAVEQVR 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 226 ELhMTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLE--IKGIY------GREMfetwYK 297
Cdd:cd08281  254 EL-TGGGVDYAFEMAGSVPALETAYEITRRGGTTVTAGLPDPEARLSVPALSLVAEErtLKGSYmgscvpRRDI----PR 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 519047159 298 MVAMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:cd08281  329 YLALYLSGrLPVDKLLTHRLPLDEINEGFDRLAAGEAVRQVI 370
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
26-285 2.05e-40

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 145.21  E-value: 2.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  26 NDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVAlgQEVRGLAIGDRVSGEGHITCGFCRNCRAGRRH 105
Cdd:PRK09880  28 NGTLVQITRGGICGSDLHYYQEGKVGNFVIKAPMVLGHEVIGKIVH--SDSSGLKEGQTVAINPSKPCGHCKYCLSHNEN 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 106 LCRNSVGVG-------VNrpGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTA-LSFNLVGEDVLITGAGPIGI 177
Cdd:PRK09880 106 QCTTMRFFGsamyfphVD--GGFTRYKVVDTAQCIPYPEKADEKVMAFAEPLAVAIHAAhQAGDLQGKRVFVSGVGPIGC 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 178 MAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAElhmtEG-FDVGMEMSGVPSAFATMLGHMNHG 256
Cdd:PRK09880 184 LIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQNDDLDHYKAE----KGyFDVSFEVSGHPSSINTCLEVTRAK 259
                        250       260       270
                 ....*....|....*....|....*....|....
gi 519047159 257 G---KIAMLGIPPsqmaiDWN--QIIFKGLEIKG 285
Cdd:PRK09880 260 GvmvQVGMGGAPP-----EFPmmTLIVKEISLKG 288
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-339 3.46e-40

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: 143.92  E-value: 3.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPgLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdewaqHTIPVPMQVGHEYVGEIVALGQevRGLa 80
Cdd:cd08242    1 MKALVLDGGLD-LRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYK------GYYPFPGVPGHEFVGIVEEGPE--AEL- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVG-VNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFgnathtALS 159
Cdd:cd08242   71 VGKRVVGEINIACGRCEYCRRGLYTHCPNRTVLGiVDRDGAFAEYLTLPLENLHVVPDLVPDEQAVFAEPL------AAA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 160 FNLV-------GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDyRLALARRMGATRAVNVQHENLGDvaaelhmteG 232
Cdd:cd08242  145 LEILeqvpitpGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSE-KLALARRLGVETVLPDEAESEGG---------G 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 233 FDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKglEIKGIYGR-EMFEtwyKMVAMLQSGL-DLTP 310
Cdd:cd08242  215 FDVVVEATGSPSGLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVN--EITLVGSRcGPFA---PALRLLRKGLvDVDP 289
                        330       340
                 ....*....|....*....|....*....
gi 519047159 311 MITHRFGVDDFQAGFAAMLSGNSGKVVLD 339
Cdd:cd08242  290 LITAVYPLEEALEAFERAAEPGALKVLLR 318
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
1-328 3.25e-39

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: 142.38  E-value: 3.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTER-APGLAmtDVPVPEVGHNDVMIRIRQTAICGTDIHIwKWDEwaqhtIPVP---MQVGHEYVGEIVALGQEV 76
Cdd:cd08285    1 MKAFAMLGIgKVGWI--EKPIPVCGPNDAIVRPTAVAPCTSDVHT-VWGG-----APGErhgMILGHEAVGVVEEVGSEV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  77 RGLAIGDRVSgEGHIT-CGFCRNCRAGRRHLCRNSVG---VGVNRPGAFAEYLVIPA--FNAFRIPDDIPDEIAAIF-DP 149
Cdd:cd08285   73 KDFKPGDRVI-VPAITpDWRSVAAQRGYPSQSGGMLGgwkFSNFKDGVFAEYFHVNDadANLAPLPDGLTDEQAVMLpDM 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 150 FGNATHTALSFNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHenlGDVAAE-L 227
Cdd:cd08285  152 MSTGFHGAELANIkLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDIVDYKN---GDVVEQiL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 228 HMT--EGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLG---------IPPSQMAIDWNQIIFKGLEIKGiyGREMFEtwy 296
Cdd:cd08285  229 KLTggKGVDAVIIAGGGQDTFEQALKVLKPGGTISNVNyygeddylpIPREEWGVGMGHKTINGGLCPG--GRLRME--- 303
                        330       340       350
                 ....*....|....*....|....*....|....
gi 519047159 297 KMVAMLQSG-LDLTPMITHRF-GVDDFQAGFAAM 328
Cdd:cd08285  304 RLASLIEYGrVDPSKLLTHHFfGFDDIEEALMLM 337
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
26-133 6.67e-39

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: 133.89  E-value: 6.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   26 NDVMIRIRQTAICGTDIHIWKWDEWaqhTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHITCGFCRNCRAGRRH 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNP---PVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYN 77
                          90       100
                  ....*....|....*....|....*...
gi 519047159  106 LCRNSVGVGVNRPGAFAEYLVIPAFNAF 133
Cdd:pfam08240  78 LCPNGRFLGYDRDGGFAEYVVVPERNLV 105
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
1-338 1.02e-37

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: 138.79  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPG--LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIwkwdewAQHTIPVPMQV--GHEYVGEIVALGQEV 76
Cdd:cd08278    1 MKTTAAVVREPGgpFVLEDVELDDPRPDEVLVRIVATGICHTDLVV------RDGGLPTPLPAvlGHEGAGVVEAVGSAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  77 RGLAIGDRV-----SgeghitCGFCRNCRAGRRHLCRNSVGV---GVNRPGA--------------------FAEYLVIP 128
Cdd:cd08278   75 TGLKPGDHVvlsfaS------CGECANCLSGHPAYCENFFPLnfsGRRPDGStplslddgtpvhghffgqssFATYAVVH 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 129 AFNAFRIPDDIPDEIAAifdPFGNATHT--ALSFNL----VGEDVLITGAGPIG---IMAAAIArhvGARNVVITDVNDY 199
Cdd:cd08278  149 ERNVVKVDKDVPLELLA---PLGCGIQTgaGAVLNVlkprPGSSIAVFGAGAVGlaaVMAAKIA---GCTTIIAVDIVDS 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 200 RLALARRMGATRAVNVQHENLGDVAAELhMTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPP--SQMAIDWNQII 277
Cdd:cd08278  223 RLELAKELGATHVINPKEEDLVAAIREI-TGGGVDYALDTTGVPAVIEQAVDALAPRGTLALVGAPPpgAEVTLDVNDLL 301
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 519047159 278 FKGLEIKGI-----YGREMFEtwyKMVAMLQSG-LDLTPMITHrFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:cd08278  302 VSGKTIRGViegdsVPQEFIP---RLIELYRQGkFPFDKLVTF-YPFEDINQAIADSESGKVIKPVL 364
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
13-338 1.99e-37

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 137.66  E-value: 1.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGH-NDVMIRIRQTAICGTDI-HIWkwdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGH 90
Cdd:PRK10309  12 VRVAESPIPEIKHqDDVLVKVASSGLCGSDIpRIF-----KNGAHYYPITLGHEFSGYVEAVGSGVDDLHPGDAVACVPL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  91 ITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHtalSFNLV----GED 166
Cdd:PRK10309  87 LPCFTCPECLRGFYSLCAKYDFIGSRRDGGNAEYIVVKRKNLFALPTDMPIEDGAFIEPITVGLH---AFHLAqgceGKN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 167 VLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGVPSAF 246
Cdd:PRK10309 164 VIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAMQTFNSREMSAPQIQSVLRELRFDQLILETAGVPQTV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 247 ATMLGHMNHGGKIAMLGIPPSQMAID---WNQIIFKGLEIKGIY--------GREmFETWYKMVAmlQSGLDLTPMITHR 315
Cdd:PRK10309 244 ELAIEIAGPRAQLALVGTLHHDLHLTsatFGKILRKELTVIGSWmnysspwpGQE-WETASRLLT--ERKLSLEPLIAHR 320
                        330       340
                 ....*....|....*....|....*
gi 519047159 316 FGVDDFQAGFAAmLSGNS--GKVVL 338
Cdd:PRK10309 321 GSFESFAQAVRD-LAGNPmpGKVLL 344
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
1-210 2.65e-37

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: 137.72  E-value: 2.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAktERAPG-LAMTDVPVPEVGH-NDVMIRIRQTAICGTDIHIWKwdewaQHT-IPVPMQVGHEYVGEIVALGQEVR 77
Cdd:cd08282    1 MKAVV--YGGPGnVAVEDVPDPKIEHpTDAIVRITTTAICGSDLHMYR-----GRTgAEPGLVLGHEAMGEVEEVGSAVE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  78 GLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNsvgVGVNRPGAF-------------AEYLVIP--AFNAFRIPDDIPDE 142
Cdd:cd08282   74 SLKVGDRVVVPFNVACGRCRNCKRGLTGVCLT---VNPGRAGGAygyvdmgpygggqAEYLRVPyaDFNLLKLPDRDGAK 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519047159 143 IAAIF----DPFGNATH-TALSFNLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGAT 210
Cdd:cd08282  151 EKDDYlmlsDIFPTGWHgLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAESIGAI 223
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
3-338 4.29e-37

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: 137.19  E-value: 4.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   3 ALAKTERAPgLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDewaqHTIPVPMQVGHEYVGEIVALGQEVRGLAIG 82
Cdd:cd05279    4 AVLWEKGKP-LSIEEIEVAPPKAGEVRIKVVATGVCHTDLHVIDGK----LPTPLPVILGHEGAGIVESIGPGVTTLKPG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  83 DRVSGEGHITCGFCRNCRAGRRHLC---RNSVGVGVNRPG------------------AFAEYLVIPAFNAFRIPDDIPD 141
Cdd:cd05279   79 DKVIPLFGPQCGKCKQCLNPRPNLCsksRGTNGRGLMSDGtsrftckgkpihhflgtsTFAEYTVVSEISLAKIDPDAPL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 142 EIAAIF-----DPFGNATHTALSfnLVGEDVLITGAGPIG---IMAAAIArhvGARNVVITDVNDYRLALARRMGATRAV 213
Cdd:cd05279  159 EKVCLIgcgfsTGYGAAVNTAKV--TPGSTCAVFGLGGVGlsvIMGCKAA---GASRIIAVDINKDKFEKAKQLGATECI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 214 NVQHENLGDVAAELHMTE-GFDVGMEMSGVPSAFATMLG--HMNhGGKIAMLGIPPS--QMAIDWNqIIFKGLEIKGIYg 288
Cdd:cd05279  234 NPRDQDKPIVEVLTEMTDgGVDYAFEVIGSADTLKQALDatRLG-GGTSVVVGVPPSgtEATLDPN-DLLTGRTIKGTV- 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519047159 289 remFETWY------KMVAMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:cd05279  311 ---FGGWKskdsvpKLVALYRQKkFPLDELITHVLPFEEINDGFDLMRSGESIRTIL 364
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
1-331 1.76e-36

