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Conserved domains on  [gi|1806958860|ref|WP_162414772|]
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zinc-dependent alcohol dehydrogenase family protein [Haloarcula salina]

Protein Classification

MDR/zinc-dependent alcohol dehydrogenase-like family protein( domain architecture ID 94789)

medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family protein may catalyze the reversible NAD(P)(H)-dependent conversion of an alcohol to its corresponding aldehyde

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-339 2.17e-132

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: 380.72  E-value: 2.17e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRV 80
Cdd:cd08234     1 MKALVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  81 AINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEVD 159
Cdd:cd08234    81 AVDPNIYCGECFYCRRGRPNLCENLTAVG----VTRNGGFAEYVVVPAKQVYKIPDnLSFEEAALAEPLSCAVHGLDLLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 160 VKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEaAIPAAAGGPVDVGAEAIG 239
Cdd:cd08234   157 IKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPSREDPE-AQKEDNPYGFDVVIEATG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 240 LVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTTEdFERAVTLLRYGRVDADALVTERIGLE 319
Cdd:cd08234   236 VPKTLEQAIEYARRGGTVLVFGVYAPDARVSISPFEIFQKELTIIGSFINPYT-FPRAIALLESGKIDVKGLVSHRLPLE 314

                         330       340
                  ....*....|....*....|
gi 1806958860 320 DLPTAFERMGNAEGLKKVVV 339
Cdd:cd08234   315 EVPEALEGMRSGGALKVVVV 334
 
Name Accession Description Interval E-value
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-339 2.17e-132

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: 380.72  E-value: 2.17e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRV 80
Cdd:cd08234     1 MKALVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  81 AINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEVD 159
Cdd:cd08234    81 AVDPNIYCGECFYCRRGRPNLCENLTAVG----VTRNGGFAEYVVVPAKQVYKIPDnLSFEEAALAEPLSCAVHGLDLLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 160 VKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEaAIPAAAGGPVDVGAEAIG 239
Cdd:cd08234   157 IKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPSREDPE-AQKEDNPYGFDVVIEATG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 240 LVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTTEdFERAVTLLRYGRVDADALVTERIGLE 319
Cdd:cd08234   236 VPKTLEQAIEYARRGGTVLVFGVYAPDARVSISPFEIFQKELTIIGSFINPYT-FPRAIALLESGKIDVKGLVSHRLPLE 314

                         330       340
                  ....*....|....*....|
gi 1806958860 320 DLPTAFERMGNAEGLKKVVV 339
Cdd:cd08234   315 EVPEALEGMRSGGALKVVVV 334
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-339 5.16e-122

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: 354.44  E-value: 5.16e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:COG1063     1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPfVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSIGGAGetiLDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEV 158
Cdd:COG1063    81 VVVEPNIPCGECRYCRRGRYNLCENLQFLGIAG---RDGGFAEYVRVPAANLVKVPDgLSDEAAALVEPLAVALHAVERA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 159 DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPVDVGAEA 237
Cdd:COG1063   158 GVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPREEDLvEAVRELTGGRGADVVIEA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 238 IGLVPTIEQANAVTAPGGSTLVFGVPDQEAtmEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADALVTERIG 317
Cdd:COG1063   238 VGAPAALEQALDLVRPGGTVVLVGVPGGPV--PIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFP 315

                         330       340
                  ....*....|....*....|...
gi 1806958860 318 LEDLPTAFERMGN-AEGLKKVVV 339
Cdd:COG1063   316 LDDAPEAFEAAADrADGAIKVVL 338
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1-338 1.73e-59

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 194.66  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMY------HGTfaVETPLVLGHESAGTVAEVGDDVAG 73
Cdd:PRK05396    1 MKALVKLKAEPgLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHIYnwdewaQKT--IPVPMVVGHEFVGEVVEVGSEVTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  74 FEVGDRVAINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDI-GEMSFEHAALAEPLACCV 152
Cdd:PRK05396   79 FKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVG----VNRPGAFAEYLVIPAFNVWKIpDDIPDDLAAIFDPFGNAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 HGVEEVDVKpGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPV 231
Cdd:PRK05396  155 HTALSFDLV-GEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAKEDLrDVMAELGMTEGF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISpfDVFFDEVGYRGSFSltTEDFE--RAVTLLRYGRVDAD 309
Cdd:PRK05396  234 DVGLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWN--KVIFKGLTIKGIYG--REMFEtwYKMSALLQSGLDLS 309

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 310 ALVTERIGLEDLPTAFERMGNAEGlKKVV 338
Cdd:PRK05396  310 PIITHRFPIDDFQKGFEAMRSGQS-GKVI 337
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 25-131 5.07e-42

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: 141.59  E-value: 5.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  25 DEVLVQVGACGVCMTDYHMYHGT-FAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCNACSYCKRGETHLCE 103
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGnPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80

                          90       100
                  ....*....|....*....|....*...
gi 1806958860 104 NNTSIGgageTILDGAFAEYVRVPAINV 131
Cdd:pfam08240  81 NGRFLG----YDRDGGFAEYVVVPERNL 104
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 29-187 7.26e-11

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 62.02  E-value: 7.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   29 VQVGACGVCMTDYHMYHGTfaVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAinptvpcnacsyckrgethlcenntsi 108
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGL--YPGEAVLGGECAGVVTRVGPGVTGLAVGDRVM--------------------------- 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  109 ggageTILDGAFAEYVRVPAINVEDI-GEMSFEHAAlAEPLACC--VHGVEEV-DVKPGDSVAI-IGAGPIGLLLLQAFR 183
Cdd:smart00829  52 -----GLAPGAFATRVVTDARLVVPIpDGWSFEEAA-TVPVVFLtaYYALVDLaRLRPGESVLIhAAAGGVGQAAIQLAR 125


                   ....
gi 1806958860  184 NAGA 187
Cdd:smart00829 126 HLGA 129
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 53-339 6.97e-06

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 47.17  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  53 PLVLGHESAGTVAEvgDDVAGFEVGDRVAINptvpcnacSYcKRGETHlcenntsiggagetilDGAFAEYVRVPAINVE 132
Cdd:TIGR02823  57 PMIPGIDAAGTVVS--SEDPRFREGDEVIVT--------GY-GLGVSH----------------DGGYSQYARVPADWLV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 133 DIGE-MSFEHAAL-------AeplACCVHGVEEVDVKPGD-SVAIIGA-GPIGLLLLQAFRNAGAAPIVVSELDDErREL 202
Cdd:TIGR02823 110 PLPEgLSLREAMAlgtagftA---ALSVMALERNGLTPEDgPVLVTGAtGGVGSLAVAILSKLGYEVVASTGKAEE-EDY 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 203 AAELGADAVVDPNE--DDPEAAIPAAAGGPVD-VGAEAI-GLVPTIEQANAVTAPGgstLVFGvPDQEATmeISPFD--- 275
Cdd:TIGR02823 186 LKELGASEVIDREDlsPPGKPLEKERWAGAVDtVGGHTLaNVLAQLKYGGAVAACG---LAGG-PDLPTT--VLPFIlrg 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806958860 276 ---VFFDEVGYrgSFSLTTEDFERAVTLLRYGRVDAdalVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:TIGR02823 260 vslLGIDSVYC--PMALREAAWQRLATDLKPRNLES---ITREITLEELPEALEQILAGQHRGRTVV 321
 
Name Accession Description Interval E-value
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-339 2.17e-132

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: 380.72  E-value: 2.17e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRV 80
Cdd:cd08234     1 MKALVYEGPGELEVEEVPVPEPGPDEVLIKVAACGICGTDLHIYEGEFGAAPPLVPGHEFAGVVVAVGSKVTGFKVGDRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  81 AINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEVD 159
Cdd:cd08234    81 AVDPNIYCGECFYCRRGRPNLCENLTAVG----VTRNGGFAEYVVVPAKQVYKIPDnLSFEEAALAEPLSCAVHGLDLLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 160 VKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEaAIPAAAGGPVDVGAEAIG 239
Cdd:cd08234   157 IKPGDSVLVFGAGPIGLLLAQLLKLNGASRVTVAEPNEEKLELAKKLGATETVDPSREDPE-AQKEDNPYGFDVVIEATG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 240 LVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTTEdFERAVTLLRYGRVDADALVTERIGLE 319
Cdd:cd08234   236 VPKTLEQAIEYARRGGTVLVFGVYAPDARVSISPFEIFQKELTIIGSFINPYT-FPRAIALLESGKIDVKGLVSHRLPLE 314

                         330       340
                  ....*....|....*....|
gi 1806958860 320 DLPTAFERMGNAEGLKKVVV 339
Cdd:cd08234   315 EVPEALEGMRSGGALKVVVV 334
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1-339 3.24e-132

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: 380.42  E-value: 3.24e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRV 80
Cdd:cd08236     1 MKALVLTGPGDLRYEDIPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAYHPPLVLGHEFSGTVEEVGSGVDDLAVGDRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  81 AINPTVPCNACSYCKRGETHLCENNTSIGGAgetiLDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEVD 159
Cdd:cd08236    81 AVNPLLPCGKCEYCKKGEYSLCSNYDYIGSR----RDGAFAEYVSVPARNLIKIPDhVDYEEAAMIEPAAVALHAVRLAG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 160 VKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVGAEAIG 239
Cdd:cd08236   157 ITLGDTVVVIGAGTIGLLAIQWLKILGAKRVIAVDIDDEKLAVARELGADDTINPKEEDVEKVRELTEGRGADLVIEAAG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 240 LVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPF-DVFFDEVGYRGSFSLT-----TEDFERAVTLLRYGRVDADALVT 313
Cdd:cd08236   237 SPATIEQALALARPGGKVVLVGIPYGDVTLSEEAFeKILRKELTIQGSWNSYsapfpGDEWRTALDLLASGKIKVEPLIT 316

                         330       340
                  ....*....|....*....|....*..
gi 1806958860 314 ERIGLEDLPTAFERMGN-AEGLKKVVV 339
Cdd:cd08236   317 HRLPLEDGPAAFERLADrEEFSGKVLL 343
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-339 5.16e-122

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: 354.44  E-value: 5.16e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:COG1063     1 MKALVLHGPGDLRLEEVPDPEPGPGEVLVRVTAVGICGSDLHIYRGGYPfVRPPLVLGHEFVGEVVEVGEGVTGLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSIGGAGetiLDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEV 158
Cdd:COG1063    81 VVVEPNIPCGECRYCRRGRYNLCENLQFLGIAG---RDGGFAEYVRVPAANLVKVPDgLSDEAAALVEPLAVALHAVERA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 159 DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPVDVGAEA 237
Cdd:COG1063   158 GVKPGDTVLVIGAGPIGLLAALAARLAGAARVIVVDRNPERLELARELGADAVVNPREEDLvEAVRELTGGRGADVVIEA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 238 IGLVPTIEQANAVTAPGGSTLVFGVPDQEAtmEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADALVTERIG 317
Cdd:COG1063   238 VGAPAALEQALDLVRPGGTVVLVGVPGGPV--PIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFP 315

                         330       340
                  ....*....|....*....|...
gi 1806958860 318 LEDLPTAFERMGN-AEGLKKVVV 339
Cdd:COG1063   316 LDDAPEAFEAAADrADGAIKVVL 338
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1-338 1.04e-110

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: 326.09  E-value: 1.04e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHM-YHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:cd08235     1 MKAAVLHGPNDVRLEEVPVPEPGPGEVLVKVRACGICGTDVKKiRGGHTDLKPPRILGHEIAGEIVEVGDGVTGFKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIG------EMSFEHAALAEPLACCVH 153
Cdd:cd08235    81 VFVAPHVPCGECHYCLRGNENMCPNYKKFG----NLYDGGFAEYVRVPAWAVKRGGvlklpdNVSFEEAALVEPLACCIN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 GVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPVD 232
Cdd:cd08235   157 AQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLvEKVRELTDGRGAD 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 233 VGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADALV 312
Cdd:cd08235   237 VVIVATGSPEAQAQALELVRKGGRILFFGGLPKGSTVNIDPNLIHYREITITGSYAASPEDYKEALELIASGKIDVKDLI 316

                         330       340
                  ....*....|....*....|....*.
gi 1806958860 313 TERIGLEDLPTAFERMGNAEGLKKVV 338
Cdd:cd08235   317 THRFPLEDIEEAFELAADGKSLKIVI 342
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 1-321 2.27e-94

(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: 284.43  E-value: 2.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHG--TFA----------VETPLVLGHESAGTVAEVG 68
Cdd:cd08233     1 MKAARYHGRKDIRVEEVPEPPVKPGEVKIKVAWCGICGSDLHEYLDgpIFIpteghphltgETAPVTLGHEFSGVVVEVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  69 DDVAGFEVGDRVAINPTVPCNACSYCKRGETHLCENNTSIGGAGEtilDGAFAEYVRVPAINVEDI-GEMSFEHAALAEP 147
Cdd:cd08233    81 SGVTGFKVGDRVVVEPTIKCGTCGACKRGLYNLCDSLGFIGLGGG---GGGFAEYVVVPAYHVHKLpDNVPLEEAALVEP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 148 LACCVHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDD-PEAAIPAA 226
Cdd:cd08233   158 LAVAWHAVRRSGFKPGDTALVLGAGPIGLLTILALKAAGASKIIVSEPSEARRELAEELGATIVLDPTEVDvVAEVRKLT 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 227 AGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEAtmEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRV 306
Cdd:cd08233   238 GGGGVDVSFDCAGVQATLDTAIDALRPRGTAVNVAIWEKPI--SFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASGKI 315

                         330
                  ....*....|....*
gi 1806958860 307 DADALVTERIGLEDL 321
Cdd:cd08233   316 DAEPLITSRIPLEDI 330
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 3-339 3.60e-88

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: 268.59  E-value: 3.60e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   3 ASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYH----GTFAVETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd05285     1 AAVLHGPGDLRLEERPIPEPGPGEVLVRVRAVGICGSDVHYYKhgriGDFVVKEPMVLGHESAGTVVAVGSGVTHLKVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENNTSIGGAGetiLDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEE 157
Cdd:cd05285    81 RVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPP---VDGTLCRYVNHPADFCHKLPDnVSLEEGALVEPLSVGVHACRR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 158 VDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAA----GGPVDV 233
Cdd:cd05285   158 AGVRPGDTVLVFGAGPIGLLTAAVAKAFGATKVVVTDIDPSRLEFAKELGATHTVNVRTEDTPESAEKIAellgGKGPDV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 234 GAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISpfDVFFDEVGYRGSFSLtTEDFERAVTLLRYGRVDADALVT 313
Cdd:cd05285   238 VIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLS--AASLREIDIRGVFRY-ANTYPTAIELLASGKVDVKPLIT 314

                         330       340
                  ....*....|....*....|....*..
gi 1806958860 314 ERIGLEDLPTAFERMGNAEGLK-KVVV 339
Cdd:cd05285   315 HRFPLEDAVEAFETAAKGKKGViKVVI 341
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 1-339 1.23e-87

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 266.59  E-value: 1.23e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:COG1064     1 MKAAVLTEPGGpLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPvPKLPLVPGHEIVGRVVAVGPGVTGFKVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDI-GEMSFEHAAlaePLAC----CVH 153
Cdd:COG1064    81 RVGVGWVDSCGTCEYCRSGRENLCENGRFTG----YTTDGGYAEYVVVPARFLVKLpDGLDPAEAA---PLLCagitAYR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 GVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSeLDDERRELAAELGADAVVDPNEDDPEaaIPAAAGGPVDV 233
Cdd:COG1064   154 ALRRAGVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVD-RSPEKLELARELGADHVVNSSDEDPV--EAVRELTGADV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 234 GAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEatMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADalvT 313
Cdd:COG1064   231 VIDTVGAPATVNAALALLRRGGRLVLVGLPGGP--IPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKIKPE---V 305

                         330       340
                  ....*....|....*....|....*.
gi 1806958860 314 ERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:COG1064   306 ETIPLEEANEALERLRAGKVRGRAVL 331
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 1-339 6.15e-87

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: 265.94  E-value: 6.15e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:cd08279     1 MRAAVLHEVGKpLEIEEVELDDPGPGEVLVRIAAAGLCHSDLHVVTGDLPAPLPAVLGHEGAGVVEEVGPGVTGVKPGDH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSIGG----AGETILD------------GAFAEYVRVPAINVEDIGE-MSFEHA 142
Cdd:cd08279    81 VVLSWIPACGTCRYCSRGQPNLCDLGAGILGgqlpDGTRRFTadgepvgamcglGTFAEYTVVPEASVVKIDDdIPLDRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 143 ALaepLACCV-HGVEEV----DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNED 217
Cdd:cd08279   161 AL---LGCGVtTGVGAVvntaRVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAVDPVPEKLELARRFGATHTVNASED 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 218 DP-EAAIPAAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSF---SLTTED 293
Cdd:cd08279   238 DAvEAVRDLTDGRGADYAFEAVGRAATIRQALAMTRKGGTAVVVGMGPPGETVSLPALELFLSEKRLQGSLygsANPRRD 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1806958860 294 FERAVTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08279   318 IPRLLDLYRAGRLKLDELVTRRYSLDEINEAFADMLAGENARGVIV 363
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1-339 2.37e-83