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: 134.68  E-value: 1.76e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIwkwDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLA 80
Cdd:cd08296    1 YKAVQVTEPGGPLELVERDVPLPGPGEVLIKVEACGVCHSDAFV---KEGAMPGLSYPRVPGHEVVGRIDAVGEGVSRWK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVSGE---GHitCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTA 157
Cdd:cd08296   78 VGDRVGVGwhgGH--CGTCDACRRGDFVHCENGKVTGVTRDGGYAEYMLAPAEALARIPDDLDAAEAAPLLCAGVTTFNA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 158 L--SFNLVGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRlALARRMGATRAVNVQHEnlgDVAAELHMTEGFDV 235
Cdd:cd08296  156 LrnSGAKPGDLVAVQGIGGLGHLAVQYAAKMGFRTVAISRGSDKA-DLARKLGAHHYIDTSKE---DVAEALQELGGAKL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 236 GMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGiygremfetWYKMVAM-----LQ-SGL-DL 308
Cdd:cd08296  232 ILATAPNAKAISALVGGLAPRGKLLILGAAGEPVAVSPLQLIMGRKSIHG---------WPSGTALdsedtLKfSALhGV 302
                        330       340
                 ....*....|....*....|...
gi 519047159 309 TPMItHRFGVDDFQAGFAAMLSG 331
Cdd:cd08296  303 RPMV-ETFPLEKANEAYDRMMSG 324
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
1-213 4.40e-34

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: 128.07  E-value: 4.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKAL-----AKTERAPgLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwDEWAQHTIP-VPmqvGHEYVGEIVALGQ 74
Cdd:cd08298    1 MKAMvlekpGPIEENP-LRLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVE-GDLPPPKLPlIP---GHEIVGRVEAVGP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  75 EVRGLAIGDRVsgeG----HITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAifdPF 150
Cdd:cd08298   76 GVTRFSVGDRV---GvpwlGSTCGECRYCRSGRENLCDNARFTGYTVDGGYAEYMVADERFAYPIPEDYDDEEAA---PL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 519047159 151 GNATHTAL-SFNLV----GEDVLITGAGPIGIMAAAIARHVGARNVVITDvNDYRLALARRMGATRAV 213
Cdd:cd08298  150 LCAGIIGYrALKLAglkpGQRLGLYGFGASAHLALQIARYQGAEVFAFTR-SGEHQELARELGADWAG 216
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
16-285 2.58e-33

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: 126.07  E-value: 2.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  16 TDVPVPEVGHNDVMIRIRQTAICGTDIHiWKWDEWAQhtIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsGEGHI--TC 93
Cdd:cd05283   15 FTFERRPLGPDDVDIKITYCGVCHSDLH-TLRNEWGP--TKYPLVPGHEIVGIVVAVGSKVTKFKVGDRV-GVGCQvdSC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  94 GFCRNCRAGRRHLCRNSVGVGVNRP-------GAFAEYLVIPAFNAFRIPDDIPDEIAAifdPF---GNATHTALSFNLV 163
Cdd:cd05283   91 GTCEQCKSGEEQYCPKGVVTYNGKYpdgtitqGGYADHIVVDERFVFKIPEGLDSAAAA---PLlcaGITVYSPLKRNGV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 164 --GEDVLITGAGPIGIMAAAIARHVGARNVVITdVNDYRLALARRMGATRAVNvqHENLGDVAAElhmTEGFDVGMEMSG 241
Cdd:cd05283  168 gpGKRVGVVGIGGLGHLAVKFAKALGAEVTAFS-RSPSKKEDALKLGADEFIA--TKDPEAMKKA---AGSLDLIIDTVS 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 519047159 242 VPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKG 285
Cdd:cd05283  242 ASHDLDPYLSLLKPGGTLVLVGAPEEPLPVPPFPLIFGRKSVAG 285
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
1-339 7.00e-33

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: 124.62  E-value: 7.00e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPG--LAMTDVPVPEVGHNDVMIRIRQTAICGTDihiWKWDEWAQHTIPVPMQVGH-EYVGEIVALGQEVR 77
Cdd:cd08253    1 MRAIRYHEFGAPdvLRLGDLPVPTPGPGEVLVRVHASGVNPVD---TYIRAGAYPGLPPLPYVPGsDGAGVVEAVGEGVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  78 GLAIGDRVsgeghitcgFCRNCRAGRRHlcrnsvgvgvnrpGAFAEYLVIPAFNAFRIPDDIPDEI-AAIFDPFGNATHT 156
Cdd:cd08253   78 GLKVGDRV---------WLTNLGWGRRQ-------------GTAAEYVVVPADQLVPLPDGVSFEQgAALGIPALTAYRA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 157 ALSFN--LVGEDVLITG-AGPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGF 233
Cdd:cd08253  136 LFHRAgaKAGETVLVHGgSGAVGHAAVQLARWAGAR-VIATASSAEGAELVRQAGADAVFNYRAEDLADRILAATAGQGV 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 234 DVGMEMSGVPSaFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGREM-FETWYKMVAMLQSGL---DLT 309
Cdd:cd08253  215 DVIIEVLANVN-LAKDLDVLAPGGRIVVYGSGGLRGTIPINPLMAKEASIRGVLLYTAtPEERAAAAEAIAAGLadgALR 293
                        330       340       350
                 ....*....|....*....|....*....|.
gi 519047159 310 PMITHRFGVDDF-QAGFAAMLSGNSGKVVLD 339
Cdd:cd08253  294 PVIAREYPLEEAaAAHEAVESGGAIGKVVLD 324
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
1-340 3.55e-32

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: 123.48  E-value: 3.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdewAQHTIPVP----MQVGHEYVGEIVALGqEV 76
Cdd:cd08230    1 MKAIAVKPGKPGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDREIVA----GEYGTAPPgedfLVLGHEALGVVEEVG-DG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  77 RGLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGV--GVN-RPGAFAEYLVIPAFNAFRIPDDIPDeIAAIFDPFGNA 153
Cdd:cd08230   76 SGLSPGDLVVPTVRRPPGKCLNCRIGRPDFCETGEYTerGIKgLHGFMREYFVDDPEYLVKVPPSLAD-VGVLLEPLSVV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 154 THTALSFNLVGE--------DVLITGAGPIGIMAAAIARHVGARNVVI--TDVNDYRLALARRMGATRaVNVQHENLGDV 223
Cdd:cd08230  155 EKAIEQAEAVQKrlptwnprRALVLGAGPIGLLAALLLRLRGFEVYVLnrRDPPDPKADIVEELGATY-VNSSKTPVAEV 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 224 AAelhmTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQ--MAIDW----------NQIIFkGLeIKGiyGREM 291
Cdd:cd08230  234 KL----VGEFDLIIEATGVPPLAFEALPALAPNGVVILFGVPGGGreFEVDGgelnrdlvlgNKALV-GS-VNA--NKRH 305
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 519047159 292 FETwykMVAMLQSGLDLTP-----MITHRFGVDDFQAGFAAMLSGNSgKVVLDW 340
Cdd:cd08230  306 FEQ---AVEDLAQWKYRWPgvlerLITRRVPLEEFAEALTEKPDGEI-KVVIEW 355
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
1-339 3.98e-32

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: 122.61  E-value: 3.98e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAP--GLAMTDV-PVPEVGHnDVMIRIRQTAICGTDIHIwKWDEWaQHTIPVPMQVGHEYVGEIVALGQEVR 77
Cdd:cd08241    1 MKAVVCKELGGpeDLVLEEVpPEPGAPG-EVRIRVEAAGVNFPDLLM-IQGKY-QVKPPLPFVPGSEVAGVVEAVGEGVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  78 GLAIGDRVsgeghitcgfcrncragrrhlcrnsvgVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAifdPFGNATHTA 157
Cdd:cd08241   78 GFKVGDRV---------------------------VALTGQGGFAEEVVVPAAAVFPLPDGLSFEEAA---ALPVTYGTA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 158 LsFNLV-------GEDVLITGA-GPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHM 229
Cdd:cd08241  128 Y-HALVrrarlqpGETVLVLGAaGGVGLAAVQLAKALGAR-VIAAASSEEKLALARALGADHVIDYRDPDLRERVKALTG 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 230 TEGFDVGMEMSGVPsAFATMLGHMNHGGKIAMLG-----IPpsqmAIDWNQIIFKGLEIKGIYGREMF--------ETWY 296
Cdd:cd08241  206 GRGVDVVYDPVGGD-VFEASLRSLAWGGRLLVIGfasgeIP----QIPANLLLLKNISVVGVYWGAYArrepellrANLA 280
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 519047159 297 KMVAMLQSGLdLTPMITHRFGVDDFQAGFAAMLSGNS-GKVVLD 339
Cdd:cd08241  281 ELFDLLAEGK-IRPHVSAVFPLEQAAEALRALADRKAtGKVVLT 323
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-340 3.39e-31