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: 255.96  E-value: 2.37e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:cd08261     1 MKALVCEKPGRLEVVDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPfASYPRILGHELSGEVVEVGEGVAGLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGEMSFEHAALAEPLACCVHGVEEVD 159
Cdd:cd08261    81 VVVDPYISCGECYACRKGRPNCCENLQVLG----VHRDGGFAEYIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRRAG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 160 VKPGDSVAIIGAGPIGLLLLQAFRNAGAApIVVSELDDERRELAAELGADAVVDP-NEDDPEAAIPAAAGGPVDVGAEAI 238
Cdd:cd08261   157 VTAGDTVLVVGAGPIGLGVIQVAKARGAR-VIVVDIDDERLEFARELGADDTINVgDEDVAARLRELTDGEGADVVIDAT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 239 GLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFdvFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADALVTERIGL 318
Cdd:cd08261   236 GNPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEF--HKKELTILGSRNATREDFPDVIDLLESGKVDPEALITHRFPF 313

                         330       340
                  ....*....|....*....|..
gi 1806958860 319 EDLPTAFER-MGNAEGLKKVVV 339
Cdd:cd08261   314 EDVPEAFDLwEAPPGGVIKVLI 335
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
10-339 6.88e-83

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 255.39  E-value: 6.88e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  10 GEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCN 89
Cdd:COG1062     2 GPLEIEEVELDEPRPGEVLVRIVAAGLCHSDLHVRDGDLPVPLPAVLGHEGAGVVEEVGPGVTGVAPGDHVVLSFIPSCG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  90 ACSYCKRGETHLCENNTSIGGAGeTILDG-------------------AFAEYVRVPAINVEDI-GEMSFEHAAlaePLA 149
Cdd:COG1062    82 HCRYCASGRPALCEAGAALNGKG-TLPDGtsrlssadgepvghffgqsSFAEYAVVPERSVVKVdKDVPLELAA---LLG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 150 CCVH-GVEEV----DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIP 224
Cdd:COG1062   158 CGVQtGAGAVlntaKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAVDPVPEKLELARELGATHTVNPADEDAVEAVR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 225 AAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSF---SLTTEDFERAVTLL 301
Cdd:COG1062   238 ELTGGGVDYAFETTGNPAVIRQALEALRKGGTVVVVGLAPPGAEISLDPFQLLLTGRTIRGSYfggAVPRRDIPRLVDLY 317

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1806958860 302 RYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:COG1062   318 RAGRLPLDELITRRYPLDEINEAFDDLRSGEVIRPVIV 355
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 10-339 2.53e-74

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: 232.90  E-value: 2.53e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  10 GEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYH----GTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPT 85
Cdd:cd08232     7 GDLRVEERPAPEPGPGEVRVRVAAGGICGSDLHYYQhggfGTVRLREPMVLGHEVSGVVEAVGPGVTGLAPGQRVAVNPS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  86 VPCNACSYCKRGETHLCENNTSIGGAGETI-LDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEVDVKPG 163
Cdd:cd08232    87 RPCGTCDYCRAGRPNLCLNMRFLGSAMRFPhVQGGFREYLVVDASQCVPLPDgLSLRRAALAEPLAVALHAVNRAGDLAG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 164 DSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPneDDPEAAIPAAAGGPVDVGAEAIGLVPT 243
Cdd:cd08232   167 KRVLVTGAGPIGALVVAAARRAGAAEIVATDLADAPLAVARAMGADETVNL--ARDPLAAYAADKGDFDVVFEASGAPAA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 244 IEQANAVTAPGGSTLVFGVPDQEATMEISPfdVFFDEVGYRGSFSLTTEdFERAVTLLRYGRVDADALVTERIGLEDLPT 323
Cdd:cd08232   245 LASALRVVRPGGTVVQVGMLGGPVPLPLNA--LVAKELDLRGSFRFDDE-FAEAVRLLAAGRIDVRPLITAVFPLEEAAE 321

                         330
                  ....*....|....*.
gi 1806958860 324 AFERMGNAEGLKKVVV 339
Cdd:cd08232   322 AFALAADRTRSVKVQL 337
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 1-304 6.85e-73

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: 227.97  E-value: 6.85e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDV--GEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVG 77
Cdd:cd08258     1 MKALVKTGPgpGNVELREVPEPEPGPGEVLIKVAAAGICGSDLHIYKGDYDpVETPVVLGHEFSGTIVEVGPDVEGWKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  78 DRV-AINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGV 155
Cdd:cd08258    81 DRVvSETTFSTCGRCPYCRRGDYNLCPHRKGIG----TQADGGFAEYVLVPEESLHELPEnLSLEAAALTEPLAVAVHAV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 156 -EEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVS-ELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDV 233
Cdd:cd08258   157 aERSGIRPGDTVVVFGPGPIGLLAAQVAKLQGATVVVVGtEKDEVRLDVAKELGADAVNGGEEDLAELVNEITDGDGADV 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1806958860 234 GAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATmEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYG 304
Cdd:cd08258   237 VIECSGAVPALEQALELLRKGGRIVQVGIFGPLAA-SIDVERIIQKELSVIGSRSSTPASWETALRLLASG 306
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 26-301 4.45e-72

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: 224.89  E-value: 4.45e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  26 EVLVQVGACGVCMTDYHMYHGT--FAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCNACSYCKRgethLCE 103
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGypPPPKLPLILGHEGAGVVVEVGPGVTGVKVGDRVVVLPNLGCGTCELCRE----LCP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 104 NNTSIGGAgetiLDGAFAEYVRVPAINVEDI-GEMSFEHAALA-EPLACCVHGVEEV-DVKPGDSVAIIGAGPIGLLLLQ 180
Cdd:cd05188    77 GGGILGEG----LDGGFAEYVVVPADNLVPLpDGLSLEEAALLpEPLATAYHALRRAgVLKPGDTVLVLGAGGVGLLAAQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 181 AFRNAGAaPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVF 260
Cdd:cd05188   153 LAKAAGA-RVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGGGADVVIDAVGGPETLAQALRLLRPGGRIVVV 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1806958860 261 GVPDQEATMEIsPFDVFFDEVGYRGSFSLTTEDFERAVTLL 301
Cdd:cd05188   232 GGTSGGPPLDD-LRRLLFKELTIIGSTGGTREDFEEALDLL 271
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-340 1.53e-71

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: 225.96  E-value: 1.53e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAV-EERERPEPAADEVLVQVGACGVCMTDYHMYHGT-FA---VETPLVLGHESAGTVAEVGDDVAGFE 75
Cdd:cd05281     1 MKAIVKTKAGPGAElVEVPVPKPGPGEVLIKVLAASICGTDVHIYEWDeWAqsrIKPPLIFGHEFAGEVVEVGEGVTRVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVAINPTVPCNACSYCKRGETHLCENnTSIGGAGetiLDGAFAEYVRVPAINV-EDIGEMSFEHAALAEPLACCVHG 154
Cdd:cd05281    81 VGDYVSAETHIVCGKCYQCRTGNYHVCQN-TKILGVD---TDGCFAEYVVVPEENLwKNDKDIPPEIASIQEPLGNAVHT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 155 VEEVDVkPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVG 234
Cdd:cd05281   157 VLAGDV-SGKSVLITGCGPIGLMAIAVAKAAGASLVIASDPNPYRLELAKKMGADVVINPREEDVVEVKSVTDGTGVDVV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 235 AEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISpfdvffDEVGYRGsfsLTT---------EDFERAVTLLRYGR 305
Cdd:cd05281   236 LEMSGNPKAIEQGLKALTPGGRVSILGLPPGPVDIDLN------NLVIFKG---LTVqgitgrkmfETWYQVSALLKSGK 306

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1806958860 306 VDADALVTERIGLEDLPTAFERMGNAEGLKKVVVP 340
Cdd:cd05281   307 VDLSPVITHKLPLEDFEEAFELMRSGKCGKVVLYP 341
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 1-339 2.62e-69

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: 219.81  E-value: 2.62e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERP--EPAADEVLVQVGACGVCMTDYHMYHG--TFAVETPLVLGHESAGTVAEVGDDVAGFEV 76
Cdd:cd08254     1 MKAWRFHKGSKGLLVLEEVPvpEPGPGEVLVKVKAAGVCHSDLHILDGgvPTLTKLPLTLGHEIAGTVVEVGAGVTNFKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  77 GDRVAINPTVPCNACSYCKRGETHLCENNTSIGGAgetiLDGAFAEYVRVPAINVEDI-GEMSFEHAALAeplACCV--- 152
Cdd:cd08254    81 GDRVAVPAVIPCGACALCRRGRGNLCLNQGMPGLG----IDGGFAEYIVVPARALVPVpDGVPFAQAAVA---TDAVltp 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 -HGVEEVD-VKPGDSVAIIGAGPIGLLLLQAFRNAGAApIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGP 230
Cdd:cd08254   154 yHAVVRAGeVKPGETVLVIGLGGLGLNAVQIAKAMGAA-VIAVDIKEEKLELAKELGADEVLNSLDDSPKDKKAAGLGGG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 231 VDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEatMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDada 310
Cdd:cd08254   233 FDVIFDFVGTQPTFEDAQKAVKPGGRIVVVGLGRDK--LTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLD--- 307

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 311 LVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08254   308 PQVETRPLDEIPEVLERLHKGKVKGRVVL 336
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 1-339 5.81e-67

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: 214.06  E-value: 5.81e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPA-ADEVLVQVGACGVCMTDYHMYHG-TFAVETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd05278     1 MKALVYLGPGKIGLEEVPDPKIQgPHDAIVRVTATSICGSDLHIYRGgVPGAKHGMILGHEFVGEVVEVGSDVKRLKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENNTSIGGAGETIlDGAFAEYVRVP-----AINVEDigEMSFEHA-ALAEPLACCV 152
Cdd:cd05278    81 RVSVPCITFCGRCRFCRRGYHAHCENGLWGWKLGNRI-DGGQAEYVRVPyadmnLAKIPD--GLPDEDAlMLSDILPTGF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 HGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPV 231
Cdd:cd05278   158 HGAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINPKNGDIvEQILELTGGRGV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPdQEATMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADAL 311
Cdd:cd05278   238 DCVIEAVGFEETFEQAVKVVRPGGTIANVGVY-GKPDPLPLLGEWFGKNLTFKTGLVPVRARMPELLDLIEEGKIDPSKL 316

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 312 VTERIGLEDLPTAFERMGNAE-GLKKVVV 339
Cdd:cd05278   317 ITHRFPLDDILKAYRLFDNKPdGCIKVVI 345
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 1-339 1.43e-66

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: 212.94  E-value: 1.43e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDvGEIAVEERERPEPAADEVLVQVGACGVCMTDYHM------------YHGTFAVETPLVLGHESAGTVAEVG 68
Cdd:cd08262     1 MRAAVFRD-GPLVVRDVPDPEPGPGQVLVKVLACGICGSDLHAtahpeamvddagGPSLMDLGADIVLGHEFCGEVVDYG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  69 DDVAG-FEVGDRVAINPTVPCNACSYCKRGEthlceNNTSIGGagetildgaFAEYVRV-PAINVEDIGEMSFEHAALAE 146
Cdd:cd08262    80 PGTERkLKVGTRVTSLPLLLCGQGASCGIGL-----SPEAPGG---------YAEYMLLsEALLLRVPDGLSMEDAALTE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 147 PLACCVHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAA 226
Cdd:cd08262   146 PLAVGLHAVRRARLTPGEVALVIGCGPIGLAVIAALKARGVGPIVASDFSPERRALALAMGADIVVDPAADSPFAAWAAE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 227 AGGPV----DVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEisPFDVFFDEVGYRGSFSLTTEDFERAVTLLR 302
Cdd:cd08262   226 LARAGgpkpAVIFECVGAPGLIQQIIEGAPPGGRIVVVGVCMESDNIE--PALAIRKELTLQFSLGYTPEEFADALDALA 303

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1806958860 303 YGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08262   304 EGKVDVAPMVTGTVGLDGVPDAFEALRDPEHHCKILV 340
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-339 3.38e-62

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


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 201.61  E-value: 3.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE--IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET--PLVLGHESAGTVAEVGDDVAGFEV 76
Cdd:cd08297     1 MKAAVVEEFGEkpYEVKDVPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPVKPklPLIGGHEGAGVVVAVGPGVSGLKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  77 GDRVAINPTV-PCNACSYCKRGETHLCENNTSIGGAgetiLDGAFAEYVRVPAINVEDIGE-MSFEHAAlaePLAC---- 150
Cdd:cd08297    81 GDRVGVKWLYdACGKCEYCRTGDETLCPNQKNSGYT----VDGTFAEYAIADARYVTPIPDgLSFEQAA---PLLCagvt 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 151 CVHGVEEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVsELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGG 229
Cdd:cd08297   154 VYKALKKAGLKPGDWVVISGAgGGLGHLGVQYAKAMGLRVIAI-DVGDEKLELAKELGADAFVDFKKSDDVEAVKELTGG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 230 PvdvGAEAIGLVPT----IEQANAVTAPGGsTLVF-GVPDQEaTMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYG 304
Cdd:cd08297   233 G---GAHAVVVTAVsaaaYEQALDYLRPGG-TLVCvGLPPGG-FIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARG 307

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1806958860 305 RVDADalVTERiGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08297   308 KVKPH--IQVV-PLEDLNEVFEKMEEGKIAGRVVV 339
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 1-339 5.55e-62

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: 201.48  E-value: 5.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA----------VETPLVLGHESAGTVAEVGDD 70
Cdd:cd08256     1 MRAVVCHGPQDYRLEEVPVPRPGPGEILVKVEACGICAGDIKCYHGAPSfwgdenqppyVKPPMIPGHEFVGRVVELGEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  71 VA--GFEVGDRVAINPTVPCNACSYCKRGETHLCENNTSIGGAGETilDGAFAEYVRVP--AINVEDIGEMSFEHAALAE 146
Cdd:cd08256    81 AEerGVKVGDRVISEQIVPCWNCRFCNRGQYWMCQKHDLYGFQNNV--NGGMAEYMRFPkeAIVHKVPDDIPPEDAILIE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 147 PLACCVHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNE-DDPEAAIPA 225
Cdd:cd08256   159 PLACALHAVDRANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVLDLKDERLALARKFGADVVLNPPEvDVVEKIKEL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 226 AAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISpfdVFFD--EVGYRGSfSLTTEDFERAVTLLRY 303
Cdd:cd08256   239 TGGYGCDIYIEATGHPSAVEQGLNMIRKLGRFVEFSVFGDPVTVDWS---IIGDrkELDVLGS-HLGPYCYPIAIDLIAS 314

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1806958860 304 GRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08256   315 GRLPTDGIVTHQFPLEDFEEAFELMARGDDSIKVVL 350
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1-340 1.50e-61

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: 200.18  E-value: 1.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPE-PAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:cd08284     1 MKAVVFKGPGDVRVEEVPIPQiQDPTDAIVKVTAAAICGSDLHIYRGHIPSTPGFVLGHEFVGEVVEVGPEVRTLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSIGGAGETILDGAFAEYVRVPA--INVEDIGEMSFEHAA--LAEPLACCVHGV 155
Cdd:cd08284    81 VVSPFTIACGECFYCRRGQSGRCAKGGLFGYAGSPNLDGAQAEYVRVPFadGTLLKLPDGLSDEAAllLGDILPTGYFGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 156 EEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVGA 235
Cdd:cd08284   161 KRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAVDPVPERLERAAALGAEPINFEDAEPVERVREATEGRGADVVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 236 EAIGLVPTIEQANAVTAPGGSTLVFGVPDQEAtMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADALVTER 315
Cdd:cd08284   241 EAVGGAAALDLAFDLVRPGGVISSVGVHTAEE-FPFPGLDAYNKNLTLRFGRCPVRSLFPELLPLLESGRLDLEFLIDHR 319

                         330       340
                  ....*....|....*....|....*
gi 1806958860 316 IGLEDLPTAFERMGNAEGLKKVVVP 340
Cdd:cd08284   320 MPLEEAPEAYRLFDKRKVLKVVLDP 344
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 2-340 1.56e-61