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: 120.33  E-value: 3.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKA--LAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIwkwdewAQHTIPVPMQVGH----EYVGEIVALGQ 74
Cdd:cd08276    1 MKAwrLSGGGGLDNLKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLI------LNGRYPPPVKDPLiplsDGAGEVVAVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  75 EVRGLAIGDRVsgeghiTCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFdPFgnAT 154
Cdd:cd08276   75 GVTRFKVGDRV------VPTFFPNWLDGPPTAEDEASALGGPIDGVLAEYVVLPEEGLVRAPDHLSFEEAATL-PC--AG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 155 HTALS--FNLV----GEDVLITGAGPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVN-VQHENLGDVAAEL 227
Cdd:cd08276  146 LTAWNalFGLGplkpGDTVLVQGTGGVSLFALQFAKAAGAR-VIATSSSDEKLERAKALGADHVINyRTTPDWGEEVLKL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 228 HMTEGFDVGMEMSGvPSAFATMLGHMNHGGKIAMLG-IPPSQMAIDWNQIIFKGLEIKGIY--GREMFETwykMVAMLQS 304
Cdd:cd08276  225 TGGRGVDHVVEVGG-PGTLAQSIKAVAPGGVISLIGfLSGFEAPVLLLPLLTKGATLRGIAvgSRAQFEA---MNRAIEA 300
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 519047159 305 gLDLTPMITHRFGVDDFQAGFAAMLSGNS-GKVVLDW 340
Cdd:cd08276  301 -HRIRPVIDRVFPFEEAKEAYRYLESGSHfGKVVIRV 336
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
3-338 7.18e-31

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: 120.14  E-value: 7.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   3 ALAKTERAPgLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIG 82
Cdd:cd08277    6 AVAWEAGKP-LVIEEIEVAPPKANEVRIKMLATSVCHTDILAIE----GFKATLFPVILGHEGAGIVESVGEGVTNLKPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  83 DRVSGEGHITCGFCRNCRAGRRHLCR----NSVGV---GVNRP-------------GAFAEYLVIPAFNAFRIPDDIPDE 142
Cdd:cd08277   81 DKVIPLFIGQCGECSNCRSGKTNLCQkyraNESGLmpdGTSRFtckgkkiyhflgtSTFSQYTVVDENYVAKIDPAAPLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 143 IA-----AIFDPFGNATHTALsfnlV--GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNV 215
Cdd:cd08277  161 HVcllgcGFSTGYGAAWNTAK----VepGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGATDFINP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 216 QH--ENLGDVAAElhMTE-GFDVGMEMSGVPSAF-----ATMLGHmnhgGKIAMLGIPPSQ-MAIDWNQII----FKGLE 282
Cdd:cd08277  237 KDsdKPVSEVIRE--MTGgGVDYSFECTGNADLMnealeSTKLGW----GVSVVVGVPPGAeLSIRPFQLIlgrtWKGSF 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519047159 283 IKGIYGREMFEtwyKMVAMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:cd08277  311 FGGFKSRSDVP---KLVSKYMNKkFDLDELITHVLPFEEINKGFDLMKSGECIRTVI 364
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
56-338 2.18e-30

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: 116.99  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  56 PVPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeghitcgFCrncragrrhlcrnsvgvgvnrPGAFAEYLVIPAFNAFRI 135
Cdd:cd08255   19 PLPLPPGYSSVGRVVEVGSGVTGFKPGDRV---------FC---------------------FGPHAERVVVPANLLVPL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 136 PDDIPDEIAAIFDPFGNATHTALSFNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVN 214
Cdd:cd08255   69 PDGLPPERAALTALAATALNGVRDAEPrLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALGPADPVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 215 vqhenlgDVAAELHMTEGFDVGMEMSGVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIK----GIYGRE 290
Cdd:cd08255  149 -------ADTADEIGGRGADVVIEASGSPSALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKRLPIRssqvYGIGRY 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 519047159 291 MFETWYKMVAMLQSGLDL------TPMITHRFGVDDFQAGFAAMLSGNSG--KVVL 338
Cdd:cd08255  222 DRPRRWTEARNLEEALDLlaegrlEALITHRVPFEDAPEAYRLLFEDPPEclKVVL 277
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
1-341 6.80e-30

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 117.06  E-value: 6.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDeWAQHTIPVpmqVGHEYVGEIVALGQEVRGLA 80
Cdd:PRK09422   1 MKAAVVNKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANGD-FGDKTGRI---LGHEGIGIVKEVGPGVTSLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  81 IGDRVS----GEGhitCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHT 156
Cdd:PRK09422  77 VGDRVSiawfFEG---CGHCEYCTTGRETLCRSVKNAGYTVDGGMAEQCIVTADYAVKVPEGLDPAQASSITCAGVTTYK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 157 ALSFNLV--GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNvqHENLGDVAAELHMTEGFD 234
Cdd:PRK09422 154 AIKVSGIkpGQWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADLTIN--SKRVEDVAKIIQEKTGGA 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 235 VGMEMSGVP-SAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKG--IYGREMFETWYKMVAMlqsGLdLTPM 311
Cdd:PRK09422 232 HAAVVTAVAkAAFNQAVDAVRAGGRVVAVGLPPESMDLSIPRLVLDGIEVVGslVGTRQDLEEAFQFGAE---GK-VVPK 307
                        330       340       350
                 ....*....|....*....|....*....|.
gi 519047159 312 ITHRfGVDDFQAGFAAMLSGN-SGKVVLDWT 341
Cdd:PRK09422 308 VQLR-PLEDINDIFDEMEQGKiQGRMVIDFT 337
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
1-338 2.74e-29

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: 114.58  E-value: 2.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTER--APGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRG 78
Cdd:cd05289    1 MKAVRIHEYggPEVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPLTLPLIPGHDVAGVVVAVGPGVTG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  79 LAIGDRVsgeghitcgFCRncragrrhlcrnsvgVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAifdPFGNATHTAL 158
Cdd:cd05289   81 FKVGDEV---------FGM---------------TPFTRGGAYAEYVVVPADELALKPANLSFEEAA---ALPLAGLTAW 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 -SFNLVGED-----VLITGA-GPIGIMAAAIARHVGARnvVITDVNDYRLALARRMGATRAVNVQHENLGDVAAElhmtE 231
Cdd:cd05289  134 qALFELGGLkagqtVLIHGAaGGVGSFAVQLAKARGAR--VIATASAANADFLRSLGADEVIDYTKGDFERAAAP----G 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 232 GFDVGMEMSGvPSAFATMLGHMNHGGKIamlgIPPSQMAIDWNQIIFKGLEIKGIYGREMFETWYKMVAMLQSGLdLTPM 311
Cdd:cd05289  208 GVDAVLDTVG-GETLARSLALVKPGGRL----VSIAGPPPAEQAAKRRGVRAGFVFVEPDGEQLAELAELVEAGK-LRPV 281
                        330       340
                 ....*....|....*....|....*...
gi 519047159 312 ITHRFGVDDFQAGFAAMLSGNS-GKVVL 338
Cdd:cd05289  282 VDRVFPLEDAAEAHERLESGHArGKVVL 309
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
17-328 6.37e-29

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: 114.33  E-value: 6.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  17 DVPVPEVGH-NDVMIRIRQTAICGTDIHIWKWDEWAQHtipvPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHITCGF 95
Cdd:cd08287   16 EVPDPVIEEpTDAVIRVVATCVCGSDLWPYRGVSPTRA----PAPIGHEFVGVVEEVGSEVTSVKPGDFVIAPFAISDGT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  96 CRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPafNA----FRIPD---DIPDEIAAIF---DPFGNATHTALSFNL-VG 164
Cdd:cd08287   92 CPFCRAGFTTSCVHGGFWGAFVDGGQGEYVRVP--LAdgtlVKVPGspsDDEDLLPSLLalsDVMGTGHHAAVSAGVrPG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 165 EDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVnvqhENLGD--VAAELHMTEGF--DVGMEMS 240
Cdd:cd08287  170 STVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAREFGATDIV----AERGEeaVARVRELTGGVgaDAVLECV 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 241 GVPSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKG------IYGREMFEtwykmvAMLQSGLDLTPMITH 314
Cdd:cd08287  246 GTQESMEQAIAIARPGGRVGYVGVPHGGVELDVRELFFRNVGLAGgpapvrRYLPELLD------DVLAGRINPGRVFDL 319
                        330
                 ....*....|....
gi 519047159 315 RFGVDDFQAGFAAM 328
Cdd:cd08287  320 TLPLDEVAEGYRAM 333
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
174-304 9.71e-29

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 108.08  E-value: 9.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  174 PIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGVPSAFATMLGHM 253
Cdd:pfam00107   1 GVGLAAIQLAKAAGAK-VIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGSPATLEQALKLL 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 519047159  254 NHGGKIAMLGIPPSQMAIDWNQIIFKGLEIKGIYGReMFETWYKMVAMLQS 304
Cdd:pfam00107  80 RPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLG-SPEEFPEALDLLAS 129
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
1-288 1.40e-28

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: 113.22  E-value: 1.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERA-PGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHiwkwdewaqhTI------PVPMQVGHEYVGEIVALG 73
Cdd:cd08264    1 MKALVFEKSGiENLKVEDVKDPKPGPGEVLIRVKMAGVNPVDYN----------VInavkvkPMPHIPGAEFAGVVEEVG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  74 QEVRGLAIGDRVSGEGHITCGFCRNCRAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFdPFGNA 153
Cdd:cd08264   71 DHVKGVKKGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGIIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASL-PVAAL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 154 T--HTALSFNL-VGEDVLITGA-GPIGIMAAAIARHVGARNVVITDVNDyrlalARRMGATRAVNvqHENLGDVAAELhm 229
Cdd:cd08264  150 TayHALKTAGLgPGETVVVFGAsGNTGIFAVQLAKMMGAEVIAVSRKDW-----LKEFGADEVVD--YDEVEEKVKEI-- 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 230 TEGFDVGMEMSGvPSAFATMLGHMNHGGKIAMLGI-PPSQMAIDWNQIIFKGLEIKGIYG 288
Cdd:cd08264  221 TKMADVVINSLG-SSFWDLSLSVLGRGGRLVTFGTlTGGEVKLDLSDLYSKQISIIGSTG 279
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-338 1.80e-25