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: 200.56  E-value: 1.56e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   2 RASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVG----DDVAG-- 73
Cdd:cd08231     2 RAAVLTGPGKpLEIREVPLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPlPIILGHEGVGRVVALGggvtTDVAGep 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  74 FEVGDRVAINPTVPCNACSYCKRGETHLCENNTSIG---GAGETILDGAFAEYVRVPA----INVEDigEMSFEHAALA- 145
Cdd:cd08231    82 LKVGDRVTWSVGAPCGRCYRCLVGDPTKCENRKKYGheaSCDDPHLSGGYAEHIYLPPgtaiVRVPD--NVPDEVAAPAn 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 146 EPLACCVHGVEEV-DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIP 224
Cdd:cd08231   160 CALATVLAALDRAgPVGAGDTVVVQGAGPLGLYAVAAAKLAGARRVIVIDGSPERLELAREFGADATIDIDELPDPQRRA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 225 AAAGGP----VDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTTEDFERAVTL 300
Cdd:cd08231   240 IVRDITggrgADVVIEASGHPAAVPEGLELLRRGGTYVLVGSVAPAGTVPLDPERIVRKNLTIIGVHNYDPSHLYRAVRF 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1806958860 301 LR--YGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVVP 340
Cdd:cd08231   320 LErtQDRFPFAELVTHRYPLEDINEALELAESGTALKVVIDP 361
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 1-338 1.73e-59

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 194.66  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMY------HGTfaVETPLVLGHESAGTVAEVGDDVAG 73
Cdd:PRK05396    1 MKALVKLKAEPgLWLTDVPVPEPGPNDVLIKVKKTAICGTDVHIYnwdewaQKT--IPVPMVVGHEFVGEVVEVGSEVTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  74 FEVGDRVAINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDI-GEMSFEHAALAEPLACCV 152
Cdd:PRK05396   79 FKVGDRVSGEGHIVCGHCRNCRAGRRHLCRNTKGVG----VNRPGAFAEYLVIPAFNVWKIpDDIPDDLAAIFDPFGNAV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 HGVEEVDVKpGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPV 231
Cdd:PRK05396  155 HTALSFDLV-GEDVLITGAGPIGIMAAAVAKHVGARHVVITDVNEYRLELARKMGATRAVNVAKEDLrDVMAELGMTEGF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISpfDVFFDEVGYRGSFSltTEDFE--RAVTLLRYGRVDAD 309
Cdd:PRK05396  234 DVGLEMSGAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWN--KVIFKGLTIKGIYG--REMFEtwYKMSALLQSGLDLS 309

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 310 ALVTERIGLEDLPTAFERMGNAEGlKKVV 338
Cdd:PRK05396  310 PIITHRFPIDDFQKGFEAMRSGQS-GKVI 337
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-339 4.36e-58

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: 191.28  E-value: 4.36e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd08260     1 MRAAVYEEFGEpLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPdVTLPHVPGHEFAGVVVEVGEDVSRWRVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIG---EMSFEHAALaepLACCV--- 152
Cdd:cd08260    81 RVTVPFVLGCGTCPYCRAGDSNVCEHQVQPG----FTHPGSFAEYVAVPRADVNLVRlpdDVDFVTAAG---LGCRFata 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 -HG-VEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVsELDDERRELAAELGADAVVDPNE-DDPEAAIPAAAGG 229
Cdd:cd08260   154 fRAlVHQARVKPGEWVAVHGCGGVGLSAVMIASALGARVIAV-DIDDDKLELARELGAVATVNASEvEDVAAAVRDLTGG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 230 PVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFD-VFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDA 308
Cdd:cd08260   233 GAHVSVDALGIPETCRNSVASLRKRGRHVQVGLTLGEEAGVALPMDrVVARELEIVGSHGMPAHRYDAMLALIASGKLDP 312

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1806958860 309 DALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08260   313 EPLVGRTISLDEAPDALAAMDDYATAGITVI 343
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-339 7.43e-58

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: 190.22  E-value: 7.43e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTF-AVETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd08259     1 MKAAILHKPNKpLQIEEVPDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFpRGKYPLILGHEIVGTVEEVGEGVERFKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENNTSIGGagetILDGAFAEYVRVPAIN-VEDIGEMSFEHAALAE-PLACCVHGVE 156
Cdd:cd08259    81 RVILYYYIPCGKCEYCLSGEENLCRNRAEYGE----EVDGGFAEYVKVPERSlVKLPDNVSDESAALAAcVVGTAVHALK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 157 EVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVDPNEDDPEaaipAAAGGPVDVGA 235
Cdd:cd08259   157 RAGVKKGDTVLVTGAgGGVGIHAIQLAKALGARVIAVTR-SPEKLKILKELGADYVIDGSKFSED----VKKLGGADVVI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 236 EAIGlVPTIEQANAVTAPGGSTLVFG-VPDQEAtmEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVdaDALVTE 314
Cdd:cd08259   232 ELVG-SPTIEESLRSLNKGGRLVLIGnVTPDPA--PLRPGLLILKEIRIIGSISATKADVEEALKLVKEGKI--KPVIDR 306

                         330       340
                  ....*....|....*....|....*
gi 1806958860 315 RIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08259   307 VVSLEDINEALEDLKSGKVVGRIVL 331
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 1-340 2.90e-57

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: 189.07  E-value: 2.90e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET--PLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd08239     1 MRGAVFPGDRTVELREFPVPVPGPGEVLLRVKASGLCGSDLHYYYHGHRAPAyqGVIPGHEPAGVVVAVGPGVTHFRVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENNTSIGGageTILDGAFAEYVRVPA---INVEDigEMSFEHAALaepLACCV--- 152
Cdd:cd08239    81 RVMVYHYVGCGACRNCRRGWMQLCTSKRAAYG---WNRDGGHAEYMLVPEktlIPLPD--DLSFADGAL---LLCGIgta 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 -HGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPV 231
Cdd:cd08239   153 yHALRRVGVSGRDTVLVVGAGPVGLGALMLARALGAEDVIGVDPSPERLELAKALGADFVINSGQDDVQEIRELTSGAGA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DVGAEAIGLVPTIEQANAVTAPGGSTLVFGVpDQEATMEISPfDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADAL 311
Cdd:cd08239   233 DVAIECSGNTAARRLALEAVRPWGRLVLVGE-GGELTIEVSN-DLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVDRL 310

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 312 VTERIGLEDLPTAFERMGNAEGLKKVVVP 340
Cdd:cd08239   311 VTHRFGLDQAPEAYALFAQGESGKVVFVF 339
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 1-340 1.37e-55

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: 184.69  E-value: 1.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA----VETPLVLGHESAGTVAEVGDDVAGFE 75
Cdd:cd05284     1 MKAARLYEYGKpLRLEDVPVPEPGPGQVLVRVGGAGVCHSDLHVIDGVWGgilpYKLPFTLGHENAGWVEEVGSGVDGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVAINPTVPCNACSYCKRGETHLCEnNTSIGGAGetiLDGAFAEYVRVPAIN-VEDIGEMSFEHAAlaePLACC--- 151
Cdd:cd05284    81 EGDPVVVHPPWGCGTCRYCRRGEENYCE-NARFPGIG---TDGGFAEYLLVPSRRlVKLPRGLDPVEAA---PLADAglt 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 152 -VHGVEEV--DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAG 228
Cdd:cd05284   154 aYHAVKKAlpYLDPGSTVVVIGVGGLGHIAVQILRALTPATVIAVDRSEEALKLAERLGADHVLNASDDVVEEVRELTGG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 229 GPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVpdqEATMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDa 308
Cdd:cd05284   234 RGADAVIDFVGSDETLALAAKLLAKGGRYVIVGY---GGHGRLPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKVK- 309

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1806958860 309 daLVTERIGLEDLPTAFERMGNAEGL-KKVVVP 340
Cdd:cd05284   310 --VEITKFPLEDANEALDRLREGRVTgRAVLVP 340
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 1-339 5.52e-55

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: 183.73  E-value: 5.52e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVG---------EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDV 71
Cdd:cd08281     1 MRAAVLRETGaptpyadsrPLVIEEVELDPPGPGEVLVKIAAAGLCHSDLSVINGDRPRPLPMALGHEAAGVVVEVGEGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  72 AGFEVGDRVAINPTVPCNACSYCKRGETHLCENNTSIGGAGeTILDG------------------AFAEYVRVPAINVED 133
Cdd:cd08281    81 TDLEVGDHVVLVFVPSCGHCRPCAEGRPALCEPGAAANGAG-TLLSGgrrlrlrggeinhhlgvsAFAEYAVVSRRSVVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 134 I-GEMSFEHAALaepLACCV-HGVEEV----DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELG 207
Cdd:cd08281   160 IdKDVPLEIAAL---FGCAVlTGVGAVvntaGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAVDLNEDKLALARELG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 208 ADAVVDPNEDDPEAAIPAAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSF 287
Cdd:cd08281   237 ATATVNAGDPNAVEQVRELTGGGVDYAFEMAGSVPALETAYEITRRGGTTVTAGLPDPEARLSVPALSLVAEERTLKGSY 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1806958860 288 ---SLTTEDFERAVTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08281   317 mgsCVPRRDIPRYLALYLSGRLPVDKLLTHRLPLDEINEGFDRLAAGEAVRQVIL 371
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 11-337 6.74e-55

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 182.96  E-value: 6.74e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  11 EIAVEERErPEPAADEVLVQVGACGVCMTDYHMYH----GTFAVETPLVLGHESAGTVAEVgdDVAGFEVGDRVAINPTV 86
Cdd:PRK09880   15 DVAVTEQE-IEWNNNGTLVQITRGGICGSDLHYYQegkvGNFVIKAPMVLGHEVIGKIVHS--DSSGLKEGQTVAINPSK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  87 PCNACSYCKRGETHLCENNTSIGGAGETI-LDGAFAEYVRVPAINVEDIGEMSFEHA-ALAEPLACCVHGVEEVDVKPGD 164
Cdd:PRK09880   92 PCGHCKYCLSHNENQCTTMRFFGSAMYFPhVDGGFTRYKVVDTAQCIPYPEKADEKVmAFAEPLAVAIHAAHQAGDLQGK 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 165 SVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDpeAAIPAAAGGPVDVGAEAIGLVPTI 244
Cdd:PRK09880  172 RVFVSGVGPIGCLIVAAVKTLGAAEIVCADVSPRSLSLAREMGADKLVNPQNDD--LDHYKAEKGYFDVSFEVSGHPSSI 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 245 EQANAVTAPGGSTLVFG----VPDQEATMEISpfdvffDEVGYRGSFSLTTEdFERAVTLLRYGRVDADALVTERIGLED 320
Cdd:PRK09880  250 NTCLEVTRAKGVMVQVGmggaPPEFPMMTLIV------KEISLKGSFRFTEE-FNTAVSWLANGVINPLPLLSAEYPFTD 322

                         330
                  ....*....|....*..
gi 1806958860 321 LPTAFERMGNAEGLKKV 337
Cdd:PRK09880  323 LEEALIFAGDKTQAAKV 339
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-339 5.67e-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. 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: 181.03  E-value: 5.67e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVG-EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDV---AGFEV 76
Cdd:cd08263     1 MKAAVLKGPNpPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELPFPPPFVLGHEISGEVVEVGPNVenpYGLSV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  77 GDRVAINPTVPCNACSYCKRGETHLCENNTSIGGAGETILD------------------GAFAEYVRVPAINVEDIGEmS 138
Cdd:cd08263    81 GDRVVGSFIMPCGKCRYCARGKENLCEDFFAYNRLKGTLYDgttrlfrldggpvymysmGGLAEYAVVPATALAPLPE-S 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 139 FEHAALAePLACCV---HG--VEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVD 213
Cdd:cd08263   160 LDYTESA-VLGCAGftaYGalKHAADVRPGETVAVIGVGGVGSSAIQLAKAFGASPIIAVDVRDEKLAKAKELGATHTVN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 214 PN-EDDPEAAIPAAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTTE 292
Cdd:cd08263   239 AAkEDAVAAIREITGGRGVDVVVEALGKPETFKLALDVVRDGGRAVVVGLAPGGATAEIPITRLVRRGIKIIGSYGARPR 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1806958860 293 -DFERAVTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08263   319 qDLPELVGLAASGKLDPEALVTHKYKLEEINEAYENLRKGLIHGRAIV 366
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 1-339 3.55e-51

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: 173.58  E-value: 3.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETP-LVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:cd08285     1 MKAFAMLGIGKVGWIEKPIPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHgMILGHEAVGVVEEVGSEVKDFKPGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSiGGAGETILDGAFAEYVRVPA--INVEDIGE-MSFEHAA-LAEPLACCVHGV 155
Cdd:cd08285    81 VIVPAITPDWRSVAAQRGYPSQSGGMLG-GWKFSNFKDGVFAEYFHVNDadANLAPLPDgLTDEQAVmLPDMMSTGFHGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 156 EEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPVDVG 234
Cdd:cd08285   160 ELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAVGSRPNRVELAKEYGATDIVDYKNGDVvEQILKLTGGKGVDAV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 235 AEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTT---EDFERAVTLLRYGRVDADAL 311
Cdd:cd08285   240 IIAGGGQDTFEQALKVLKPGGTISNVNYYGEDDYLPIPREEWGVGMGHKTINGGLCPggrLRMERLASLIEYGRVDPSKL 319

                         330       340       350
                  ....*....|....*....|....*....|
gi 1806958860 312 VTERI-GLEDLPTAFERMGNAE-GLKKVVV 339
Cdd:cd08285   320 LTHHFfGFDDIEEALMLMKDKPdDLIKPVI 349
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 2-339 1.91e-50

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: 171.85  E-value: 1.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   2 RASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRV 80
Cdd:cd05279     2 KAAVLWEKGKpLSIEEIEVAPPKAGEVRIKVVATGVCHTDLHVIDGKLPTPLPVILGHEGAGIVESIGPGVTTLKPGDKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  81 AINPTVPCNACSYCKRGETHLCENNTSIGGAGEtILDG------------------AFAEYVRVPAINVEDI-GEMSFEH 141
Cdd:cd05279    82 IPLFGPQCGKCKQCLNPRPNLCSKSRGTNGRGL-MSDGtsrftckgkpihhflgtsTFAEYTVVSEISLAKIdPDAPLEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 142 AALaepLACCVH-----GVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNE 216
Cdd:cd05279   161 VCL---IGCGFStgygaAVNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAVDINKDKFEKAKQLGATECINPRD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 217 --DDPEAAIPAAAGGPVDVGAEAIGLVPTIEQANAVTAP-GGSTLVFGVPDQEATMEISPFDVFFDEV---GYRGSFSLt 290
Cdd:cd05279   238 qdKPIVEVLTEMTDGGVDYAFEVIGSADTLKQALDATRLgGGTSVVVGVPPSGTEATLDPNDLLTGRTikgTVFGGWKS- 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1806958860 291 TEDFERAVTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd05279   317 KDSVPKLVALYRQKKFPLDELITHVLPFEEINDGFDLMRSGESIRTILT 365
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 1-307 2.98e-50

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: 170.87  E-value: 2.98e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVE-ERERPEPAADEVLVQVGACGVCMTDYHMYHGTF-------------AVETPLVLGHESAGTVAE 66
Cdd:cd08240     1 MKAAAVVEPGKPLEEvEIDTPKPPGTEVLVKVTACGVCHSDLHIWDGGYdlgggktmslddrGVKLPLVLGHEIVGEVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  67 VGDDVAGFEVGDRVAINPTVPCNACSYCKRGETHLCENNTSIGGagetILDGAFAEYVRVPAIN-VEDIGEMSFehaALA 145
Cdd:cd08240    81 VGPDAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRALGI----FQDGGYAEYVIVPHSRyLVDPGGLDP---ALA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 146 EPLAC----CVHGVEEVDVKPGD-SVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPE 220
Cdd:cd08240   154 ATLACsgltAYSAVKKLMPLVADePVVIIGAGGLGLMALALLKALGPANIIVVDIDEAKLEAAKAAGADVVVNGSDPDAA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 221 AAIPAAAGGPVD-----VGAEAiglvpTIEQANAVTAPGGSTLVFGVPDQEATMEIsPFDVfFDEVGYRGSFSLTTEDFE 295
Cdd:cd08240   234 KRIIKAAGGGVDavidfVNNSA-----TASLAFDILAKGGKLVLVGLFGGEATLPL-PLLP-LRALTIQGSYVGSLEELR 306

                         330
                  ....*....|..
gi 1806958860 296 RAVTLLRYGRVD 307
Cdd:cd08240   307 ELVALAKAGKLK 318
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 11-327 3.43e-50

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: 171.93  E-value: 3.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  11 EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHG--------TFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAI 82
Cdd:cd08265    38 ELRVEDVPVPNLKPDEILIRVKACGICGSDIHLYETdkdgyilyPGLTEFPVVIGHEFSGVVEKTGKNVKNFEKGDPVTA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  83 NPTVPCNACSYCKRGETHLCENNTSIGGAgetiLDGAFAEYVRVPAINVEDIGEM--------SFEHAALAEPLACCVHG 154
Cdd:cd08265   118 EEMMWCGMCRACRSGSPNHCKNLKELGFS----ADGAFAEYIAVNARYAWEINELreiysedkAFEAGALVEPTSVAYNG 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 155 VEEV--DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP----EAAIPAAAG 228
Cdd:cd08265   194 LFIRggGFRPGAYVVVYGAGPIGLAAIALAKAAGASKVIAFEISEERRNLAKEMGADYVFNPTKMRDclsgEKVMEVTKG 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 229 GPVDVGAEAIGLVP-TIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDE-VGYRGSFSLTTedFERAVTLLRYGRV 306
Cdd:cd08265   274 WGADIQVEAAGAPPaTIPQMEKSIAINGKIVYIGRAATTVPLHLEVLQVRRAQiVGAQGHSGHGI--FPSVIKLMASGKI 351