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: 104.61  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  16 TDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGeghitcgf 95
Cdd:cd08267   17 VEVPIPTPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLGRPFPPIPGMDFAGEVVAVGSGVTRFKVGDEVFG-------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  96 crncragrrhlcrnsvGVGVNRPGAFAEYLVIPAFNAFRIPDDI-PDEIAAIfdpfGNATHTALSFnLV-------GEDV 167
Cdd:cd08267   89 ----------------RLPPKGGGALAEYVVAPESGLAKKPEGVsFEEAAAL----PVAGLTALQA-LRdagkvkpGQRV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 168 LITGA-GPIGIMAAAIARHVGARNVVIT-DVNdyrLALARRMGATRAVNVQHEnlgDVAAELHMTEGFDVGMEMSG-VPS 244
Cdd:cd08267  148 LINGAsGGVGTFAVQIAKALGAHVTGVCsTRN---AELVRSLGADEVIDYTTE---DFVALTAGGEKYDVIFDAVGnSPF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 245 AFATMLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGL----EIKGIYGREMFETWYKMVAMLQSGlDLTPMITHRFGVDD 320
Cdd:cd08267  222 SLYRASLALKPGGRYVSVGGGPSGLLLVLLLLPLTLGgggrRLKFFLAKPNAEDLEQLAELVEEG-KLKPVIDSVYPLED 300
                        330
                 ....*....|....*....
gi 519047159 321 FQAGFAAMLSGNS-GKVVL 338
Cdd:cd08267  301 APEAYRRLKSGRArGKVVI 319
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
1-338 3.08e-23

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: 98.28  E-value: 3.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALakTERAPG----LAMTDVPVPEVGHNDVMIRIRQTAICGTDIhiwkwdewAQ---------HTIPVPmqvGHEYVG 67
Cdd:cd05276    1 MKAI--VIKEPGgpevLELGEVPKPAPGPGEVLIRVAAAGVNRADL--------LQrqglyppppGASDIL---GLEVAG 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  68 EIVALGQEVRGLAIGDRVsgeghitCGFCrncrAGrrhlcrnsvgvgvnrpGAFAEYLVIPAFNAFRIPDDIPDEIAA-- 145
Cdd:cd05276   68 VVVAVGPGVTGWKVGDRV-------CALL----AG----------------GGYAEYVVVPAGQLLPVPEGLSLVEAAal 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 146 ---IFDPFGNATHTAlsfNL-VGEDVLIT-GAGPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENL 220
Cdd:cd05276  121 pevFFTAWQNLFQLG---GLkAGETVLIHgGASGVGTAAIQLAKALGAR-VIATAGSEEKLEACRALGADVAINYRTEDF 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 221 GDVAAELHMTEGFDVGMEMSGvPSAFATMLGHMNHGGKIAMLGIppsqMA-----IDWNQIIFKGLEIKG--------IY 287
Cdd:cd05276  197 AEEVKEATGGRGVDVILDMVG-GDYLARNLRALAPDGRLVLIGL----LGgakaeLDLAPLLRKRLTLTGstlrsrslEE 271
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 519047159 288 GREMF-ETWYKMVAMLQSGLdLTPMITHRFGVDDFQAGFAAMLSG-NSGKVVL 338
Cdd:cd05276  272 KAALAaAFREHVWPLFASGR-IRPVIDKVFPLEEAAEAHRRMESNeHIGKIVL 323
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
16-338 2.86e-22

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 96.21  E-value: 2.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  16 TDVPVPEVGHNDVMIRIRQTAICGTDIHI---W--------------KWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRG 78
Cdd:cd08274   19 DDVPVPTPAPGEVLIRVGACGVNNTDINTregWystevdgatdstgaGEAGWWGGTLSFPRIQGADIVGRVVAVGEGVDT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  79 LAIGDRVsgeghitcgFCRNC-RAGRRHLCRNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPD-EIAAIFDPFGNATHT 156
Cdd:cd08274   99 ARIGERV---------LVDPSiRDPPEDDPADIDYIGSERDGGFAEYTVVPAENAYPVNSPLSDvELATFPCSYSTAENM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 157 ALSFNLV-GEDVLITGA-GPIGIMAAAIARHVGARnvVITDVNDYRLALARRMGATRAVNvqHENLGDVAAELHMTEGFD 234
Cdd:cd08274  170 LERAGVGaGETVLVTGAsGGVGSALVQLAKRRGAI--VIAVAGAAKEEAVRALGADTVIL--RDAPLLADAKALGGEPVD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 235 VGMEMSGVPsAFATMLGHMNHGGKIAMLGIPPSQMA-IDWNQIIFKGLEIKGI--YGREMFEtwyKMVAMLQSGLdLTPM 311
Cdd:cd08274  246 VVADVVGGP-LFPDLLRLLRPGGRYVTAGAIAGPVVeLDLRTLYLKDLTLFGStlGTREVFR---RLVRYIEEGE-IRPV 320
                        330       340       350
                 ....*....|....*....|....*....|
gi 519047159 312 ITHRFGVDDF---QAGFAAmlSGNSGKVVL 338
Cdd:cd08274  321 VAKTFPLSEIreaQAEFLE--KRHVGKLVL 348
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
13-339 5.93e-22

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: 94.65  E-value: 5.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIhiwkwdeWA-----QHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsg 87
Cdd:cd05282   14 LELVSLPIPPPGPGEVLVRMLAAPINPSDL-------ITisgayGSRPPLPAVPGNEGVGVVVEVGSGVSGLLVGQRV-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  88 eghitcgfcrncragrrhlcrnsVGVGVNrpGAFAEYLVIPAFNAFRIPDDIPDEIAAIF--DPFgnathTALSF----- 160
Cdd:cd05282   85 -----------------------LPLGGE--GTWQEYVVAPADDLIPVPDSISDEQAAMLyiNPL-----TAWLMlteyl 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 161 -NLVGEDVLITGAGP-IGIMAAAIARHVGAR--NVVITDVNDYRLalaRRMGATRAVNVQHENLGDVAAELHMTEGFDVG 236
Cdd:cd05282  135 kLPPGDWVIQNAANSaVGRMLIQLAKLLGFKtiNVVRRDEQVEEL---KALGADEVIDSSPEDLAQRVKEATGGAGARLA 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 237 MEMSGVPSAfATMLGHMNHGGKI----AMLGIPPSqmaIDWNQIIFKGLEIKGIYGREMFETWYK---------MVAMLQ 303
Cdd:cd05282  212 LDAVGGESA-TRLARSLRPGGTLvnygLLSGEPVP---FPRSVFIFKDITVRGFWLRQWLHSATKeakqetfaeVIKLVE 287
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 519047159 304 SGlDLTPMITHRFGVDDFQAGFAAMLS-GNSGKVVLD 339
Cdd:cd05282  288 AG-VLTTPVGAKFPLEDFEEAVAAAEQpGRGGKVLLT 323
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
1-194 6.09e-22

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: 94.96  E-value: 6.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKAL-AKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWaqhtIPVPMQVGHEYVGEIVALGQEVRGL 79
Cdd:cd08249    1 QKAAvLTGPGGGLLVVVDVPVPKPGPDEVLVKVKAVALNPVDWKHQDYGFI----PSYPAILGCDFAGTVVEVGSGVTRF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVsgeghitCGFCRNCRAGRrhlcrnsvgvgvNRPGAFAEYLVIPAFNAFRIPDDIPDEIAA------------IF 147
Cdd:cd08249   77 KVGDRV-------AGFVHGGNPND------------PRNGAFQEYVVADADLTAKIPDNISFEEAAtlpvglvtaalaLF 137
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 519047159 148 DPFG-NATHTALSFNLVGEDVLITGAG-PIGIMAAAIARHVGARnvVIT 194
Cdd:cd08249  138 QKLGlPLPPPKPSPASKGKPVLIWGGSsSVGTLAIQLAKLAGYK--VIT 184
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
13-235 2.08e-21

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: 93.27  E-value: 2.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVmiRIRQTAIcGT---DIHIWKwdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeg 89
Cdd:cd05286   14 LEYEDVPVPEPGPGEV--LVRNTAI-GVnfiDTYFRS----GLYPLPLPFVLGVEGAGVVEAVGPGVTGFKVGDRV---- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  90 hitcGFCrncragrrhlcrnsvgvgvNRPGAFAEYLVIPAFNAFRIPDDIPDEIAA--IFDpfGNATHTAL--SFNL-VG 164
Cdd:cd05286   83 ----AYA-------------------GPPGAYAEYRVVPASRLVKLPDGISDETAAalLLQ--GLTAHYLLreTYPVkPG 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519047159 165 EDVLITG-AGPIGIMAAAIARHVGARnvVITDV-NDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDV 235
Cdd:cd05286  138 DTVLVHAaAGGVGLLLTQWAKALGAT--VIGTVsSEEKAELARAAGADHVINYRDEDFVERVREITGGRGVDV 208
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
13-339 1.68e-20

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: 91.20  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdewAQHTIPV-PMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGHI 91
Cdd:cd08301   15 LVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWE----AKGQTPLfPRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  92 TCGFCRNCRAGRRHLC---RNSVGVGVNRPG-------------------AFAEYLVIPAFNAFRIPDDIPDEIAAIFDp 149
Cdd:cd08301   91 ECKECRHCKSEKSNMCdllRINTDRGVMINDgksrfsingkpiyhfvgtsTFSEYTVVHVGCVAKINPEAPLDKVCLLS- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 150 FGNATHTALSFNLV----GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQ--HENLGDV 223
Cdd:cd08301  170 CGVSTGLGAAWNVAkvkkGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKFGVTEFVNPKdhDKPVQEV 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 224 AAElhMTE-GFDVGMEMSGVPSAFATMLGHMNHG-GKIAMLGIPPSQMAIDWNQI-IFKGLEIKG-IYGRemfetwYK-- 297
Cdd:cd08301  250 IAE--MTGgGVDYSFECTGNIDAMISAFECVHDGwGVTVLLGVPHKDAVFSTHPMnLLNGRTLKGtLFGG------YKpk 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 519047159 298 -----MVAM-LQSGLDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVLD 339
Cdd:cd08301  322 tdlpnLVEKyMKKELELEKFITHELPFSEINKAFDLLLKGECLRCILH 369
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
13-339 2.05e-20

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: 91.22  E-value: 2.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPV-PEVGHnDVMIRIRQTAICGTDIHIWKwdewAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeghI 91
Cdd:cd08299   20 FSIEEIEVaPPKAH-EVRIKIVATGICRSDDHVVS----GKLVTPFPVILGHEAAGIVESVGEGVTTVKPGDKV-----I 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  92 T-----CGFCRNCRAGRRHLC-RNSVGV-------GVNR-------------PGAFAEYLVIPAFNAFRIPDDIPDE--- 142
Cdd:cd08299   90 PlfvpqCGKCRACLNPESNLClKNDLGKpqglmqdGTSRftckgkpihhflgTSTFSEYTVVDEIAVAKIDAAAPLEkvc 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 143 -IAAIFDP-FGNATHTAlsfnLV--GEDVLITGAGPIG---IMAAAIArhvGARNVVITDVNDYRLALARRMGATRAVNV 215
Cdd:cd08299  170 lIGCGFSTgYGAAVNTA----KVtpGSTCAVFGLGGVGlsaIMGCKAA---GASRIIAVDINKDKFAKAKELGATECINP 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 216 Q--HENLGDVAAElhMT-EGFDVGMEMSGVPSAFATMLG--HMNHGGKIaMLGIPPS--QMAIDwNQIIFKGLEIKGIY- 287
Cdd:cd08299  243 QdyKKPIQEVLTE--MTdGGVDFSFEVIGRLDTMKAALAscHEGYGVSV-IVGVPPSsqNLSIN-PMLLLTGRTWKGAVf 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 519047159 288 -GREMFETWYKMVA-MLQSGLDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVLD 339
Cdd:cd08299  319 gGWKSKDSVPKLVAdYMAKKFNLDPLITHTLPFEKINEGFDLLRSGKSIRTVLT 372
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-339 7.07e-20

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 88.77  E-value: 7.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTER--APGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHtiPVPMQVGHEYVGEIVALGQEVRG 78
Cdd:cd08272    1 MKALVLESFggPEVFELREVPRPQPGPGQVLVRVHASGVNPLDTKIRRGGAAARP--PLPAILGCDVAGVVEAVGEGVTR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  79 LAIGDRVSGeghitcgfcrncragrrhlCRNSVGvgvNRPGAFAEYLVIPAFNAFRIPDDIP-DEIAAIFDPFGNA---- 153
Cdd:cd08272   79 FRVGDEVYG-------------------CAGGLG---GLQGSLAEYAVVDARLLALKPANLSmREAAALPLVGITAwegl 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 154 -THTALSfnlVGEDVLI-TGAGPIGIMAAAIARHVGARnvVITDVNDYRLALARRMGATRAVNVQhENLGDVAAELHMTE 231
Cdd:cd08272  137 vDRAAVQ---AGQTVLIhGGAGGVGHVAVQLAKAAGAR--VYATASSEKAAFARSLGADPIIYYR-ETVVEYVAEHTGGR 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 232 GFDV------GMEMSGVPSAfATMLGHMnhggkIAMLGIPPsqmaIDWNQIIFKGLEIKGIY---------GREMF-ETW 295
Cdd:cd08272  211 GFDVvfdtvgGETLDASFEA-VALYGRV-----VSILGGAT----HDLAPLSFRNATYSGVFtllplltgeGRAHHgEIL 280
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 519047159 296 YKMVAMLQSGLdLTPMI-THRFGVDDFQAGFAAMLSGNS-GKVVLD 339
Cdd:cd08272  281 REAARLVERGQ-LRPLLdPRTFPLEEAAAAHARLESGSArGKIVID 325
PLN02740 PLN02740
Alcohol dehydrogenase-like
5-338 3.71e-19

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 87.54  E-value: 3.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   5 AKTERAPG--LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMqvGHEYVGEIVALGQEVRGLAIG 82
Cdd:PLN02740  13 AAVAWGPGepLVMEEIRVDPPQKMEVRIKILYTSICHTDLSAWKGENEAQRAYPRIL--GHEAAGIVESVGEGVEDLKAG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  83 DRV----SGEghitCGFCRNCRAGRRHLC------------------RNSVgVGVNRP-------GAFAEYLVIPAFNAF 133
Cdd:PLN02740  91 DHVipifNGE----CGDCRYCKRDKTNLCetyrvdpfksvmvndgktRFST-KGDGQPiyhflntSTFTEYTVLDSACVV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 134 RIPDDIPDEIAAIFDpFGNATHTALSFNLV----GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGA 209
Cdd:PLN02740 166 KIDPNAPLKKMSLLS-CGVSTGVGAAWNTAnvqaGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKEMGI 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 210 TRAVNVQ------HENLgdvaaeLHMTE-GFDVGMEMSGVPSAFATMLGHMNHG-GKIAMLGIPPSQMAIDWNQI-IFKG 280
Cdd:PLN02740 245 TDFINPKdsdkpvHERI------REMTGgGVDYSFECAGNVEVLREAFLSTHDGwGLTVLLGIHPTPKMLPLHPMeLFDG 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519047159 281 LEIKG-IYGREMFETWYKMVAM--LQSGLDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:PLN02740 319 RSITGsVFGDFKGKSQLPNLAKqcMQGVVNLDGFITHELPFEKINEAFQLLEDGKALRCLL 379
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
13-338 9.22e-19

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: 85.73  E-value: 9.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIhIWKWDEWAQHTIPvPMQVGHEYVGEIVALGQEVRGLAIGDRVSGeghit 92
Cdd:cd08268   15 LRIEELPVPAPGAGEVLIRVEAIGLNRADA-MFRRGAYIEPPPL-PARLGYEAAGVVEAVGAGVTGFAVGDRVSV----- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 cgfcrncragrrhlcrnSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFdpfGNATHTALsFNLV-------GE 165
Cdd:cd08268   88 -----------------IPAADLGQYGTYAEYALVPAAAVVKLPDGLSFVEAAAL---WMQYLTAY-GALVelaglrpGD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 166 DVLITGA-GPIGIMAAAIARHVGARNVVITDVNDYRLALaRRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGVPS 244
Cdd:cd08268  147 SVLITAAsSSVGLAAIQIANAAGATVIATTRTSEKRDAL-LALGAAHVIVTDEEDLVAEVLRITGGKGVDVVFDPVGGPQ 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 245 aFATMLGHMNHGGKIAMLGIPPSQMAID--WNQiIFKGLEIKGIygrEMFETWY------KMVAMLQSGLD---LTPMIT 313
Cdd:cd08268  226 -FAKLADALAPGGTLVVYGALSGEPTPFplKAA-LKKSLTFRGY---SLDEITLdpearrRAIAFILDGLAsgaLKPVVD 300
                        330       340
                 ....*....|....*....|....*.
gi 519047159 314 HRFGVDDFQAGFAAMLSGNS-GKVVL 338
Cdd:cd08268  301 RVFPFDDIVEAHRYLESGQQiGKIVV 326
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
22-209 3.64e-17

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 81.77  E-value: 3.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  22 EVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHtipVPMQVGHEYVGEIVALGQEVRGLAIGDRVsGEGHI--TCGFCRNC 99
Cdd:PLN02514  31 KTGPEDVVIKVIYCGICHTDLHQIKNDLGMSN---YPMVPGHEVVGEVVEVGSDVSKFTVGDIV-GVGVIvgCCGECSPC 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 100 RAGRRHLCRNSV----GVGVN-RP--GAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALS-FNLVGEDVL--I 169
Cdd:PLN02514 107 KSDLEQYCNKRIwsynDVYTDgKPtqGGFASAMVVDQKFVVKIPEGMAPEQAAPLLCAGVTVYSPLShFGLKQSGLRggI 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 519047159 170 TGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGA 209
Cdd:PLN02514 187 LGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGA 226
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
13-339 1.27e-16

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: 79.97  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPV--PEVGhnDVMIRIRQTAICGTDIHIWKWDEwAQHTIPVPMqvGHEYVGEIVALGQEVRGLAIGDRVSGEGH 90
Cdd:cd08300   15 LSIEEVEVapPKAG--EVRIKILATGVCHTDAYTLSGAD-PEGLFPVIL--GHEGAGIVESVGEGVTSVKPGDHVIPLYT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  91 ITCGFCRNCRAGRRHLC---RNSVGVGVNRPG------------------AFAEYLVIPAFNAFRIPDDIP-DEIA---- 144
Cdd:cd08300   90 PECGECKFCKSGKTNLCqkiRATQGKGLMPDGtsrfsckgkpiyhfmgtsTFSEYTVVAEISVAKINPEAPlDKVCllgc 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 145 AIFDPFGNATHTAlsfNL-VGEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENLGDV 223
Cdd:cd08300  170 GVTTGYGAVLNTA---KVePGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPKDHDKPIQ 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 224 AAELHMTE-GFDVGMEMSGVPSAFATMLGHMNHG-GKIAMLGIPPSQMAIDWN--QII----FKGLEIKGIYGREMFEtw 295
Cdd:cd08300  247 QVLVEMTDgGVDYTFECIGNVKVMRAALEACHKGwGTSVIIGVAAAGQEISTRpfQLVtgrvWKGTAFGGWKSRSQVP-- 324
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 519047159 296 yKMVAMLQSG-LDLTPMITHRFGVDDFQAGFAAMLSGNSGKVVLD 339
Cdd:cd08300  325 -KLVEDYMKGkIKVDEFITHTMPLDEINEAFDLMHAGKSIRTVVK 368
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-235 1.94e-16

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 79.24  E-value: 1.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPGLAMTD--VPVPEVGHNDVMIRIRQTAICGTDihiWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRG 78
Cdd:cd08271    1 MKAWVLPKPGAALQLTLeeIEIPGPGAGEVLVKVHAAGLNPVD---WKVIAWGPPAWSYPHVPGVDGAGVVVAVGAKVTG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  79 LAIGDRVSGEGHITcgfcrncragrrhlcrnsvgvgvnRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTAL 158
Cdd:cd08271   78 WKVGDRVAYHASLA------------------------RGGSFAEYTVVDARAVLPLPDSLSFEEAAALPCAGLTAYQAL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 SFNL---VGEDVLITGA-GPIGIMAAAIARHVGARnvVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFD 234
Cdd:cd08271  134 FKKLrieAGRTILITGGaGGVGSFAVQLAKRAGLR--VITTCSKRNFEYVKSLGADHVIDYNDEDVCERIKEITGGRGVD 211

                 .
gi 519047159 235 V 235
Cdd:cd08271  212 A 212
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
13-338 1.98e-15