                         330       340
                  ....*....|....*....|.
gi 1806958860 307 DADALVTERIGLEDLPTAFER 327
Cdd:cd08265   352 DMTKIITARFPLEGIMEAIKA 372
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 2-331 1.63e-49

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 169.57  E-value: 1.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   2 RASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYH----GTFAVETPLVLGHESAGTVAEVGDDVAGFEVG 77
Cdd:PLN02702   19 MAAWLVGVNTLKIQPFKLPPLGPHDVRVRMKAVGICGSDVHYLKtmrcADFVVKEPMVIGHECAGIIEEVGSEVKHLVVG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  78 DRVAINPTVPCNACSYCKRGETHLCENNTSIGGAGetiLDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVE 156
Cdd:PLN02702   99 DRVALEPGISCWRCNLCKEGRYNLCPEMKFFATPP---VHGSLANQVVHPADLCFKLPEnVSLEEGAMCEPLSVGVHACR 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 157 EVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAV--VDPNEDDPEAAIPA---AAGGPV 231
Cdd:PLN02702  176 RANIGPETNVLVMGAGPIGLVTMLAARAFGAPRIVIVDVDDERLSVAKQLGADEIvlVSTNIEDVESEVEEiqkAMGGGI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVF-FDEVG---YRGSFSLTTEdferavtLLRYGRVD 307
Cdd:PLN02702  256 DVSFDCVGFNKTMSTALEATRAGGKVCLVGMGHNEMTVPLTPAAAReVDVVGvfrYRNTWPLCLE-------FLRSGKID 328

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 308 ADALVTERIGL--EDLPTAFE---RMGNA 331
Cdd:PLN02702  329 VKPLITHRFGFsqKEVEEAFEtsaRGGNA 357
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 1-338 2.19e-49

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: 169.31  E-value: 2.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADE-VLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:cd08282     1 MKAVVYGGPGNVAVEDVPDPKIEHPTdAIVRITTTAICGSDLHMYRGRTGAEPGLVLGHEAMGEVEEVGSAVESLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENN------TSIGGAGETILDGAFAEYVRVP-------AINVEDIGEMSFEHAALAE 146
Cdd:cd08282    81 VVVPFNVACGRCRNCKRGLTGVCLTVnpgragGAYGYVDMGPYGGGQAEYLRVPyadfnllKLPDRDGAKEKDDYLMLSD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 147 PLACCVHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAvVDPNEDDPEAAIPAA 226
Cdd:cd08282   161 IFPTGWHGLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGASRVYVVDHVPERLDLAESIGAIP-IDFSDGDPVEQILGL 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 227 AGGPVD-----VGAEAIGL----VP--TIEQANAVTAPGGSTLVFGV---------PDQEATMEIS-PFDVFFdevgyRG 285
Cdd:cd08282   240 EPGGVDravdcVGYEARDRggeaQPnlVLNQLIRVTRPGGGIGIVGVyvaedpgagDAAAKQGELSfDFGLLW-----AK 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1806958860 286 SFSLTT-----EDFERA-VTLLRYGRVDADALVTERIGLEDLPTAFERMgNAEGLKKVV 338
Cdd:cd08282   315 GLSFGTgqapvKKYNRQlRDLILAGRAKPSFVVSHVISLEDAPEAYARF-DKRLETKVV 372
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-340 3.27e-49

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: 167.42  E-value: 3.27e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAveTPLVLGHESAGTVAEVGDdvaGFEVGDRV 80
Cdd:cd08242     1 MKALVLDGGLDLRVEDLPKPEPPPGEALVRVLLAGICNTDLEIYKGYYP--FPGVPGHEFVGIVEEGPE---AELVGKRV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  81 A--INptVPCNACSYCKRGETHLCENNTSIGGAGetiLDGAFAEYVRVPAINVEDI-GEMSFEHAALAEPLACCVHGVEE 157
Cdd:cd08242    76 VgeIN--IACGRCEYCRRGLYTHCPNRTVLGIVD---RDGAFAEYLTLPLENLHVVpDLVPDEQAVFAEPLAAALEILEQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 158 VDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGAdAVVDPNEDDPEaaipaaaGGPVDVGAEA 237
Cdd:cd08242   151 VPITPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGR-HSEKLALARRLGV-ETVLPDEAESE-------GGGFDVVVEA 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 238 IGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVffDEVGYRGSfslTTEDFERAVTLLRYGRVDADALVTERIG 317
Cdd:cd08242   222 TGSPSGLELALRLVRPRGTVVLKSTYAGPASFDLTKAVV--NEITLVGS---RCGPFAPALRLLRKGLVDVDPLITAVYP 296

                         330       340
                  ....*....|....*....|...
gi 1806958860 318 LEDLPTAFERMGNAEGLKKVVVP 340
Cdd:cd08242   297 LEEALEAFERAAEPGALKVLLRP 319
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 6-339 2.94e-48

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: 164.84  E-value: 2.94e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   6 LTDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYH-MYHGT---FAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVA 81
Cdd:cd08269     1 LTGPGRFEVEEHPRPTPGPGQVLVRVEGCGVCGSDLPaFNQGRpwfVYPAEPGGPGHEGWGRVVALGPGVRGLAVGDRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  82 InptvpcnacsyckrgethlcenntsiggagetILDGAFAEYVRVPAINVEDIGEMSFEHAALAEPLACCVHGVEEVDVK 161
Cdd:cd08269    81 G--------------------------------LSGGAFAEYDLADADHAVPLPSLLDGQAFPGEPLGCALNVFRRGWIR 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 162 PGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVV-DPNEDDPEAAIPAAAGGPVDVGAEAIGL 240
Cdd:cd08269   129 AGKTVAVIGAGFIGLLFLQLAAAAGARRVIAIDRRPARLALARELGATEVVtDDSEAIVERVRELTGGAGADVVIEAVGH 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 241 VPTIEQANAVTAPGGSTLVFGVPDQEatmeisPFDVFFDEVGYRG---------SFSLTTEDFERAVTLLRYGRVDADAL 311
Cdd:cd08269   209 QWPLDLAGELVAERGRLVIFGYHQDG------PRPVPFQTWNWKGidlinaverDPRIGLEGMREAVKLIADGRLDLGSL 282

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 312 VTERIGLEDLPTAFERMGNA-EGLKKVVV 339
Cdd:cd08269   283 LTHEFPLEELGDAFEAARRRpDGFIKGVI 311
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 14-339 1.16e-46

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: 161.90  E-value: 1.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  14 VEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVpCNACSY 93
Cdd:cd08278    17 LEDVELDDPRPDEVLVRIVATGICHTDLVVRDGGLPTPLPAVLGHEGAGVVEAVGSAVTGLKPGDHVVLSFAS-CGECAN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  94 CKRGETHLCENNTSIGGAGeTILDGA--------------------FAEYVRVPAINVEDIGEMsfEHAALAEPLACcvh 153
Cdd:cd08278    96 CLSGHPAYCENFFPLNFSG-RRPDGStplslddgtpvhghffgqssFATYAVVHERNVVKVDKD--VPLELLAPLGC--- 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 GV--------EEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPA 225
Cdd:cd08278   170 GIqtgagavlNVLKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAVDIVDSRLELAKELGATHVINPKEEDLVAAIRE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 226 AAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGS---FSLTTEDFERAVTLLR 302
Cdd:cd08278   250 ITGGGVDYALDTTGVPAVIEQAVDALAPRGTLALVGAPPPGAEVTLDVNDLLVSGKTIRGViegDSVPQEFIPRLIELYR 329

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1806958860 303 YGRVDADALVTERiGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08278   330 QGKFPFDKLVTFY-PFEDINQAIADSESGKVIKPVLR 365
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 1-339 1.37e-46

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 160.97  E-value: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE-IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:PRK13771    1 MKAVILPGFKQgYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPrMKYPVILGHEVVGTVEEVGENVKGFKPGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENNTSIGGAgetiLDGAFAEYVRVPAINVEDIGE-MSFEHAALAeplACC----VH 153
Cdd:PRK13771   81 RVASLLYAPDGTCEYCRSGEEAYCKNRLGYGEE----LDGFFAEYAKVKVTSLVKVPPnVSDEGAVIV---PCVtgmvYR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 GVEEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAApiVVSELDDERRELAAELGADAVVDPNEDDPEaaipAAAGGPVD 232
Cdd:PRK13771  154 GLRRAGVKKGETVLVTGAgGGVGIHAIQVAKALGAK--VIAVTSSESKAKIVSKYADYVIVGSKFSEE----VKKIGGAD 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 233 VGAEAIGlVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVdaDALV 312
Cdd:PRK13771  228 IVIETVG-TPTLEESLRSLNMGGKIIQIGNVDPSPTYSLRLGYIILKDIEIIGHISATKRDVEEALKLVAEGKI--KPVI 304

                         330       340
                  ....*....|....*....|....*..
gi 1806958860 313 TERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:PRK13771  305 GAEVSLSEIDKALEELKDKSRIGKILV 331
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 1-339 1.47e-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: 1.47e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPE-PAADEVLVQVGACGVCMTDYHMYHGTFAVETP-LVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd08286     1 MKALVYHGPGKISWEDRPKPTiQEPTDAIVKMLKTTICGTDLHILKGDVPTVTPgRILGHEGVGVVEEVGSAVTNFKVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENntsiGG--AGETIlDGAFAEYVRVP-----------AINVEDIGEMSfehAALA 145
Cdd:cd08286    81 RVLISCISSCGTCGYCRKGLYSHCES----GGwiLGNLI-DGTQAEYVRIPhadnslyklpeGVDEEAAVMLS---DILP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 146 EPLACcvhGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP-EAAIP 224
Cdd:cd08286   153 TGYEC---GVLNGKVKPGDTVAIVGAGPVGLAALLTAQLYSPSKIIMVDLDDNRLEVAKKLGATHTVNSAKGDAiEQVLE 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 225 AAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEIspfDVFFDE---VGYRGSFSLTTEDFERAVTll 301
Cdd:cd08286   230 LTDGRGVDVVIEAVGIPATFELCQELVAPGGHIANVGVHGKPVDLHL---EKLWIKnitITTGLVDTNTTPMLLKLVS-- 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1806958860 302 rYGRVDADALVTERIGLEDLPTAFERMGNAEGLK--KVVV 339
Cdd:cd08286   305 -SGKLDPSKLVTHRFKLSEIEKAYDTFSAAAKHKalKVII 343
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 1-339 2.75e-45

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: 157.80  E-value: 2.75e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE---IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGT--FAVETPLVLGHESAGTVAEVGDDVAGFE 75
Cdd:cd08266     1 MKAVVIRGHGGpevLEYGDLPEPEPGPDEVLVRVKAAALNHLDLWVRRGMpgIKLPLPHILGSDGAGVVEAVGPGVTNVK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVAINPTVPCNACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGE-MSFEHAAlAEPLaccVHG 154
Cdd:cd08266    81 PGQRVVIYPGISCGRCEYCLAGRENLCAQYGILG----EHVDGGYAEYVAVPARNLLPIPDnLSFEEAA-AAPL---TFL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 155 ------VEEVDVKPGDSVAIIGAGP-IGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVDP-NEDDPEAAIPAA 226
Cdd:cd08266   153 tawhmlVTRARLRPGETVLVHGAGSgVGSAAIQIAKLFGATVIATAG-SEDKLERAKELGADYVIDYrKEDFVREVRELT 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 227 AGGPVDVGAEAIGLVpTIEQANAVTAPGGSTLVFGVpdqeATMEISPFD---VFFDEVGYRGSFSLTTEDFERAVTLLRY 303
Cdd:cd08266   232 GKRGVDVVVEHVGAA-TWEKSLKSLARGGRLVTCGA----TTGYEAPIDlrhVFWRQLSILGSTMGTKAELDEALRLVFR 306

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1806958860 304 GRVdaDALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08266   307 GKL--KPVIDSVFPLEEAAEAHRRLESREQFGKIVL 340
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 14-328 2.78e-43

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: 152.09  E-value: 2.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  14 VEERERPEPAADEVLVQVGACGVCMTDYHMYHGT-FAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTV-PCNAC 91
Cdd:cd08245    14 PEEVPVPEPGPGEVLIKIEACGVCHTDLHAAEGDwGGSKYPLVPGHEIVGEVVEVGAGVEGRKVGDRVGVGWLVgSCGRC 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  92 SYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGE-MSFEHAAlaePLACC----VHGVEEVDVKPGDSV 166
Cdd:cd08245    94 EYCRRGLENLCQKAVNTG----YTTQGGYAEYMVADAEYTVLLPDgLPLAQAA---PLLCAgitvYSALRDAGPRPGERV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 167 AIIGAGPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVGAEaiglVPTIEQ 246
Cdd:cd08245   167 AVLGIGGLGHLAVQYARAMGFETVAITR-SPDKRELARKLGADEVVDSGAELDEQAAAGGADVILVTVVS----GAAAEA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 247 ANAVTAPGGSTLVFGVPDQEaTMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADalvTERIGLEDLPTAFE 326
Cdd:cd08245   242 ALGGLRRGGRIVLVGLPESP-PFSPDIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVKPM---IETFPLDQANEAYE 317


                  ..
gi 1806958860 327 RM 328
Cdd:cd08245   318 RM 319
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 12-338 9.26e-43

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: 151.72  E-value: 9.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  12 IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVaINPTVP-CNA 90
Cdd:cd08277    15 LVIEEIEVAPPKANEVRIKMLATSVCHTDILAIEGFKATLFPVILGHEGAGIVESVGEGVTNLKPGDKV-IPLFIGqCGE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  91 CSYCKRGETHLCENNTSIGGA------------GETILD----GAFAEYVRVPAINVEDIGEMS-FEHAALaepLACCV- 152
Cdd:cd08277    94 CSNCRSGKTNLCQKYRANESGlmpdgtsrftckGKKIYHflgtSTFSQYTVVDENYVAKIDPAApLEHVCL---LGCGFs 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 --HG--VEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDD--PEAAIPAA 226
Cdd:cd08277   171 tgYGaaWNTAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGVDINEDKFEKAKEFGATDFINPKDSDkpVSEVIREM 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 227 AGGPVDVGAEAIGLVPTIEQANAVTAPG-GSTLVFGVPDqEATMEISPFDV---------FFDevGYRGSFSLTtedfeR 296
Cdd:cd08277   251 TGGGVDYSFECTGNADLMNEALESTKLGwGVSVVVGVPP-GAELSIRPFQLilgrtwkgsFFG--GFKSRSDVP-----K 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1806958860 297 AVTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVV 338
Cdd:cd08277   323 LVSKYMNKKFDLDELITHVLPFEEINKGFDLMKSGECIRTVI 364
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 14-332 1.28e-42

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: 150.47  E-value: 1.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  14 VEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEVGDRVAinptVP----- 87
Cdd:cd08296    15 LVERDVPLPGPGEVLIKVEACGVCHSDAFVKEGAMPgLSYPRVPGHEVVGRIDAVGEGVSRWKVGDRVG----VGwhggh 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  88 CNACSYCKRGETHLCENNTSIGGAgetiLDGAFAEYVRVPAINVEDIGE-MSFEHAAlaePLACC----VHGVEEVDVKP 162
Cdd:cd08296    91 CGTCDACRRGDFVHCENGKVTGVT----RDGGYAEYMLAPAEALARIPDdLDAAEAA---PLLCAgvttFNALRNSGAKP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 163 GDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVDPNEDDPEAAIPAAAggpvdvGAEAIglVP 242
Cdd:cd08296   164 GDLVAVQGIGGLGHLAVQYAAKMGFRTVAISR-GSDKADLARKLGAHHYIDTSKEDVAEALQELG------GAKLI--LA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 243 TIEQANAVT------APGGSTLVFGVPDQeaTMEISPFDVFFDEVGYRGSFSLTTEDFERAvtlLRYGRVDADALVTERI 316
Cdd:cd08296   235 TAPNAKAISalvgglAPRGKLLILGAAGE--PVAVSPLQLIMGRKSIHGWPSGTALDSEDT---LKFSALHGVRPMVETF 309

                         330
                  ....*....|....*.
gi 1806958860 317 GLEDLPTAFERMGNAE 332
Cdd:cd08296   310 PLEKANEAYDRMMSGK 325
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 25-131 5.07e-42

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: 141.59  E-value: 5.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  25 DEVLVQVGACGVCMTDYHMYHGT-FAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCNACSYCKRGETHLCE 103
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGnPPVKLPLILGHEFAGEVVEVGPGVTGLKVGDRVVVEPLIPCGKCEYCREGRYNLCP 80