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


Pssm-ID: 176252 [Multi-domain]  Cd Length: 324  Bit Score: 76.22  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIhiWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVSGEGhit 92
Cdd:cd08292   16 LEIGEVPKPTPGAGEVLVRTTLSPIHNHDL--WTIRGTYGYKPELPAIGGSEAVGVVDAVGEGVKGLQVGQRVAVAP--- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 cgfcrncragrrhlcrnsvgvgvnRPGAFAEYLVIPAFNAFRIPDDIPDEIAA--IFDPFgnathTALSF----NLVGED 166
Cdd:cd08292   91 ------------------------VHGTWAEYFVAPADGLVPLPDGISDEVAAqlIAMPL-----SALMLldflGVKPGQ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 167 VLI--TGAGPIGIMAAAIARhvgARNV-VITDVN-DYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGv 242
Cdd:cd08292  142 WLIqnAAGGAVGKLVAMLAA---ARGInVINLVRrDAGVAELRALGIGPVVSTEQPGWQDKVREAAGGAPISVALDSVG- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 243 PSAFATMLGHMNHGGKI----AMLGIPpsqMAIDWNQIIFKGLEIKGIYG----REMFETWYK-----MVAMLQSGLDLT 309
Cdd:cd08292  218 GKLAGELLSLLGEGGTLvsfgSMSGEP---MQISSGDLIFKQATVRGFWGgrwsQEMSVEYRKrmiaeLLTLALKGQLLL 294
                        330       340       350
                 ....*....|....*....|....*....|
gi 519047159 310 PmITHRFGVDDF-QAGFAAMLSGNSGKVVL 338
Cdd:cd08292  295 P-VEAVFDLGDAaKAAAASMRPGRAGKVLL 323
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
17-241 1.90e-14

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: 73.45  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  17 DVPVPEVGHNDVMIRIRQTAICGTDIHIW--KWDEWaqhTIPvPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeghitcg 94
Cdd:cd08250   22 DVPVPLPGPGEVLVKNRFVGINASDINFTagRYDPG---VKP-PFDCGFEGVGEVVAVGEGVTDFKVGDAV--------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  95 fcrncragrrhlcrnsvgvGVNRPGAFAEYLVIPAFNAFRIPddipdEIAAIFDPFGNATHTA-LSFNLVG-----EDVL 168
Cdd:cd08250   89 -------------------ATMSFGAFAEYQVVPARHAVPVP-----ELKPEVLPLLVSGLTAsIALEEVGemksgETVL 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 519047159 169 ITGA-GPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELhMTEGFDVGMEMSG 241
Cdd:cd08250  145 VTAAaGGTGQFAVQLAKLAGCH-VIGTCSSDEKAEFLKSLGCDRPINYKTEDLGEVLKKE-YPKGVDVVYESVG 216
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
58-338 4.16e-14

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: 71.83  E-value: 4.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  58 PMQVGHEYVGEIVALGQEVRGLAIGDRVsgeghitCGFCrncragrrhlcrnsvgvgvnrPGAFAEYLVIPAFNAFRIPD 137
Cdd:cd05195   28 ETPLGLECSGIVTRVGSGVTGLKVGDRV-------MGLA---------------------PGAFATHVRVDARLVVKIPD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 138 DIPDEIAA-IFDPFGNATHtALsFNL----VGEDVLIT-GAGPIGIMAAAIARHVGARnvVITDV-NDYRLALARRMGAT 210
Cdd:cd05195   80 SLSFEEAAtLPVAYLTAYY-AL-VDLarlqKGESVLIHaAAGGVGQAAIQLAQHLGAE--VFATVgSEEKREFLRELGGP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 211 RAvNVQHENLGDVAAE-LHMT--EGFDV------GMEMSGVPSAFATmLGHMNHGGKIAMLGIPPSQMAIDWNQIIFKGL 281
Cdd:cd05195  156 VD-HIFSSRDLSFADGiLRATggRGVDVvlnslsGELLRASWRCLAP-FGRFVEIGKRDILSNSKLGMRPFLRNVSFSSV 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519047159 282 EIKGIY---GREMFETWYKMVAMLQSGLdLTPMITHRFGVDDFQAGFAAMLSG-NSGKVVL 338
Cdd:cd05195  234 DLDQLArerPELLRELLREVLELLEAGV-LKPLPPTVVPSASEIDAFRLMQSGkHIGKVVL 293
PGDH cd05288
Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the ...
13-338 3.10e-13

Prostaglandin dehydrogenases; Prostaglandins and related eicosanoids are metabolized by the oxidation of the 15(S)-hydroxyl group of the NAD+-dependent (type I 15-PGDH) 15-prostaglandin dehydrogenase (15-PGDH) followed by reduction by NADPH/NADH-dependent (type II 15-PGDH) delta-13 15-prostaglandin reductase (13-PGR) to 15-keto-13,14,-dihydroprostaglandins. 13-PGR is a bifunctional enzyme, since it also has leukotriene B(4) 12-hydroxydehydrogenase activity. These 15-PGDH and related enzymes are members of the medium chain dehydrogenase/reductase family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176190 [Multi-domain]  Cd Length: 329  Bit Score: 69.82  E-value: 3.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAIcgtDIHIWKWdewaqhtipvpMQVGHEYVgEIVALGQEVRGLAIGdRVSGEGHit 92
Cdd:cd05288   20 FELVEVPLPELKDGEVLVRTLYLSV---DPYMRGW-----------MSDAKSYS-PPVQLGEPMRGGGVG-EVVESRS-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 cgfcrncragrrhlcrNSVGVG--VNRPGAFAEYLVIPAFNAFR-IPDDIPDEIAAIFDPFGNATHTALsFNLV------ 163
Cdd:cd05288   82 ----------------PDFKVGdlVSGFLGWQEYAVVDGASGLRkLDPSLGLPLSAYLGVLGMTGLTAY-FGLTeigkpk 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 164 -GEDVLITGA-GPIGIMAAAIARHVGARNVVIT---DVNDYrlaLARRMGATRAVNVQHENLGDVAAElHMTEGFDVGME 238
Cdd:cd05288  145 pGETVVVSAAaGAVGSVVGQIAKLLGARVVGIAgsdEKCRW---LVEELGFDAAINYKTPDLAEALKE-AAPDGIDVYFD 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 239 MSGVPsAFATMLGHMNHGGKIAMLG------IPPSQMAIDWNQIIFKGLEIKG-IYGREM--FETWYK-MVAMLQSGlDL 308
Cdd:cd05288  221 NVGGE-ILDAALTLLNKGGRIALCGaisqynATEPPGPKNLGNIITKRLTMQGfIVSDYAdrFPEALAeLAKWLAEG-KL 298
                        330       340       350
                 ....*....|....*....|....*....|.
gi 519047159 309 TPMITHRFGVDDFQAGFAAMLSG-NSGKVVL 338
Cdd:cd05288  299 KYREDVVEGLENAPEAFLGLFTGkNTGKLVV 329
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
12-339 4.03e-13

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


Pssm-ID: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 69.54  E-value: 4.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  12 GLAMTDVPVPEVGHNDVMIRIRQtaiCG---TDIHIwkwdewAQHTIPVPMQ----VGHEYVGEIVALGQEVRGLAIGDR 84
Cdd:cd08275   13 KLKVEKEALPEPSSGEVRVRVEA---CGlnfADLMA------RQGLYDSAPKppfvPGFECAGTVEAVGEGVKDFKVGDR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  85 VsgeghitcgfcrncragrrhlcrnsvgVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFdPFGNATHTALSFNL-- 162
Cdd:cd08275   84 V---------------------------MGLTRFGGYAEVVNVPADQVFPLPDGMSFEEAAAF-PVNYLTAYYALFELgn 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 163 --VGEDVLI-TGAGPIGIMAAAIARHVgaRNV-VITDVNDYRLALARRMGATRAVNVQHENLGDVAAELhMTEGFDVGME 238
Cdd:cd08275  136 lrPGQSVLVhSAAGGVGLAAGQLCKTV--PNVtVVGTASASKHEALKENGVTHVIDYRTQDYVEEVKKI-SPEGVDIVLD 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 239 MSGVPSaFATMLGHMNHGGKIAMLG------------------------IPPSQMaIDWNQIIFkGLEIKGIY--GREMF 292
Cdd:cd08275  213 ALGGED-TRKSYDLLKPMGRLVVYGaanlvtgekrswfklakkwwnrpkVDPMKL-ISENKSVL-GFNLGWLFeeRELLT 289
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 519047159 293 ETWYKMVAMLQSGLdLTPMITHRFGVDDFQAGFAAMLSG-NSGKVVLD 339
Cdd:cd08275  290 EVMDKLLKLYEEGK-IKPKIDSVFPFEEVGEAMRRLQSRkNIGKVVLT 336
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
55-189 1.06e-12

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 67.80  E-value: 1.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159    55 IPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeghitCGFCrncragrrhlcrnsvgvgvnrPGAFAEYLVIPAFNAFR 134
Cdd:smart00829  20 YPGEAVLGGECAGVVTRVGPGVTGLAVGDRV-------MGLA---------------------PGAFATRVVTDARLVVP 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519047159   135 IPDDIPDEIAA-IFDPFGNATHtALsFNLV----GEDVLI-TGAGPIGIMAAAIARHVGAR 189
Cdd:smart00829  72 IPDGWSFEEAAtVPVVFLTAYY-AL-VDLArlrpGESVLIhAAAGGVGQAAIQLARHLGAE 130
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
22-265 1.35e-12

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 67.98  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  22 EVGHNDVMIRIRQTAICGTDIHIWKwDEWAQHTIP-VPmqvGHEYVGEIVALGQEVRGLAIGDRVsGEGHI--TCGFCRN 98
Cdd:PLN02586  34 ENGDEDVTVKILYCGVCHSDLHTIK-NEWGFTRYPiVP---GHEIVGIVTKLGKNVKKFKEGDRV-GVGVIvgSCKSCES 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  99 CRAGRRHLC------RNSVGV-GVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF---NLVGEDVL 168
Cdd:PLN02586 109 CDQDLENYCpkmiftYNSIGHdGTKNYGGYSDMIVVDQHFVLRFPDNLPLDAGAPLLCAGITVYSPMKYygmTEPGKHLG 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 169 ITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAvnVQHENLGDVAAELHMtegFDVGMEMSGVPSAFAT 248
Cdd:PLN02586 189 VAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSF--LVSTDPEKMKAAIGT---MDYIIDTVSAVHALGP 263
                        250
                 ....*....|....*..
gi 519047159 249 MLGHMNHGGKIAMLGIP 265
Cdd:PLN02586 264 LLGLLKVNGKLITLGLP 280
PLN02827 PLN02827
Alcohol dehydrogenase-like
13-338 2.38e-11

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 64.54  E-value: 2.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIhiwkwDEWAQHTIpVPMQVGHEYVGEIVALGQEVRGLAIGDRV----SGE 88
Cdd:PLN02827  25 LVMEEVEVSPPQPLEIRIKVVSTSLCRSDL-----SAWESQAL-FPRIFGHEASGIVESIGEGVTEFEKGDHVltvfTGE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  89 ghitCGFCRNCRAGRRHLCRNsvgVGVNRPG------------------------AFAEYLVIPAFNAFRIPDDIPDEIA 144
Cdd:PLN02827  99 ----CGSCRHCISGKSNMCQV---LGLERKGvmhsdqktrfsikgkpvyhycavsSFSEYTVVHSGCAVKVDPLAPLHKI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 145 AIFDpFGNATHTALSFNLV----GEDVLITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGATRAVNVQHENL 220
Cdd:PLN02827 172 CLLS-CGVAAGLGAAWNVAdvskGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFINPNDLSE 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 221 GDVAAELHMTE-GFDVGMEMSGVPSAFATMLGHMNHG-GKIAMLGIPPSQMAIDWNQIIF-KGLEIKGiygrEMFETWyK 297
Cdd:PLN02827 251 PIQQVIKRMTGgGADYSFECVGDTGIATTALQSCSDGwGLTVTLGVPKAKPEVSAHYGLFlSGRTLKG----SLFGGW-K 325
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 519047159 298 MVAMLQSGLD--------LTPMITHRFGVDDFQAGFAAMLSGNSGKVVL 338
Cdd:PLN02827 326 PKSDLPSLVDkymnkeimIDEFITHNLSFDEINKAFELMREGKCLRCVI 374
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
13-338 5.39e-11

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 63.05  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPevGHNDVMIRIRQTAICGTDI----HIWkwdeWAQHTIPVPMqvGHEYVGEIVALGQEVRGLAIGDRVsge 88
Cdd:cd08273   17 VVEADLPEP--AAGEVVVKVEASGVSFADVqmrrGLY----PDQPPLPFTP--GYDLVGRVDALGSGVTGFEVGDRV--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  89 ghitcgfcrncragrrhlcrnsvgVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIF-----DPFGNATHTALSfnLV 163
Cdd:cd08273   86 ------------------------AALTRVGGNAEYINLDAKYLVPVPEGVDAAEAVCLvlnyvTAYQMLHRAAKV--LT 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 164 GEDVLITGA-GPIGIMAAAIARHVGARnvVITDVNDYRLALARRMGATrAVNVQHEnlgDVAAELHMTEGFDVGMEMSGV 242
Cdd:cd08273  140 GQRVLIHGAsGGVGQALLELALLAGAE--VYGTASERNHAALRELGAT-PIDYRTK---DWLPAMLTPGGVDVVFDGVGG 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 243 PSaFATMLGHMNHGGKIAMLGIP----PSQMAIDWNQIIFKGL-EIKGIYG------------REMFETWYK-----MVA 300
Cdd:cd08273  214 ES-YEESYAALAPGGTLVCYGGNssllQGRRSLAALGSLLARLaKLKLLPTgrratfyyvwrdRAEDPKLFRqdlteLLD 292
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 519047159 301 MLQSGlDLTPMITHRFGVDDFQAGFAAMLSGN-SGKVVL 338
Cdd:cd08273  293 LLAKG-KIRPKIAKRLPLSEVAEAHRLLESGKvVGKIVL 330
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
22-265 1.48e-10

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 61.96  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  22 EVGHNDVMIRIRQTAICGTDIHIWKwDEWAQHTIPVpmQVGHEYVGEIVALGQEVRGLAIGDRVsGEGHI--TCGFCRNC 99
Cdd:PLN02178  28 ENGENDVTVKILFCGVCHSDLHTIK-NHWGFSRYPI--IPGHEIVGIATKVGKNVTKFKEGDRV-GVGVIigSCQSCESC 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 100 RAGRRHLCRNSVGV-------GVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSF----NLVGEDVL 168
Cdd:PLN02178 104 NQDLENYCPKVVFTynsrssdGTRNQGGYSDVIVVDHRFVLSIPDGLPSDSGAPLLCAGITVYSPMKYygmtKESGKRLG 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 169 ITGAGPIGIMAAAIARHVGARNVVITDVNDYRLALARRMGA-TRAVNVQHENLGDVAAELhmtegfDVGMEMSGVPSAFA 247
Cdd:PLN02178 184 VNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGAdSFLVTTDSQKMKEAVGTM------DFIIDTVSAEHALL 257
                        250
                 ....*....|....*...
gi 519047159 248 TMLGHMNHGGKIAMLGIP 265
Cdd:PLN02178 258 PLFSLLKVSGKLVALGLP 275
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
16-235 1.65e-10

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: 61.47  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  16 TDVPVPEVGH-NDVMIRIRQTAI--------CG---TDIHIW-KWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIG 82
Cdd:cd08248   19 ENARIPVIRKpNQVLIKVHAASVnpidvlmrSGygrTLLNKKrKPQSCKYSGIEFPLTLGRDCSGVVVDIGSGVKSFEIG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  83 DRVSGeghitcgfcrncragrrhlcrnsvGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFdPFgnATHTALS--- 159
Cdd:cd08248   99 DEVWG------------------------AVPPWSQGTHAEYVVVPENEVSKKPKNLSHEEAASL-PY--AGLTAWSalv 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 160 -------FNLVGEDVLITGA-GPIGIMAAAIARHVGArNVVITDVNDYRLaLARRMGATRAVNVqheNLGDVAAELHMTE 231
Cdd:cd08248  152 nvgglnpKNAAGKRVLILGGsGGVGTFAIQLLKAWGA-HVTTTCSTDAIP-LVKSLGADDVIDY---NNEDFEEELTERG 226

                 ....
gi 519047159 232 GFDV 235
Cdd:cd08248  227 KFDV 230
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
56-338 3.71e-10

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


Pssm-ID: 176213 [Multi-domain]  Cd Length: 303  Bit Score: 60.13  E-value: 3.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  56 PVPMQVGHEYVGEIVALGQEVRGLAIGDRVSgeghitcgfcrncragrrhlcrnsVGVGVnRPGAFAEYLVIPAFNAFRI 135
Cdd:cd08251   36 PYPFTPGFEASGVVRAVGPHVTRLAVGDEVI------------------------AGTGE-SMGGHATLVTVPEDQVVRK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 136 PDDIPDEIAAIFdP--FGNATHTALSFNLV-GEDVLI-TGAGPIGIMAAAIARHVGArNVVITDVNDYRLALARRMGATR 211
Cdd:cd08251   91 PASLSFEEACAL-PvvFLTVIDAFARAGLAkGEHILIqTATGGTGLMAVQLARLKGA-EIYATASSDDKLEYLKQLGVPH 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 212 AVNVQHEnlgDVAAEL-HMT--EGFDVGMEM-SGvpSAFATMLGHMNHGGK---IAMLGIpPSQMAIDW-----NQIIFK 279
Cdd:cd08251  169 VINYVEE---DFEEEImRLTggRGVDVVINTlSG--EAIQKGLNCLAPGGRyveIAMTAL-KSAPSVDLsvlsnNQSFHS 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 519047159 280 ------GLEIKGIYGREMFEtwykMVAMLQSGlDLTPMITHRFGVDDFQAGFAAMLSG-NSGKVVL 338
Cdd:cd08251  243 vdlrklLLLDPEFIADYQAE----MVSLVEEG-ELRPTVSRIFPFDDIGEAYRYLSDReNIGKVVV 303
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
1-285 4.12e-10

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


Pssm-ID: 176251 [Multi-domain]  Cd Length: 324  Bit Score: 60.31  E-value: 4.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKAL-----AKTERAPGLAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdewAQHTI--PVPMQVGHEYVGEIVALG 73
Cdd:cd08291    1 MKALlleeyGKPLEVKELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLK----GQYGStkALPVPPGFEGSGTVVAAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  74 QEVRGLA-IGDRVSgeghitcgfcrnCRAGRrhlcrnsvgvgvnrPGAFAEYLVIPAFNAFRIPDDIPDEIAA--IFDPF 150
Cdd:cd08291   77 GGPLAQSlIGKRVA------------FLAGS--------------YGTYAEYAVADAQQCLPLPDGVSFEQGAssFVNPL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 151 gnathTALSF-NLVGED-----VLITGAGPIGIMAAAIARHVGAR--NVVitdVNDYRLALARRMGATRAVNVQHEN--- 219
Cdd:cd08291  131 -----TALGMlETAREEgakavVHTAAASALGRMLVRLCKADGIKviNIV---RRKEQVDLLKKIGAEYVLNSSDPDfle 202
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519047159 220 -LGDVAAELHMTEGFD-VGMEMSGvpSAFATMlghMNHG-----GKIAMLGIPPsqmaIDWNQIIFKGLEIKG 285
Cdd:cd08291  203 dLKELIAKLNATIFFDaVGGGLTG--QILLAM---PYGStlyvyGYLSGKLDEP----IDPVDLIFKNKSIEG 266
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
1-339 4.84e-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: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 57.00  E-value: 4.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159   1 MKALAKTERAPG-LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKwdEWAQHTIPvpmqvGHEYVGEIVALGQEVRGL 79
Cdd:cd08270    1 MRALVVDPDAPLrLRLGEVPDPQPAPHEALVRVAAISLNRGELKFAA--ERPDGAVP-----GWDAAGVVERAAADGSGP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  80 AIGDRVsgeghitcgfcrncragrrhlcrnsvgVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTAL- 158
Cdd:cd08270   74 AVGARV---------------------------VGLGAMGAWAELVAVPTGWLAVLPDGVSFAQAATLPVAGVTALRALr 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 159 -SFNLVGEDVLITGA-GPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVnvqhenlgdVAAELHMTEGFDVG 236
Cdd:cd08270  127 rGGPLLGRRVLVTGAsGGVGRFAVQLAALAGAH-VVAVVGSPARAEGLRELGAAEVV---------VGGSELSGAPVDLV 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 237 MEMSGVPSaFATMLGHMNHGGKIAMLGIPPSQ-MAIDWNQIIFKGLEiKGIYGREMFETW------YKMVAMLQSGLdLT 309
Cdd:cd08270  197 VDSVGGPQ-LARALELLAPGGTVVSVGSSSGEpAVFNPAAFVGGGGG-RRLYTFFLYDGEplaadlARLLGLVAAGR-LD 273
                        330       340       350
                 ....*....|....*....|....*....|.
gi 519047159 310 PMITHRFGVDDFQAGFAAMLSGN-SGKVVLD 339
Cdd:cd08270  274 PRIGWRGSWTEIDEAAEALLARRfRGKAVLD 304
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
123-340 6.22e-09