                          90       100
                  ....*....|....*....|....*...
gi 1806958860 104 NNTSIGgageTILDGAFAEYVRVPAINV 131
Cdd:pfam08240  81 NGRFLG----YDRDGGFAEYVVVPERNL 104
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 1-340 1.54e-41

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: 148.84  E-value: 1.54e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERerPEPA---ADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDVAGFEV 76
Cdd:cd08283     1 MKALVWHGKGDVRVEEV--PDPKiedPTDAIVRVTATAICGSDLHLYHGYIPgMKKGDILGHEFMGVVEEVGPEVRNLKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  77 GDRVAINPTVPCNACSYCKRGETHLCEN-NTS------IGGAGETIL---------DGAFAEYVRVP-----AINVEDig 135
Cdd:cd08283    79 GDRVVVPFTIACGECFYCKRGLYSQCDNtNPSaemaklYGHAGAGIFgyshltggyAGGQAEYVRVPfadvgPFKIPD-- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 136 EMSFEHAA-LAEPLACCVHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDP 214
Cdd:cd08283   157 DLSDEKALfLSDILPTGYHAAELAEVKPGDTVAVWGCGPVGLFAARSAKLLGAERVIAIDRVPERLEMARSHLGAETINF 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 215 NEDD--PEAAIPAAAGGPVDVGAEAIGLvptieqaNAVTAPGGStlvfgVPDQEATMEISPFDVF---------FDEVGY 283
Cdd:cd08283   237 EEVDdvVEALRELTGGRGPDVCIDAVGM-------EAHGSPLHK-----AEQALLKLETDRPDALreaiqavrkGGTVSI 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 284 RGSFSLTTEDF------ERAVTL-------LRY----------GRVDADALVTERIGLEDLPTAFERMGNAE--GLKKVV 338
Cdd:cd08283   305 IGVYGGTVNKFpigaamNKGLTLrmgqthvQRYlprlleliesGELDPSFIITHRLPLEDAPEAYKIFDKKEdgCIKVVL 384


                  ..
gi 1806958860 339 VP 340
Cdd:cd08283   385 KP 386
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1-339 6.90e-41

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: 145.68  E-value: 6.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE---IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAV--ETPLVLGHESAGTVAEVGDDVAGFE 75
Cdd:COG0604     1 MKAIVITEFGGpevLELEEVPVPEPGPGEVLVRVKAAGVNPADLLIRRGLYPLppGLPFIPGSDAAGVVVAVGEGVTGFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVAINPTvpcnacsyckrgethlcenntsiggagetilDGAFAEYVRVPAINVEDIGE-MSFEHAAlAEPLACCV-- 152
Cdd:COG0604    81 VGDRVAGLGR-------------------------------GGGYAEYVVVPADQLVPLPDgLSFEEAA-ALPLAGLTaw 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 HGVEEV-DVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPI-VVSelDDERRELAAELGADAVVDPNEDD-PEAAIPAAAG 228
Cdd:COG0604   129 QALFDRgRLKPGETVLVHGAaGGVGSAAVQLAKALGARVIaTAS--SPEKAELLRALGADHVIDYREEDfAERVRALTGG 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 229 GPVDVGAEAIGlVPTIEQANAVTAPGGSTLVFGVPDQEATmEISPFDVFFDEVGYRGSFSLTT------EDFERAVTLLR 302
Cdd:COG0604   207 RGVDVVLDTVG-GDTLARSLRALAPGGRLVSIGAASGAPP-PLDLAPLLLKGLTLTGFTLFARdpaerrAALAELARLLA 284

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1806958860 303 YGRVdaDALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:COG0604   285 AGKL--RPVIDRVFPLEEAAEAHRLLESGKHRGKVVL 319
PRK10083 PRK10083
putative oxidoreductase; Provisional
 11-326 9.37e-40

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 142.96  E-value: 9.37e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  11 EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHG--TFAvETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPC 88
Cdd:PRK10083   11 SLAIEERPIPQPAAGEVRVKVKLAGICGSDSHIYRGhnPFA-KYPRVIGHEFFGVIDAVGEGVDAARIGERVAVDPVISC 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  89 NACSYCKRGETHLCENNTSIGgageTILDGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHGVEEVDVKPGDSVA 167
Cdd:PRK10083   90 GHCYPCSIGKPNVCTSLVVLG----VHRDGGFSEYAVVPAKNAHRIPDaIADQYAVMVEPFTIAANVTGRTGPTEQDVAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 168 IIGAGPIGLLLLQAFRNA-GAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIpaaaggpvdvgaEAIGLVPT--- 243
Cdd:PRK10083  166 IYGAGPVGLTIVQVLKGVyNVKAVIVADRIDERLALAKESGADWVINNAQEPLGEAL------------EEKGIKPTlii 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 244 --------IEQANAVTAPGGSTLVFG-------VPDQEAT-MEISPFdvffdevgyrgSFSLTTEDFERAVTLLRYGRVD 307
Cdd:PRK10083  234 daachpsiLEEAVTLASPAARIVLMGfssepseIVQQGITgKELSIF-----------SSRLNANKFPVVIDWLSKGLID 302

                         330
                  ....*....|....*....
gi 1806958860 308 ADALVTERIGLEDLPTAFE 326
Cdd:PRK10083  303 PEKLITHTFDFQHVADAIE 321
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-332 2.41e-39

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: 141.55  E-value: 2.41e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIA-----VEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVGDDVAGF 74
Cdd:cd08298     1 MKAMVLEKPGPIEenplrLTEVPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKlPLIPGHEIVGRVEAVGPGVTRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  75 EVGDRVAINP---TvpCNACSYCKRGETHLCENNTSiggAGETIlDGAFAEYVRVPAINVEDIGE-MSFEHAAlaePLAC 150
Cdd:cd08298    81 SVGDRVGVPWlgsT--CGECRYCRSGRENLCDNARF---TGYTV-DGGYAEYMVADERFAYPIPEdYDDEEAA---PLLC 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 151 C----VHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVDPNEDDPEAAIPAA 226
Cdd:cd08298   152 AgiigYRALKLAGLKPGQRLGLYGFGASAHLALQIARYQGAEVFAFTR-SGEHQELARELGADWAGDSDDLPPEPLDAAI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 227 aggpvdVGAEAIGLVPtieQANAVTAPGGsTLVFGVPdQEATMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRV 306
Cdd:cd08298   231 ------IFAPVGALVP---AALRAVKKGG-RVVLAGI-HMSDIPAFDYELLWGEKTIRSVANLTRQDGEEFLKLAAEIPI 299

                         330       340
                  ....*....|....*....|....*.
gi 1806958860 307 DAdalVTERIGLEDLPTAFERMGNAE 332
Cdd:cd08298   300 KP---EVETYPLEEANEALQDLKEGR 322
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 1-340 1.89e-36

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: 134.36  E-value: 1.89e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERP---EPaaDEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVG 77
Cdd:cd08287     1 MRATVIHGPGDIRVEEVPDPvieEP--TDAVIRVVATCVCGSDLWPYRGVSPTRAPAPIGHEFVGVVEEVGSEVTSVKPG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  78 DRVAINPTVPCNACSYCKRGETHLCENntsiGGAGETILDGAFAEYVRVP---------AINVEDIGEMSFEHAALAEPL 148
Cdd:cd08287    79 DFVIAPFAISDGTCPFCRAGFTTSCVH----GGFWGAFVDGGQGEYVRVPladgtlvkvPGSPSDDEDLLPSLLALSDVM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 149 ACCVHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGA-DAVVDPNEDDPEAAIPAAA 227
Cdd:cd08287   155 GTGHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAMSRHEDRQALAREFGAtDIVAERGEEAVARVRELTG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 228 GGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEatMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVD 307
Cdd:cd08287   235 GVGADAVLECVGTQESMEQAIAIARPGGRVGYVGVPHGG--VELDVRELFFRNVGLAGGPAPVRRYLPELLDDVLAGRIN 312

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1806958860 308 ADALVTERIGLEDLPTAFERMGNAEGLKKVVVP 340
Cdd:cd08287   313 PGRVFDLTLPLDEVAEGYRAMDERRAIKVLLRP 345
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 1-339 2.79e-35

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: 131.57  E-value: 2.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALT-DVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETP----LVLGHESAGTVAEVGDDvAGFE 75
Cdd:cd08230     1 MKAIAVKpGKPGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDREIVAGEYGTAPPgedfLVLGHEALGVVEEVGDG-SGLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVAinPTV--PCNACSYCKRGETHLCENNTSIgGAGETILDGAFAEYVRVPAINVEDIGEMSFEHAALAEPLACCVH 153
Cdd:cd08230    80 PGDLVV--PTVrrPPGKCLNCRIGRPDFCETGEYT-ERGIKGLHGFMREYFVDDPEYLVKVPPSLADVGVLLEPLSVVEK 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 GVEEVD-------VKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVS--ELDDERRELAAELGADAVVDPNEDDPEaaip 224
Cdd:cd08230   157 AIEQAEavqkrlpTWNPRRALVLGAGPIGLLAALLLRLRGFEVYVLNrrDPPDPKADIVEELGATYVNSSKTPVAE---- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 225 AAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEIsPFDVFFDEVGYR-----GSFSLTTEDFERAVT 299
Cdd:cd08230   233 VKLVGEFDLIIEATGVPPLAFEALPALAPNGVVILFGVPGGGREFEV-DGGELNRDLVLGnkalvGSVNANKRHFEQAVE 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1806958860 300 LL-----RYGRVdADALVTERIGLEDLPTAFERmgNAEGLKKVVV 339
Cdd:cd08230   312 DLaqwkyRWPGV-LERLITRRVPLEEFAEALTE--KPDGEIKVVI 353
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 1-328 6.20e-34

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 127.46  E-value: 6.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEI-AVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:PRK09422    1 MKAAVVNKDHTGdVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANGDFGDKTGRILGHEGIGIVKEVGPGVTSLKVGDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVP-CNACSYCKRGETHLCENntsIGGAGETIlDGAFAEYVRVP---AINVEDigemSFEHAAlAEPLAC----C 151
Cdd:PRK09422   81 VSIAWFFEgCGHCEYCTTGRETLCRS---VKNAGYTV-DGGMAEQCIVTadyAVKVPE----GLDPAQ-ASSITCagvtT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 152 VHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPV 231
Cdd:PRK09422  152 YKAIKVSGIKPGQWIAIYGAGGLGNLALQYAKNVFNAKVIAVDINDDKLALAKEVGADLTINSKRVEDVAKIIQEKTGGA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DvgAEAIGLVPTI--EQANAVTAPGGSTLVFGVPDQeaTMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVdad 309
Cdd:PRK09422  232 H--AAVVTAVAKAafNQAVDAVRAGGRVVAVGLPPE--SMDLSIPRLVLDGIEVVGSLVGTRQDLEEAFQFGAEGKV--- 304

                         330
                  ....*....|....*....
gi 1806958860 310 ALVTERIGLEDLPTAFERM 328
Cdd:PRK09422  305 VPKVQLRPLEDINDIFDEM 323
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
1-339 9.03e-34

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 127.26  E-value: 9.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERERPE-PAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDR 79
Cdd:PRK10309    1 MKSVVNDTDGIVRVAESPIPEiKHQDDVLVKVASSGLCGSDIPRIFKNGAHYYPITLGHEFSGYVEAVGSGVDDLHPGDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  80 VAINPTVPCNACSYCKRGETHLCENNTSIGGAGEtildGAFAEYVRVPAINVEDI-GEMSFEHAALAEPLACCVHGVEEV 158
Cdd:PRK10309   81 VACVPLLPCFTCPECLRGFYSLCAKYDFIGSRRD----GGNAEYIVVKRKNLFALpTDMPIEDGAFIEPITVGLHAFHLA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 159 DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVD-VGAEA 237
Cdd:PRK10309  157 QGCEGKNVIIIGAGTIGLLAIQCAVALGAKSVTAIDINSEKLALAKSLGAMQTFNSREMSAPQIQSVLRELRFDqLILET 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 238 IGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFD-VFFDEVGYRGSFSLTT-----EDFERAVTLLRYGRVDADAL 311
Cdd:PRK10309  237 AGVPQTVELAIEIAGPRAQLALVGTLHHDLHLTSATFGkILRKELTVIGSWMNYSspwpgQEWETASRLLTERKLSLEPL 316

                         330       340
                  ....*....|....*....|....*...
gi 1806958860 312 VTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:PRK10309  317 IAHRGSFESFAQAVRDLAGNPMPGKVLL 344
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 1-220 5.18e-33

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: 124.77  E-value: 5.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVG--EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd08264     1 MKALVFEKSGieNLKVEDVKDPKPGPGEVLIRVKMAGVNPVDYNVINAVKVKPMPHIPGAEFAGVVEEVGDHVKGVKKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVAINPTVPCNACSYCKRGETHLCENntsiGGAGETILDGAFAEYVRVPAINVEDIGEMSFEHAALAEPLACCV--HGVE 156
Cdd:cd08264    81 RVVVYNRVFDGTCDMCLSGNEMLCRN----GGIIGVVSNGGYAEYIVVPEKNLFKIPDSISDELAASLPVAALTayHALK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1806958860 157 EVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVSelddeRRELAAELGADAVVDPNEDDPE 220
Cdd:cd08264   157 TAGLGPGETVVVFGAsGNTGIFAVQLAKMMGAEVIAVS-----RKDWLKEFGADEVVDYDEVEEK 216
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 18-218 7.43e-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: 124.53  E-value: 7.43e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  18 ERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTV-PCNACSYCK 95
Cdd:cd05283    18 ERRPLGPDDVDIKITYCGVCHSDLHTLRNEWGPTKyPLVPGHEIVGIVVAVGSKVTKFKVGDRVGVGCQVdSCGTCEQCK 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  96 RGETHLCENN---TSIGGAGETILDGAFAEYVRVPAINVEDIGE-MSFEHAAlaePLACCvhGV------EEVDVKPGDS 165
Cdd:cd05283    98 SGEEQYCPKGvvtYNGKYPDGTITQGGYADHIVVDERFVFKIPEgLDSAAAA---PLLCA--GItvysplKRNGVGPGKR 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1806958860 166 VAIIGAGPIGLLLLQaFRNA-GAAPIVVSELDDeRRELAAELGADAVVDPNEDD 218
Cdd:cd05283   173 VGVVGIGGLGHLAVK-FAKAlGAEVTAFSRSPS-KKEDALKLGADEFIATKDPE 224
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 46-335 5.40e-32

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: 120.84  E-value: 5.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  46 GTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINptvpcnacsyckrgethlcenntsiggagetildGAFAEYVR 125
Cdd:cd08255    14 GTEKLPLPLPPGYSSVGRVVEVGSGVTGFKPGDRVFCF----------------------------------GPHAERVV 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 126 VPA---INVEDigEMSFEHAALAEPLACCVHGVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERREL 202
Cdd:cd08255    60 VPAnllVPLPD--GLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARREL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 203 AAELG-ADAVVDPNEDDpeaaipaAAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPF-----DV 276
Cdd:cd08255   138 AEALGpADPVAADTADE-------IGGRGADVVIEASGSPSALETALRLLRDRGRVVLVGWYGLKPLLLGEEFhfkrlPI 210

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806958860 277 FFDEVGYRGS----FSLTTE-DFERAVTLLRYGRVdaDALVTERIGLEDLPTAFERM--GNAEGLK 335
Cdd:cd08255   211 RSSQVYGIGRydrpRRWTEArNLEEALDLLAEGRL--EALITHRVPFEDAPEAYRLLfeDPPECLK 274
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 13-339 9.90e-32

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: 122.42  E-value: 9.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  13 AVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVaINPTVP-CNAC 91
Cdd:cd08299    21 SIEEIEVAPPKAHEVRIKIVATGICRSDDHVVSGKLVTPFPVILGHEAAGIVESVGEGVTTVKPGDKV-IPLFVPqCGKC 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  92 SYCKRGETHLCENNtSIGGAGETILDG------------------AFAEYVRVPAINVEDIgemsfehAALAEPLACCVH 153
Cdd:cd08299   100 RACLNPESNLCLKN-DLGKPQGLMQDGtsrftckgkpihhflgtsTFSEYTVVDEIAVAKI-------DAAAPLEKVCLI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 G----------VEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNE-DDP-EA 221
Cdd:cd08299   172 GcgfstgygaaVNTAKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAVDINKDKFAKAKELGATECINPQDyKKPiQE 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 222 AIPAAAGGPVDVGAEAIGLVPTIEQANAVTAPG-GSTLVFGVPDQEATMEISPFDVFFDEVgYRGSFS---LTTEDFERA 297
Cdd:cd08299   252 VLTEMTDGGVDFSFEVIGRLDTMKAALASCHEGyGVSVIVGVPPSSQNLSINPMLLLTGRT-WKGAVFggwKSKDSVPKL 330

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1806958860 298 VTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08299   331 VADYMAKKFNLDPLITHTLPFEKINEGFDLLRSGKSIRTVLT 372
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1-339 4.07e-31

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: 119.20  E-value: 4.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVG---EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA----VETPLVLGHESAGTVAEVGDDVAG 73
Cdd:cd05289     1 MKAVRIHEYGgpeVLELADVPTPEPGPGEVLVKVHAAGVNPVDLKIREGLLKaafpLTLPLIPGHDVAGVVVAVGPGVTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  74 FEVGDRVainptvpcnacsYCKRGETHlcenntsiggagetilDGAFAEYVRVPAinvEDI----GEMSFEHAAlAEPLA 149
Cdd:cd05289    81 FKVGDEV------------FGMTPFTR----------------GGAYAEYVVVPA---DELalkpANLSFEEAA-ALPLA 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 150 ccvhG-------VEEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPI-VVSElddERRELAAELGADAVVDPNEDDPE 220
Cdd:cd05289   129 ----GltawqalFELGGLKAGQTVLIHGAaGGVGSFAVQLAKARGARVIaTASA---ANADFLRSLGADEVIDYTKGDFE 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 221 aaiPAAAGGPVDVGAEAIGlVPTIEQANAVTAPGGsTLVFGVPDQEATMEISPFDVFFDEVGYRGSfsltTEDFERAVTL 300
Cdd:cd05289   202 ---RAAAPGGVDAVLDTVG-GETLARSLALVKPGG-RLVSIAGPPPAEQAAKRRGVRAGFVFVEPD----GEQLAELAEL 272

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1806958860 301 LRYGRVDADalVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd05289   273 VEAGKLRPV--VDRVFPLEDAAEAHERLESGHARGKVVL 309
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 14-338 2.28e-30

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: 118.49  E-value: 2.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  14 VEERERPEPAADEVLVQVGACGVCMTDYHMY-----HGTFavetPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPC 88
Cdd:cd08300    17 IEEVEVAPPKAGEVRIKILATGVCHTDAYTLsgadpEGLF----PVILGHEGAGIVESVGEGVTSVKPGDHVIPLYTPEC 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  89 NACSYCKRGETHLCENNTSIGG-------------AGETILD----GAFAEYVRVPAINVEDIGEMS-FEHAALaepLAC 150
Cdd:cd08300    93 GECKFCKSGKTNLCQKIRATQGkglmpdgtsrfscKGKPIYHfmgtSTFSEYTVVAEISVAKINPEApLDKVCL---LGC 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 151 CVH-GVEEV----DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP--EAAI 223
Cdd:cd08300   170 GVTtGYGAVlntaKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGIDINPDKFELAKKFGATDCVNPKDHDKpiQQVL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 224 PAAAGGPVDVGAEAIGLVPTIEQANAVTAPG-GSTLVFGVpdQEATMEIS--PFDVFFDEV-------GYRGsfsltTED 293
Cdd:cd08300   250 VEMTDGGVDYTFECIGNVKVMRAALEACHKGwGTSVIIGV--AAAGQEIStrPFQLVTGRVwkgtafgGWKS-----RSQ 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1806958860 294 FERAVTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVV 338
Cdd:cd08300   323 VPKLVEDYMKGKIKVDEFITHTMPLDEINEAFDLMHAGKSIRTVV 367
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 10-341 1.17e-29

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: 117.54  E-value: 1.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  10 GEIAVEERERPEPAADEVLVQVGACGVCMTDY--------HMYHGTFAVETPLVLGHESAGTVAEVGDDVAG-FEVGDRV 80
Cdd:cd08238    12 GDLRLEKFELPEIADDEILVRVISDSLCFSTWklalqgsdHKKVPNDLAKEPVILGHEFAGTILKVGKKWQGkYKPGQRF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  81 AINPtvpcnACSYckrgethlcENNTSIGGAGETILdGAFAEYVRVPAINVED----IGE-MSFEHAALAEPLACCV--- 152
Cdd:cd08238    92 VIQP-----ALIL---------PDGPSCPGYSYTYP-GGLATYHIIPNEVMEQdcllIYEgDGYAEASLVEPLSCVIgay 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 -------HGVEE--VDVKPGDSVAIIG-AGPIGLLLLQAFRNAGAAP--IVVSELDDER--------RELAAELGADAV- 211
Cdd:cd08238   157 tanyhlqPGEYRhrMGIKPGGNTAILGgAGPMGLMAIDYAIHGPIGPslLVVTDVNDERlaraqrlfPPEAASRGIELLy 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 212 VDP-NEDDPEAAIPAAAGgpvDVGAEAI-GLVPT---IEQANAVTAPGGSTLVFGVP-DQEATMEISPFDVFFDEVGYRG 285
Cdd:cd08238   237 VNPaTIDDLHATLMELTG---GQGFDDVfVFVPVpelVEEADTLLAPDGCLNFFAGPvDKNFSAPLNFYNVHYNNTHYVG 313

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1806958860 286 SFSLTTEDFERAVTLLRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVVPG 341
Cdd:cd08238   314 TSGGNTDDMKEAIDLMAAGKLNPARMVTHIGGLNAAAETTLNLPGIPGGKKLIYTQ 369
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 12-276 5.23e-27

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: 108.30  E-value: 5.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  12 IAVEERERPEPAADEVLVQVGACGVCMTDyhMYH--GTFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAinptvpcn 89
Cdd:cd05286    14 LEYEDVPVPEPGPGEVLVRNTAIGVNFID--TYFrsGLYPLPLPFVLGVEGAGVVEAVGPGVTGFKVGDRVA-------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  90 acsYCKRGethlcenntsiggagetildGAFAEYVRVPA---INVEDigEMSFEHAAlaeplACCVHG------VEEV-D 159
Cdd:cd05286    84 ---YAGPP--------------------GAYAEYRVVPAsrlVKLPD--GISDETAA-----ALLLQGltahylLRETyP 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 160 VKPGDSVAI-IGAGPIGLLLLQAFRNAGAAPI-VVSelDDERRELAAELGADAVVDPNEDD-PEAAIPAAAGGPVDVGAE 236
Cdd:cd05286   134 VKPGDTVLVhAAAGGVGLLLTQWAKALGATVIgTVS--SEEKAELARAAGADHVINYRDEDfVERVREITGGRGVDVVYD 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1806958860 237 AIGlVPTIEQANAVTAPGGsTLV-FGvpdqEATMEISPFDV 276
Cdd:cd05286   212 GVG-KDTFEGSLDSLRPRG-TLVsFG----NASGPVPPFDL 246
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 1-339 4.42e-26

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: 106.13  E-value: 4.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEERER--PEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPLVLGHESAGTVAEVGDDVAGFEVGD 78
Cdd:cd08249     1 QKAAVLTGPGGGLLVVVDVpvPKPGPDEVLVKVKAVALNPVDWKHQDYGFIPSYPAILGCDFAGTVVEVGSGVTRFKVGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  79 RVainptvpcnaCSYCKrgethlcenntsiGGAGETILDGAFAEYVRVPAINVEDIGE-MSFEHAA-------------- 143
Cdd:cd08249    81 RV----------AGFVH-------------GGNPNDPRNGAFQEYVVADADLTAKIPDnISFEEAAtlpvglvtaalalf 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 144 ----LAEPLAccvhgvEEVDVKPGDSVAIIGAG-PIGLLLLQAFRNAGAAPIVVSelDDERRELAAELGADAVVDPNEDD 218
Cdd:cd08249   138 qklgLPLPPP------KPSPASKGKPVLIWGGSsSVGTLAIQLAKLAGYKVITTA--SPKNFDLVKSLGADAVFDYHDPD 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 219 PEAAIPAAAGGPVDVGAEAIGLVPTIEQ-ANAVTAPGGSTLVF--GVPDQEATM---EISPFDVFFDEVGYRGSFSLTTE 292
Cdd:cd08249   210 VVEDIRAATGGKLRYALDCISTPESAQLcAEALGRSGGGKLVSllPVPEETEPRkgvKVKFVLGYTVFGEIPEDREFGEV 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1806958860 293 DFERAVTLLRYGRVDADALVTERIGLEDLPTAFERM--GNAEGlKKVVV 339
Cdd:cd08249   290 FWKYLPELLEEGKLKPHPVRVVEGGLEGVQEGLDLLrkGKVSG-EKLVV 337
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1-339 8.13e-26

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: 105.27  E-value: 8.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRA---SALTDVGEIAVEErERPEPAA-DEVLVQVGACGVCMTDYHMYHGT--FAVETPLVLGHESAGTVAEVGDDVAGF 74
Cdd:cd08241     1 MKAvvcKELGGPEDLVLEE-VPPEPGApGEVRIRVEAAGVNFPDLLMIQGKyqVKPPLPFVPGSEVAGVVEAVGEGVTGF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  75 EVGDRVainptvpcnacsyckrgethlcenntsIGGAGetilDGAFAEYVRVPAINVEDIGE-MSFEHAAlAEPLACCV- 152
Cdd:cd08241    80 KVGDRV---------------------------VALTG----QGGFAEEVVVPAAAVFPLPDgLSFEEAA-ALPVTYGTa 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 153 -HG-VEEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPI-VVSelDDERRELAAELGADAVVDPNEDD-PEAAIPAAA 227
Cdd:cd08241   128 yHAlVRRARLQPGETVLVLGAaGGVGLAAVQLAKALGARVIaAAS--SEEKLALARALGADHVIDYRDPDlRERVKALTG 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 228 GGPVDVGAEAIGLvPTIEQANAVTAPGGSTLVFGVpdqeATMEISPFD-------------VFFDEVGyRGSFSLTTEDF 294
Cdd:cd08241   206 GRGVDVVYDPVGG-DVFEASLRSLAWGGRLLVIGF----ASGEIPQIPanllllknisvvgVYWGAYA-RREPELLRANL 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1806958860 295 ERAVTLLRYGRVdaDALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08241   280 AELFDLLAEGKI--RPHVSAVFPLEQAAEALRALADRKATGKVVL 322
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-339 1.03e-24

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: 102.23  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEI---AVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET--PLVLGHESAGTVAEVGDDVAGFE 75
Cdd:cd08276     1 MKAWRLSGGGGLdnlKLVEEPVPEPGPGEVLVRVHAVSLNYRDLLILNGRYPPPVkdPLIPLSDGAGEVVAVGEGVTRFK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVA--INPTVPcnacsyckRGETHLCENNTSIGGAgetiLDGAFAEY--------VRVPAInvedigeMSFEHAALa 145
Cdd:cd08276    81 VGDRVVptFFPNWL--------DGPPTAEDEASALGGP----IDGVLAEYvvlpeeglVRAPDH-------LSFEEAAT- 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 146 epLACcvHGV-------EEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVDPNEDD 218
Cdd:cd08276   141 --LPC--AGLtawnalfGLGPLKPGDTVLVQGTGGVSLFALQFAKAAGARVIATSS-SDEKLERAKALGADHVINYRTTP 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 219 peaaipaaaggpvDVGAEA--------------IGLVPTIEQANAVTAPGGSTLVFGVPDQEATmEISPFDVFFDEVGYR 284
Cdd:cd08276   216 -------------DWGEEVlkltggrgvdhvveVGGPGTLAQSIKAVAPGGVISLIGFLSGFEA-PVLLLPLLTKGATLR 281

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1806958860 285 GSFSLTTEDFERAVTLLryGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08276   282 GIAVGSRAQFEAMNRAI--EAHRIRPVIDRVFPFEEAKEAYRYLESGSHFGKVVI 334
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1-339 1.48e-24

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: 101.89  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE---IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPL--VLGHESAGTVAEVGDDVAGFE 75
Cdd:cd08253     1 MRAIRYHEFGApdvLRLGDLPVPTPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLpyVPGSDGAGVVEAVGEGVDGLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVAINptvpcnacsyckrgethlcenntsigGAGETILDGAFAEYVRVPAINVEDIGE-MSFEH-AALAEPLACCVH 153
Cdd:cd08253    81 VGDRVWLT--------------------------NLGWGRRQGTAAEYVVVPADQLVPLPDgVSFEQgAALGIPALTAYR 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 GV-EEVDVKPGDSVAIIG-AGPIGLLLLQAFRNAGAAPI-VVSelDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGG 229
Cdd:cd08253   135 ALfHRAGAKAGETVLVHGgSGAVGHAAVQLARWAGARVIaTAS--SAEGAELVRQAGADAVFNYRAEDLaDRILAATAGQ 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 230 PVDVGAEaIGLVPTIEQANAVTAPGGSTLVFGVPDQEATMEISPFdvFFDEVGYRGS--FSLTTEDFERAVTLLRYGRVD 307
Cdd:cd08253   213 GVDVIIE-VLANVNLAKDLDVLAPGGRIVVYGSGGLRGTIPINPL--MAKEASIRGVllYTATPEERAAAAEAIAAGLAD 289

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1806958860 308 --ADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08253   290 gaLRPVIAREYPLEEAAAAHEAVESGGAIGKVVL 323
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 12-338 7.78e-24

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: 100.45  E-value: 7.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  12 IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCNA 90
Cdd:cd08301    15 LVIEEVEVAPPQAMEVRIKILHTSLCHTDVYFWEAKGQTPLfPRILGHEAAGIVESVGEGVTDLKPGDHVLPVFTGECKE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  91 CSYCKRGETHLCENNTSIGGAGETILDGA------------------FAEYVRVPAINVEDIG-EMSFEHAALaepLACC 151
Cdd:cd08301    95 CRHCKSEKSNMCDLLRINTDRGVMINDGKsrfsingkpiyhfvgtstFSEYTVVHVGCVAKINpEAPLDKVCL---LSCG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 152 VH-----GVEEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNE-DDP-EAAIP 224
Cdd:cd08301   172 VStglgaAWNVAKVKKGSTVAIFGLGAVGLAVAEGARIRGASRIIGVDLNPSKFEQAKKFGVTEFVNPKDhDKPvQEVIA 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 225 AAAGGPVDVGAEAIGLVPTIEQANAVTAPG-GSTLVFGVPDQEATMEISPFDvFFDEVGYRGSF---SLTTEDFERAVTL 300
Cdd:cd08301   252 EMTGGGVDYSFECTGNIDAMISAFECVHDGwGVTVLLGVPHKDAVFSTHPMN-LLNGRTLKGTLfggYKPKTDLPNLVEK 330

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1806958860 301 LRYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVV 338
Cdd:cd08301   331 YMKKELELEKFITHELPFSEINKAFDLLLKGECLRCIL 368
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 7-339 8.65e-23

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: 96.90  E-value: 8.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   7 TDVGEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHG----TFAVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAi 82
Cdd:cd08267     9 PEVLLLLEVEVPIPTPKPGEVLVKVHAASVNPVDWKLRRGppklLLGRPFPPIPGMDFAGEVVAVGSGVTRFKVGDEVF- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  83 nptvpcnacsyckrgethlcenntsigGAGETILDGAFAEYVRVPAINVEDIGE-MSFEHAAlAEPLACC--VHGVEEV- 158
Cdd:cd08267    88 ---------------------------GRLPPKGGGALAEYVVAPESGLAKKPEgVSFEEAA-ALPVAGLtaLQALRDAg 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 159 DVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVV-SElddERRELAAELGADAVVDPNEDDPEaaIPAAAGGPVDVGAE 236
Cdd:cd08267   140 KVKPGQRVLINGAsGGVGTFAVQIAKALGAHVTGVcST---RNAELVRSLGADEVIDYTTEDFV--ALTAGGEKYDVIFD 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 237 AIGLVP-TIEQANAVTAPGGS--TLVFGVPDQEATMEISPFDVFFdeVGYRGSFSLTT---EDFERAVTLLRYGRVdaDA 310
Cdd:cd08267   215 AVGNSPfSLYRASLALKPGGRyvSVGGGPSGLLLVLLLLPLTLGG--GGRRLKFFLAKpnaEDLEQLAELVEEGKL--KP 290

                         330       340
                  ....*....|....*....|....*....
gi 1806958860 311 LVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08267   291 VIDSVYPLEDAPEAYRRLKSGRARGKVVI 319
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 14-268 1.61e-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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 96.13  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  14 VEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPL--VLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCNac 91
Cdd:cd08268    17 IEELPVPAPGAGEVLIRVEAIGLNRADAMFRRGAYIEPPPLpaRLGYEAAGVVEAVGAGVTGFAVGDRVSVIPAADLG-- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  92 syckRGethlcenntsiggagetildGAFAEYVRVPAINVEDIGE-MSFEHAALAEPLACCVHG--VEEVDVKPGDSVAI 168
Cdd:cd08268    95 ----QY--------------------GTYAEYALVPAAAVVKLPDgLSFVEAAALWMQYLTAYGalVELAGLRPGDSVLI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 169 IGA-GPIGLLLLQAFRNAGAAPIVVSeLDDERRELAAELGADAVVDPNEDD-PEAAIPAAAGGPVDVGAEAIGlVPTIEQ 246
Cdd:cd08268   151 TAAsSSVGLAAIQIANAAGATVIATT-RTSEKRDALLALGAAHVIVTDEEDlVAEVLRITGGKGVDVVFDPVG-GPQFAK 228