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


Pssm-ID: 176199 [Multi-domain]  Cd Length: 341  Bit Score: 56.60  E-value: 6.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 123 EYLVIPAFNAFRIPDDIPDEIAAIFDPFGNATHTALSFNLVG----EDVLITGAGPIG-IMAAAIARHVGARNVVITDVN 197
Cdd:cd08237  119 DYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIAhkdrNVIGVWGDGNLGyITALLLKQIYPESKLVVFGKH 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 198 DYRLALARRMGATRAVNvqhenlgDVAAELHMTEGFD-VGMEMSGvpSAFATMLGHMNHGGKIAMLGIPPSQMAIDWNQI 276
Cdd:cd08237  199 QEKLDLFSFADETYLID-------DIPEDLAVDHAFEcVGGRGSQ--SAINQIIDYIRPQGTIGLMGVSEYPVPINTRMV 269
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 519047159 277 IFKGLEIKGI--YGREMFEtwyKMVAMLQSGLD----LTPMITHRF---GVDDFQAGFAAMLSGNSGKVVLDW 340
Cdd:cd08237  270 LEKGLTLVGSsrSTREDFE---RAVELLSRNPEvaeyLRKLVGGVFpvrSINDIHRAFESDLTNSWGKTVMEW 339
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
13-338 1.03e-08

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


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 55.84  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  13 LAMTDVPVPEVGHNDVMIRIRQTAICGTDIHIWKWDEWAQHTIPVPMQVGHEYVGEIVALGQEVRGLAIGDRVsgeghit 92
Cdd:cd08244   15 LVPEDVPDPVPGPGQVRIAVAAAGVHFVDTQLRSGWGPGPFPPELPYVPGGEVAGVVDAVGPGVDPAWLGRRV------- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  93 cgfcrncragrrhlcrnsVGVGVNRPGAFAEYLVIPAFNAFRIPD--DIPDEIAAIFDP------FGNATHTAlsfnlvG 164
Cdd:cd08244   88 ------------------VAHTGRAGGGYAELAVADVDSLHPVPDglDLEAAVAVVHDGrtalglLDLATLTP------G 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 165 EDVLITGA-GPIGIMAAAIARHVGARnVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAELHMTEGFDVGMEMSGVP 243
Cdd:cd08244  144 DVVLVTAAaGGLGSLLVQLAKAAGAT-VVGAAGGPAKTALVRALGADVAVDYTRPDWPDQVREALGGGGVTVVLDGVGGA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 244 SAFATmLGHMNHGGKIAMLGIPP-SQMAIDWNQIIFKGLEIKGIYGREMFETwyKMVAMLQSGLD------LTPMITHRF 316
Cdd:cd08244  223 IGRAA-LALLAPGGRFLTYGWASgEWTALDEDDARRRGVTVVGLLGVQAERG--GLRALEARALAeaaagrLVPVVGQTF 299
                        330       340
                 ....*....|....*....|...
gi 519047159 317 GVDDFQAGFAAMLS-GNSGKVVL 338
Cdd:cd08244  300 PLERAAEAHAALEArSTVGKVLL 322
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
62-340 1.14e-07

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: 52.99  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  62 GHEYVGEIVALGQEVRGLAIGDRVSgeghitcgfcrncragrrhlcrnsvgvgVNRP--GAFAEYLVIPAFNAFRIPDDI 139
Cdd:cd08290   68 GNEGVGEVVKVGSGVKSLKPGDWVI----------------------------PLRPglGTWRTHAVVPADDLIKVPNDV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 140 PDEIAAIF--DPfgnatHTAL----SF-NLVGEDVLITGAG--PIGIMAAAIARHVGARNV-VITDVNDYRLALAR--RM 207
Cdd:cd08290  120 DPEQAATLsvNP-----CTAYrlleDFvKLQPGDWVIQNGAnsAVGQAVIQLAKLLGIKTInVVRDRPDLEELKERlkAL 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 208 GATRAVNvqhENlgdvaaELHMTEGFDVGMEMSGVP----------SAFATMLGHMNHGGKI----AMLGIPpsqMAIDW 273
Cdd:cd08290  195 GADHVLT---EE------ELRSLLATELLKSAPGGRpklalncvggKSATELARLLSPGGTMvtygGMSGQP---VTVPT 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 274 NQIIFKGLEIKGIYGREmfetWYKM------VAMLQSGLDL-------TPMIT--HRFGVDDFQAGFA-AMLSGNSGKVV 337
Cdd:cd08290  263 SLLIFKDITLRGFWLTR----WLKRanpeekEDMLEELAELiregklkAPPVEkvTDDPLEEFKDALAnALKGGGGGKQV 338

                 ...
gi 519047159 338 LDW 340
Cdd:cd08290  339 LVM 341
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
99-263 1.62e-06

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: 49.08  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  99 CRAGRRHLCrNSVGVGVNRPGAFAEYLVIPAFNAFRIPDDIPDEIAAIfdpFGNATHTA-LSFNLVGE--------DVLI 169
Cdd:cd05280   77 FREGDEVLV-TGYDLGMNTDGGFAEYVRVPADWVVPLPEGLSLREAMI---LGTAGFTAaLSVHRLEDngqtpedgPVLV 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159 170 TGA-GPIGIMAAAIARHVGARNVVITDVNDYRlALARRMGATRAVNVQHENLGDVAAELHMTEGF--D-VGMEMsgvpsa 245
Cdd:cd05280  153 TGAtGGVGSIAVAILAKLGYTVVALTGKEEQA-DYLKSLGASEVLDREDLLDESKKPLLKARWAGaiDtVGGDV------ 225
                        170
                 ....*....|....*...
gi 519047159 246 FATMLGHMNHGGKIAMLG 263
Cdd:cd05280  226 LANLLKQTKYGGVVASCG 243
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
165-326 2.91e-06

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 47.71  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  165 EDVLITGAGPIGIMAAAIARHV-GARNVVITDVNDY---RLALARRMGATRaVNVQHENLGDVAAElhmTEGFDVGMEMS 240
Cdd:pfam16912  32 RSALVLGNGPLGLLALAMLRVQrGFDRVYCLGRRDRpdpTIDLVEELGATY-VDSRETPVDEIPAA---HEPMDLVYEAT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  241 GVPS-AFATMlGHMNHGGKIAMLGIP-PSQMAID----WNQIIfkgLEIKGIYG-----REMFETWYKMVAMLQSGLdLT 309
Cdd:pfam16912 108 GYAPhAFEAI-DALAPNGVAALLGVPtSWTFEIDggalHRELV---LHNKALVGsvnanRRHFEAAADTLAAAPEWF-LD 182
                         170
                  ....*....|....*..
gi 519047159  310 PMITHRFGVDDFQAGFA 326
Cdd:pfam16912 183 ALVTGVVPLDEFEEAFE 199
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
164-219 2.44e-05

L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, catalyzes the NADPH-dependent conversion of l-sorbose 1-phosphate to d-glucitol 6-phosphate in the metabolism of L-sorbose to (also converts d-fructose 1-phosphate to d-mannitol 6-phosphate). The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of an beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176200 [Multi-domain]  Cd Length: 410  Bit Score: 45.89  E-value: 2.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 519047159 164 GEDVLITGAGPIGIMAAAIARH--VGARNVVITDVNDYRLALARRM----GATRAVNVQHEN 219
Cdd:cd08238  177 GNTAILGGAGPMGLMAIDYAIHgpIGPSLLVVTDVNDERLARAQRLfppeAASRGIELLYVN 238
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
17-209 3.12e-05

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


Pssm-ID: 176208 [Multi-domain]  Cd Length: 393  Bit Score: 45.49  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  17 DVPVPEVGHNDVMIRIRQTAICGTDIhiwkwdeWAQHTIPV-------------PMQV-GHEYVGEIVALGQEVRGLAIG 82
Cdd:cd08246   34 DVPVPELGPGEVLVAVMAAGVNYNNV-------WAALGEPVstfaarqrrgrdePYHIgGSDASGIVWAVGEGVKNWKVG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 519047159  83 DRVSGEGHITCGFCRNCRAGRRHLCRNSV--GVGVNRpGAFAEYLVIPAFNAFRIPDDIPDEIAAIFdPFGNATHTALSF 160
Cdd:cd08246  107 DEVVVHCSVWDGNDPERAGGDPMFDPSQRiwGYETNY-GSFAQFALVQATQLMPKPKHLSWEEAAAY-MLVGATAYRMLF 184
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 519047159 161 ----NLV--GEDVLITGA-GPIGIMAAAIARHVGARNV-VITDvnDYRLALARRMGA 209
Cdd:cd08246  185 gwnpNTVkpGDNVLIWGAsGGLGSMAIQLARAAGANPVaVVSS--EEKAEYCRALGA 239
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
167-209 4.74e-03

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


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 37.10  E-value: 4.74e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 519047159   167 VLITGAGPIGIMAAAIARHVGARnVVITDVNDYRLA-LARRMGA 209
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAE-VTVLDVRPARLRqLESLLGA 65
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
166-226 5.85e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 38.16  E-value: 5.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 519047159 166 DVLITGAGPIGIMAAAIARHVGArNVVITDVNDYRLALARRMGATRAVNVQHENLGDVAAE 226
Cdd:cd01620  164 KVLIIGAGVVGLGAAKIAKKLGA-NVLVYDIKEEKLKGVETLGGSRLRYSQKEELEKELKQ 223
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
164-198 6.80e-03

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 37.87  E-value: 6.80e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 519047159 164 GEDVLITGAGPIGIMAAAIARHVGaRNVVITDVND 198
Cdd:COG0446  124 GKRAVVIGGGPIGLELAEALRKRG-LKVTLVERAP 157
 
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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