                         250       260
                  ....*....|....*....|..
gi 1806958860 247 ANAVTAPGGSTLVFGVPDQEAT 268
Cdd:cd08268   229 LADALAPGGTLVVYGALSGEPT 250
MDR3 cd08275
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 12-262 9.64e-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: 176236 [Multi-domain]  Cd Length: 337  Bit Score: 94.19  E-value: 9.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  12 IAVEERERPEPAADEVLVQVGACGV----CMTDYHMYHGTfaVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAinptvp 87
Cdd:cd08275    14 LKVEKEALPEPSSGEVRVRVEACGLnfadLMARQGLYDSA--PKPPFVPGFECAGTVEAVGEGVKDFKVGDRVM------ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  88 cnACSYCkrgethlcenntsiggagetildGAFAEYVRVPAINVEDIGE-MSFEHAA------LAEPLACCVHGveevDV 160
Cdd:cd08275    86 --GLTRF-----------------------GGYAEVVNVPADQVFPLPDgMSFEEAAafpvnyLTAYYALFELG----NL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 161 KPGDSVAI-IGAGPIGLLLLQ---AFRNAGaapiVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVGAE 236
Cdd:cd08275   137 RPGQSVLVhSAAGGVGLAAGQlckTVPNVT----VVGTASASKHEALKENGVTHVIDYRTQDYVEEVKKISPEGVDIVLD 212

                         250       260
                  ....*....|....*....|....*.
gi 1806958860 237 AIGlVPTIEQANAVTAPGGSTLVFGV 262
Cdd:cd08275   213 ALG-GEDTRKSYDLLKPMGRLVVYGA 237
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-239 1.26e-21

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 93.90  E-value: 1.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEI-AVEERE---RPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET---------------------PLV 55
Cdd:cd08274     1 MRAVLLTGHGGLdKLVYRDdvpVPTPAPGEVLIRVGACGVNNTDINTREGWYSTEVdgatdstgageagwwggtlsfPRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  56 LGHESAGTVAEVGDDVAGFEVGDRVAINPTVPcnacsyckRGETHLCENNTSIGGAgetiLDGAFAEYVRVPAINVEDI- 134
Cdd:cd08274    81 QGADIVGRVVAVGEGVDTARIGERVLVDPSIR--------DPPEDDPADIDYIGSE----RDGGFAEYTVVPAENAYPVn 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 135 GEMSFEHAALaepLACCVHGVEEV----DVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVSELDDErrELAAELGAD 209
Cdd:cd08274   149 SPLSDVELAT---FPCSYSTAENMleraGVGAGETVLVTGAsGGVGSALVQLAKRRGAIVIAVAGAAKE--EAVRALGAD 223

                         250       260       270
                  ....*....|....*....|....*....|
gi 1806958860 210 AVVDPNEDDPEaAIPAAAGGPVDVGAEAIG 239
Cdd:cd08274   224 TVILRDAPLLA-DAKALGGEPVDVVADVVG 252
PLN02740 PLN02740
Alcohol dehydrogenase-like
 14-335 2.52e-21

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 93.71  E-value: 2.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  14 VEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET--PLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCNAC 91
Cdd:PLN02740   25 MEEIRVDPPQKMEVRIKILYTSICHTDLSAWKGENEAQRayPRILGHEAAGIVESVGEGVEDLKAGDHVIPIFNGECGDC 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  92 SYCKRGETHLCE--------------NNT--SIGGAGETIL----DGAFAEYVRVPAINVEDIGEMS-FEHAALaepLAC 150
Cdd:PLN02740  105 RYCKRDKTNLCEtyrvdpfksvmvndGKTrfSTKGDGQPIYhflnTSTFTEYTVLDSACVVKIDPNApLKKMSL---LSC 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 151 CVH-GV----EEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDP--EAAI 223
Cdd:PLN02740  182 GVStGVgaawNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGVDINPEKFEKGKEMGITDFINPKDSDKpvHERI 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 224 PAAAGGPVDVGAEAIGLVPTIEQANAVTAPG-GSTLVFGVPDQEATMEISPFDVFfdeVGYR------GSFSLTTEDFER 296
Cdd:PLN02740  262 REMTGGGVDYSFECAGNVEVLREAFLSTHDGwGLTVLLGIHPTPKMLPLHPMELF---DGRSitgsvfGDFKGKSQLPNL 338

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1806958860 297 AVTLLRyGRVDADALVTERIGLEDLPTAFERMGNAEGLK 335
Cdd:PLN02740  339 AKQCMQ-GVVNLDGFITHELPFEKINEAFQLLEDGKALR 376
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-339 9.38e-21

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 91.18  E-value: 9.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAV---EERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAV-ETPLVLGHESAGTVAEVGDDVAGFEV 76
Cdd:cd08271     1 MKAWVLPKPGAALQltlEEIEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAwSYPHVPGVDGAGVVVAVGAKVTGWKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  77 GDRVAInptvpcnacsyckrgetHlcennTSIGGagetilDGAFAEYVRVPAINVEDI-GEMSFEHAA-LAEPLACCVHG 154
Cdd:cd08271    81 GDRVAY-----------------H-----ASLAR------GGSFAEYTVVDARAVLPLpDSLSFEEAAaLPCAGLTAYQA 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 155 VEEV-DVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVSEldDERRELAAELGADAVVD-PNEDDPEAAIPAAAGGPV 231
Cdd:cd08271   133 LFKKlRIEAGRTILITGGaGGVGSFAVQLAKRAGLRVITTCS--KRNFEYVKSLGADHVIDyNDEDVCERIKEITGGRGV 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DVGAEAIGLVPTIEQANAVTAPGGSTLVFGVPDQeatmeiSPFDVF-----FDEV--------GYRGSFSLTTEDFERAV 298
Cdd:cd08271   211 DAVLDTVGGETAAALAPTLAFNGHLVCIQGRPDA------SPDPPFtralsVHEValgaahdhGDPAAWQDLRYAGEELL 284

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1806958860 299 TLLRYGRVdaDALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08271   285 ELLAAGKL--EPLVIEVLPFEQLPEALRALKDRHTRGKIVV 323
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 1-218 4.60e-20

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: 89.04  E-value: 4.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVG---EIAVEERERPEPAADEVLVQVGACGV----CMTDYHMYHGTfaVETPLVLGHESAGTVAEVGDDVAG 73
Cdd:cd05276     1 MKAIVIKEPGgpeVLELGEVPKPAPGPGEVLIRVAAAGVnradLLQRQGLYPPP--PGASDILGLEVAGVVVAVGPGVTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  74 FEVGDRVainptvpcnaCSYCkrgethlcenntsiggAGetildGAFAEYVRVPAINVEDIGE-MSFEHAA-LAEPLACC 151
Cdd:cd05276    79 WKVGDRV----------CALL----------------AG-----GGYAEYVVVPAGQLLPVPEgLSLVEAAaLPEVFFTA 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1806958860 152 VHGVEEV-DVKPGDSVAI-IGAGPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVDPNEDD 218
Cdd:cd05276   128 WQNLFQLgGLKAGETVLIhGGASGVGTAAIQLAKALGARVIATAG-SEEKLEACRALGADVAINYRTED 195
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
173-301 4.11e-19

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 81.88  E-value: 4.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 173 PIGLLLLQAFRNAGAAPIVVSeLDDERRELAAELGADAVVDPNEDDP-EAAIPAAAGGPVDVGAEAIGLVPTIEQANAVT 251
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVD-GSEEKLELAKELGADHVINPKETDLvEEIKELTGGKGVDVVFDCVGSPATLEQALKLL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1806958860 252 APGGSTLVFGVPDQEAtmEISPFDVFFDEVGYRGSFSLTTEDFERAVTLL 301
Cdd:pfam00107  80 RPGGRVVVVGLPGGPL--PLPLAPLLLKELTILGSFLGSPEEFPEALDLL 127
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-217 7.50e-18

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 82.99  E-value: 7.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAV-EERE--RPEPAADEVLVQVGACGVCMTDYHMYHGT--FAVETPLVLGHESAGTVAEVGDDVAGFE 75
Cdd:cd08272     1 MKALVLESFGGPEVfELREvpRPQPGPGQVLVRVHASGVNPLDTKIRRGGaaARPPLPAILGCDVAGVVEAVGEGVTRFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  76 VGDRVAinptvpcnacsYCKRGethlcenntsIGGAGetildGAFAEYVRVPAinveDI-----GEMSFEHAAlAEPLac 150
Cdd:cd08272    81 VGDEVY-----------GCAGG----------LGGLQ-----GSLAEYAVVDA----RLlalkpANLSMREAA-ALPL-- 127

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1806958860 151 cVHG------VEEVDVKPGDSVAI-IGAGPIGLLLLQAFRNAGAapIVVSELDDERRELAAELGADAVVDPNED 217
Cdd:cd08272   128 -VGItaweglVDRAAVQAGQTVLIhGGAGGVGHVAVQLAKAAGA--RVYATASSEKAAFARSLGADPIIYYRET 198
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 25-210 6.16e-17

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: 79.92  E-value: 6.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  25 DEVLVQVGACGVCMTDYHMYHGTFAVEtPLVLGHESAGTVAEVGDDVAGFEVGDRVAInptvpcnacsyckrgethlcen 104
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVALGLLPGD-ETPLGLECSGIVTRVGSGVTGLKVGDRVMG---------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 105 ntsiggagetILDGAFAEYVRVPAINVEDIGE-MSFEHAAlAEPLACC--VHGVEEV-DVKPGDSVAII-GAGPIGLLLL 179
Cdd:cd05195    58 ----------LAPGAFATHVRVDARLVVKIPDsLSFEEAA-TLPVAYLtaYYALVDLaRLQKGESVLIHaAAGGVGQAAI 126

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1806958860 180 QAFRNAGAAPIV-VSelDDERRELAAELGADA 210
Cdd:cd05195   127 QLAQHLGAEVFAtVG--SEEKREFLRELGGPV 156
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1-339 9.16e-17

Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 79.58  E-value: 9.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAV---EERERPEPAADEVLVQVGACGVCMTDYHMYHGTFA-VETPLVLGHESAGTVAEVGDDvaGFEV 76
Cdd:cd08243     1 MKAIVIEQPGGPEVlklREIPIPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPsVKFPRVLGIEAVGEVEEAPGG--TFTP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  77 GDRVAinptvpcnacsyckrgethlcennTSIGGAGETIlDGAFAEYVRVPAINVEDI-GEMSFEH-AALAEPLaCCVHG 154
Cdd:cd08243    79 GQRVA------------------------TAMGGMGRTF-DGSYAEYTLVPNEQVYAIdSDLSWAElAALPETY-YTAWG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 155 V--EEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAApIVVSELDDERRELAAELGADAVVDPNEDDPEaaIPAAAGGPV 231
Cdd:cd08243   133 SlfRSLGLQPGDTLLIRGGtSSVGLAALKLAKALGAT-VTATTRSPERAALLKELGADEVVIDDGAIAE--QLRAAPGGF 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 232 DVGAEAIGlVPTIEQANAVTAPGGSTLVFGVPDQEATME-ISPFDVFFDEVG--YRGSFSLTTEDF--ERAVTLLRYGRV 306
Cdd:cd08243   210 DKVLELVG-TATLKDSLRHLRPGGIVCMTGLLGGQWTLEdFNPMDDIPSGVNltLTGSSSGDVPQTplQELFDFVAAGHL 288

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1806958860 307 daDALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08243   289 --DIPPSKVFTFDEIVEAHAYMESNRAFGKVVV 319
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 24-212 3.89e-16

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 78.30  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  24 ADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTV-PCNACSYCKRGETHL 101
Cdd:PLN02514   34 PEDVVIKVIYCGICHTDLHQIKNDLGMSNyPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGVIVgCCGECSPCKSDLEQY 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 102 CENN-------------TSIGGAGETILDGAFAeyVRVPAinvedigEMSFEHAAlaePLACCvhGVEEVD-------VK 161
Cdd:PLN02514  114 CNKRiwsyndvytdgkpTQGGFASAMVVDQKFV--VKIPE-------GMAPEQAA---PLLCA--GVTVYSplshfglKQ 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1806958860 162 PGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVV 212
Cdd:PLN02514  180 SGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGADDYL 230
crotonyl_coA_red cd08246
crotonyl-CoA reductase; Crotonyl-CoA reductase, a member of the medium chain dehydrogenase ...
 20-218 3.95e-16

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: 78.61  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  20 PEPAADEVLVQVGACGVCMTDYHMYHG----TFAV-------ETPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPC 88
Cdd:cd08246    38 PELGPGEVLVAVMAAGVNYNNVWAALGepvsTFAArqrrgrdEPYHIGGSDASGIVWAVGEGVKNWKVGDEVVVHCSVWD 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  89 NACSYCKRGETHLCENNtSIGGAGETilDGAFAEYVRVPAINV-EDIGEMSFEHAAlAEPLACC-----VHGVEEVDVKP 162
Cdd:cd08246   118 GNDPERAGGDPMFDPSQ-RIWGYETN--YGSFAQFALVQATQLmPKPKHLSWEEAA-AYMLVGAtayrmLFGWNPNTVKP 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1806958860 163 GDSVAIIGA-GPIGLLLLQAFRNAGAAPI-VVSelDDERRELAAELGADAVVDPNEDD 218
Cdd:cd08246   194 GDNVLIWGAsGGLGSMAIQLARAAGANPVaVVS--SEEKAEYCRALGAEGVINRRDFD 249
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 10-326 1.69e-15

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: 76.16  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  10 GEIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVETPL--VLGHESAGTVAEVGDDVAGFEVGDRVAinptvp 87
Cdd:cd05282    12 LVLELVSLPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSRPPLpaVPGNEGVGVVVEVGSGVSGLLVGQRVL------ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  88 cnacsyckrgethlcenntSIGGAgetildGAFAEYVRVPA---INVEDigEMSFEHAA--LAEPLACCVHGVEEVDVKP 162
Cdd:cd05282    86 -------------------PLGGE------GTWQEYVVAPAddlIPVPD--SISDEQAAmlYINPLTAWLMLTEYLKLPP 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 163 GDSVAIIGAGP-IGLLLLQAFRNAGAAPIVVSELDDERRELAAeLGADAVVD-PNEDDPEAAIPAAAGGPVDVGAEAIGL 240
Cdd:cd05282   139 GDWVIQNAANSaVGRMLIQLAKLLGFKTINVVRRDEQVEELKA-LGADEVIDsSPEDLAQRVKEATGGAGARLALDAVGG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 241 VPTIEQANAVtAPGGSTLVFGVPDQEAtMEISPFDVFFDEVGYRGsFSLT-----------TEDFERAVTLLRYGRvdAD 309
Cdd:cd05282   218 ESATRLARSL-RPGGTLVNYGLLSGEP-VPFPRSVFIFKDITVRG-FWLRqwlhsatkeakQETFAEVIKLVEAGV--LT 292

                         330
                  ....*....|....*..
gi 1806958860 310 ALVTERIGLEDLPTAFE 326
Cdd:cd05282   293 TPVGAKFPLEDFEEAVA 309
PLN02827 PLN02827
Alcohol dehydrogenase-like
 12-338 4.13e-15

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 75.32  E-value: 4.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  12 IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVetPLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTVPCNAC 91
Cdd:PLN02827   25 LVMEEVEVSPPQPLEIRIKVVSTSLCRSDLSAWESQALF--PRIFGHEASGIVESIGEGVTEFEKGDHVLTVFTGECGSC 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  92 SYCKRGETHLCE-------------NNTSIGGAGETILD----GAFAEYVRVP---AINVEDIGEMSfEHAALAEPLACC 151
Cdd:PLN02827  103 RHCISGKSNMCQvlglerkgvmhsdQKTRFSIKGKPVYHycavSSFSEYTVVHsgcAVKVDPLAPLH-KICLLSCGVAAG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 152 VHGVEEV-DVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNE-DDP-EAAIPAAAG 228
Cdd:PLN02827  182 LGAAWNVaDVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGVDINPEKAEKAKTFGVTDFINPNDlSEPiQQVIKRMTG 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 229 GPVDVGAEAIGLVPTIEQANAVTAPG-GSTLVFGVPdqEATMEISP-FDVFFDEVGYRGSFS---LTTEDFERAVTLLRY 303
Cdd:PLN02827  262 GGADYSFECVGDTGIATTALQSCSDGwGLTVTLGVP--KAKPEVSAhYGLFLSGRTLKGSLFggwKPKSDLPSLVDKYMN 339

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1806958860 304 GRVDADALVTERIGLEDLPTAFERMGNAEGLKKVV 338
Cdd:PLN02827  340 KEIMIDEFITHNLSFDEINKAFELMREGKCLRCVI 374
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 14-339 1.17e-14

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 73.84  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  14 VEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET--PLVLGHESAGTVAEVGDDVAGFEVGDRV-AINPTvpcna 90
Cdd:cd08273    17 VVEADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPplPFTPGYDLVGRVDALGSGVTGFEVGDRVaALTRV----- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  91 csyckrgethlcenntsiggagetildGAFAEYVRVPAINVEDIGEMSFEHAALAEPLA-----CCVHGVeeVDVKPGDS 165
Cdd:cd08273    92 ---------------------------GGNAEYINLDAKYLVPVPEGVDAAEAVCLVLNyvtayQMLHRA--AKVLTGQR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 166 VAIIGA-GPIGLLLLQAFRNAGAAPIVVSelDDERRELAAELGADAVVdpnEDDPEAAIPAAAGGPVDVGAEAIGLvPTI 244
Cdd:cd08273   143 VLIHGAsGGVGQALLELALLAGAEVYGTA--SERNHAALRELGATPID---YRTKDWLPAMLTPGGVDVVFDGVGG-ESY 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 245 EQANAVTAPGGSTLVFGVP---DQE--------------ATMEISPFD---VFFDEVGYRGSFSLT-TEDFERAVTLLRY 303
Cdd:cd08273   217 EESYAALAPGGTLVCYGGNsslLQGrrslaalgsllarlAKLKLLPTGrraTFYYVWRDRAEDPKLfRQDLTELLDLLAK 296

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1806958860 304 GRVdaDALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd08273   297 GKI--RPKIAKRLPLSEVAEAHRLLESGKVVGKIVL 330
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 19-332 3.61e-14

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 72.60  E-value: 3.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  19 RPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTV-PCNACSYCKR 96
Cdd:PLN02586   32 RRENGDEDVTVKILYCGVCHSDLHTIKNEWGFTRyPIVPGHEIVGIVTKLGKNVKKFKEGDRVGVGVIVgSCKSCESCDQ 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  97 GETHLCEN----NTSIGGAGeTILDGAFAEYVRVPAINVEDIGE-MSFEHAAlaePLACC---------VHGVEEvdvkP 162
Cdd:PLN02586  112 DLENYCPKmiftYNSIGHDG-TKNYGGYSDMIVVDQHFVLRFPDnLPLDAGA---PLLCAgitvyspmkYYGMTE----P 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 163 GDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVGAEAIGLVP 242
Cdd:PLN02586  184 GKHLGVAGLGGLGHVAVKIGKAFGLKVTVISSSSNKEDEAINRLGADSFLVSTDPEKMKAAIGTMDYIIDTVSAVHALGP 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 243 TIeqanAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGyrGSFSLTTEDFERAVTLLRYGRVDADalvTERIGLEDLP 322
Cdd:PLN02586  264 LL----GLLKVNGKLITLGLPEKPLELPIFPLVLGRKLVG--GSDIGGIKETQEMLDFCAKHNITAD---IELIRMDEIN 334

                         330
                  ....*....|
gi 1806958860 323 TAFERMGNAE 332
Cdd:PLN02586  335 TAMERLAKSD 344
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 1-268 3.70e-14

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: 72.02  E-value: 3.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVG---EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGT----FAVETPLVLGHESAGTVAEVGDDVAG 73
Cdd:cd08244     1 MRAIRLHEFGppeVLVPEDVPDPVPGPGQVRIAVAAAGVHFVDTQLRSGWgpgpFPPELPYVPGGEVAGVVDAVGPGVDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  74 FEVGDRVAinptvpcnacsyckrgethlcennTSIGGAGetildGAFAEYVRVPAINVEDIGEmsfeHAALAEPLACCVH 153
Cdd:cd08244    81 AWLGRRVV------------------------AHTGRAG-----GGYAELAVADVDSLHPVPD----GLDLEAAVAVVHD 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 154 GV------EEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVSELDDeRRELAAELGADAVVDPNEDD-PEAAIPA 225
Cdd:cd08244   128 GRtalgllDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAGATVVGAAGGPA-KTALVRALGADVAVDYTRPDwPDQVREA 206

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1806958860 226 AAGGPVDVGAEAIGlVPTIEQANAVTAPGGSTLVFGVPDQEAT 268
Cdd:cd08244   207 LGGGGVTVVLDGVG-GAIGRAALALLAPGGRFLTYGWASGEWT 248
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 11-326 1.68e-12

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: 67.39  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  11 EIAVEERERPEpaaDEVLVQVGACGVCMTDYHMYHGTFAVET-----PLVLGHESAGTVaeVGDDVAGFEVGDRVAINPT 85
Cdd:cd08237    15 EVTYEEENLRE---DWVIVRPTYLSICHADQRYYQGNRSPEAlkkklPMALIHEGIGVV--VSDPTGTYKVGTKVVMVPN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  86 VPCNACSYCKRG---ETHLCenntSIGgagetiLDGAFAEYVRVPAINVEDIGEMSFEH-AALAEPLACCVHGVEEVD-- 159
Cdd:cd08237    90 TPVEKDEIIPENylpSSRFR----SSG------YDGFMQDYVFLPPDRLVKLPDNVDPEvAAFTELVSVGVHAISRFEqi 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 160 -VKPGDSVAIIGAGPIG----LLLLQAFrnaGAAPIVVSELDDERRELAAELGADAVVDpneDDPEAAIpaaaggpVDVG 234
Cdd:cd08237   160 aHKDRNVIGVWGDGNLGyitaLLLKQIY---PESKLVVFGKHQEKLDLFSFADETYLID---DIPEDLA-------VDHA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 235 AEAIGLV---PTIEQANAVTAPGGSTLVFGVpdQEATMEISPFDVFFDEVGYRGSFSLTTEDFERAVTLLRYGRVDADAL 311
Cdd:cd08237   227 FECVGGRgsqSAINQIIDYIRPQGTIGLMGV--SEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYL 304

                         330       340
                  ....*....|....*....|.
gi 1806958860 312 ------VTERIGLEDLPTAFE 326
Cdd:cd08237   305 rklvggVFPVRSINDIHRAFE 325
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 1-213 1.97e-11

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 64.08  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVE------ERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVE-TPLVLGHESAGTVAEVGDDVAG 73
Cdd:cd08252     1 MKAIGFTQPLPITDPdslidiELPKPVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPgQPKILGWDASGVVEAVGSEVTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  74 FEVGDRVAinptvpcnacsYckrgethlcenntsiggAGETILDGAFAEYVRVpainveD---IGEM----SFEHAAlAE 146
Cdd:cd08252    81 FKVGDEVY-----------Y-----------------AGDITRPGSNAEYQLV------DeriVGHKpkslSFAEAA-AL 125

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1806958860 147 PLACCVH--------GVEEVDVKPGDSVAII-GAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVD 213
Cdd:cd08252   126 PLTSLTAwealfdrlGISEDAENEGKTLLIIgGAGGVGSIAIQLAKQLTGLTVIATASRPESIAWVKELGADHVIN 201
ETR_like_1 cd08291
2-enoyl thioester reductase (ETR) like proteins, child 1; 2-enoyl thioester reductase (ETR) ...
 1-291 4.18e-11

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: 63.01  E-value: 4.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVG------EIAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET--PLVLGHESAGTVAEVGD-DV 71
Cdd:cd08291     1 MKALLLEEYGkplevkELSLPEPEVPEPGPGEVLIKVEAAPINPSDLGFLKGQYGSTKalPVPPGFEGSGTVVAAGGgPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  72 AGFEVGDRVAinptvpcnacsyCKRGEthlcenntsiggagetilDGAFAEYVRVPAINV----EDIgemSFEHAA--LA 145
Cdd:cd08291    81 AQSLIGKRVA------------FLAGS------------------YGTYAEYAVADAQQClplpDGV---SFEQGAssFV 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 146 EPLACCVHgVEEvdVKPGDSVAII---GAGPIGLLLLQAFRNAGAAPI-VVSEldDERRELAAELGADAVVDPNEDD-PE 220
Cdd:cd08291   128 NPLTALGM-LET--AREEGAKAVVhtaAASALGRMLVRLCKADGIKVInIVRR--KEQVDLLKKIGAEYVLNSSDPDfLE 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806958860 221 AAIPAAAGGPVDVGAEAIGLVPTIEQANAvtAPGGSTL-VFGVPDQEATMEISPFDVFFDEVGYRGsFSLTT 291
Cdd:cd08291   203 DLKELIAKLNATIFFDAVGGGLTGQILLA--MPYGSTLyVYGYLSGKLDEPIDPVDLIFKNKSIEG-FWLTT 271
PKS_ER smart00829
Enoylreductase; Enoylreductase in Polyketide synthases.
 29-187 7.26e-11

Enoylreductase; Enoylreductase in Polyketide synthases.


Pssm-ID: 214840 [Multi-domain]  Cd Length: 287  Bit Score: 62.02  E-value: 7.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   29 VQVGACGVCMTDYHMYHGTfaVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAinptvpcnacsyckrgethlcenntsi 108
Cdd:smart00829   1 IEVRAAGLNFRDVLIALGL--YPGEAVLGGECAGVVTRVGPGVTGLAVGDRVM--------------------------- 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  109 ggageTILDGAFAEYVRVPAINVEDI-GEMSFEHAAlAEPLACC--VHGVEEV-DVKPGDSVAI-IGAGPIGLLLLQAFR 183
Cdd:smart00829  52 -----GLAPGAFATRVVTDARLVVPIpDGWSFEEAA-TVPVVFLtaYYALVDLaRLRPGESVLIhAAAGGVGQAAIQLAR 125


                   ....
gi 1806958860  184 NAGA 187
Cdd:smart00829 126 HLGA 129
ETR_like_2 cd08292
2-enoyl thioester reductase (ETR) like proteins, child 2; 2-enoyl thioester reductase (ETR) ...
 1-301 3.26e-10

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: 60.42  E-value: 3.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGE----IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAV--ETPLVLGHESAGTVAEVGDDVAGF 74
Cdd:cd08292     1 MRAAVHTQFGDpadvLEIGEVPKPTPGAGEVLVRTTLSPIHNHDLWTIRGTYGYkpELPAIGGSEAVGVVDAVGEGVKGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  75 EVGDRVAINPtvpcnacsyckrgethlcenntsiggagetiLDGAFAEYVRVPA---INVEDigEMSFEHAA--LAEPLA 149
Cdd:cd08292    81 QVGQRVAVAP-------------------------------VHGTWAEYFVAPAdglVPLPD--GISDEVAAqlIAMPLS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 150 CCVHgVEEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVSELDDERRELAAeLGADAVVDPNEDD-----PEAAI 223
Cdd:cd08292   128 ALML-LDFLGVKPGQWLIQNAAgGAVGKLVAMLAAARGINVINLVRRDAGVAELRA-LGIGPVVSTEQPGwqdkvREAAG 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 224 PAAAGGPVD-VGAEAIGlvptieQANAVTAPGGSTLVFGVPDQEaTMEISPFDVFFDEVGYRG------SFSLTTEDFER 296
Cdd:cd08292   206 GAPISVALDsVGGKLAG------ELLSLLGEGGTLVSFGSMSGE-PMQISSGDLIFKQATVRGfwggrwSQEMSVEYRKR 278


                  ....*
gi 1806958860 297 AVTLL 301
Cdd:cd08292   279 MIAEL 283
polyketide_synthase cd08251
polyketide synthase; Polyketide synthases produce polyketides in step by step mechanism that ...
 18-218 6.24e-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: 59.36  E-value: 6.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  18 ERPEPAADEVLVQVGACGVCMTDYHMYHGTFAV--ETPLVLGHESAGTVAEVGDDVAGFEVGDRVainptvpcnacsyck 95
Cdd:cd08251     1 EVAPPGPGEVRIQVRAFSLNFGDLLCVRGLYPTmpPYPFTPGFEASGVVRAVGPHVTRLAVGDEV--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  96 rgethlcenntsIGGAGETIldGAFAEYVRVPAINV-EDIGEMSFEHAAlAEPLA--CCVHGVEEVDVKPGDSVAIIGA- 171
Cdd:cd08251    66 ------------IAGTGESM--GGHATLVTVPEDQVvRKPASLSFEEAC-ALPVVflTVIDAFARAGLAKGEHILIQTAt 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1806958860 172 GPIGLLLLQAFRNAGAApIVVSELDDERRELAAELGADAVVDPNEDD 218
Cdd:cd08251   131 GGTGLMAVQLARLKGAE-IYATASSDDKLEYLKQLGVPHVINYVEED 176
RTN4I1 cd08248
Human Reticulon 4 Interacting Protein 1; Human Reticulon 4 Interacting Protein 1 is a member ...
 1-339 6.67e-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: 59.54  E-value: 6.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAVEE--RERPEPA---ADEVLVQV----------------GACGVCMTDYHMYHGTFAVETPLVLGHE 59
Cdd:cd08248     1 MKAWQIHSYGGIDSLLllENARIPVirkPNQVLIKVhaasvnpidvlmrsgyGRTLLNKKRKPQSCKYSGIEFPLTLGRD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  60 SAGTVAEVGDDVAGFEVGDRV--AINPTVPcnacsyckrgethlcenntsiggagetildGAFAEYVRVPAINV-EDIGE 136
Cdd:cd08248    81 CSGVVVDIGSGVKSFEIGDEVwgAVPPWSQ------------------------------GTHAEYVVVPENEVsKKPKN 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 137 MSFEHAAlAEPLACCV-------HGVEEVDVKPGDSVAIIGA-GPIGLLLLQAFRNAGAapIVVSELDDERRELAAELGA 208
Cdd:cd08248   131 LSHEEAA-SLPYAGLTawsalvnVGGLNPKNAAGKRVLILGGsGGVGTFAIQLLKAWGA--HVTTTCSTDAIPLVKSLGA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 209 DAVVD-PNEDDPEaaiPAAAGGPVDVGAEAIGlVPTIEQANAVTAPGGS--TLVfgvpdqeatmeiSPFDVFFDEVGYRG 285
Cdd:cd08248   208 DDVIDyNNEDFEE---ELTERGKFDVILDTVG-GDTEKWALKLLKKGGTyvTLV------------SPLLKNTDKLGLVG 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 286 SFSLTTEDFERAV-------TLLRYGRVDADALVTERI-----------------GLEDLPTAFERM--GNAEGlkKVVV 339
Cdd:cd08248   272 GMLKSAVDLLKKNvksllkgSHYRWGFFSPSGSALDELaklvedgkikpvidkvfPFEEVPEAYEKVesGHARG--KTVI 349
MDR_yhdh_yhfp cd05280
Yhdh and yhfp-like putative quinone oxidoreductases; Yhdh and yhfp-like putative quinone ...
 53-339 1.53e-09

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: 58.32  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  53 PLVLGHESAGTVAEVGDDvaGFEVGDRVAINPtvpcnacsyCKRGETHlcenntsiggagetilDGAFAEYVRVPAINVE 132
Cdd:cd05280    58 PHTPGIDAAGTVVSSDDP--RFREGDEVLVTG---------YDLGMNT----------------DGGFAEYVRVPADWVV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 133 DIGE-------MSFEHAALAEPLAccVHGVEEVDVKPGDS-VAIIGA-GPIGLLLLQAFRNAGAAPIVVSElDDERRELA 203
Cdd:cd05280   111 PLPEglslreaMILGTAGFTAALS--VHRLEDNGQTPEDGpVLVTGAtGGVGSIAVAILAKLGYTVVALTG-KEEQADYL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 204 AELGADAVVDPNEDDPEAA---IPAAAGGPVD-VGAEAI-GLVPTIEQANAVTAPGgstLVFGvPDQEATmeISPFDVff 278
Cdd:cd05280   188 KSLGASEVLDREDLLDESKkplLKARWAGAIDtVGGDVLaNLLKQTKYGGVVASCG---NAAG-PELTTT--VLPFIL-- 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1806958860 279 devgyRG-------SFSLTTEDFERAVTLL-RYGRVDADALVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:cd05280   260 -----RGvsllgidSVNCPMELRKQVWQKLaTEWKPDLLEIVVREISLEELPEAIDRLLAGKHRGRTVV 323
PTZ00354 PTZ00354
alcohol dehydrogenase; Provisional
 1-216 3.02e-09

alcohol dehydrogenase; Provisional


Pssm-ID: 173547 [Multi-domain]  Cd Length: 334  Bit Score: 57.73  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860   1 MRASALTDVGEIAV---EERERPEPAADEVLVQVGACGVCMTDYHMYHGTFAV---ETPLvLGHESAGTVAEVGDDVAGF 74
Cdd:PTZ00354    2 MRAVTLKGFGGVDVlkiGESPKPAPKRNDVLIKVSAAGVNRADTLQRQGKYPPppgSSEI-LGLEVAGYVEDVGSDVKRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  75 EVGDRV-AInptvpcnacsyckrgethlcenntsIGGagetildGAFAEYVRVPAINVEDI-GEMSFEHA-ALAEPL--- 148
Cdd:PTZ00354   81 KEGDRVmAL-------------------------LPG-------GGYAEYAVAHKGHVMHIpQGYTFEEAaAIPEAFlta 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806958860 149 --ACCVHGveevDVKPGDSVAI-IGAGPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVV-DPNE 216
Cdd:PTZ00354  129 wqLLKKHG----DVKKGQSVLIhAGASGVGTAAAQLAEKYGAATIITTS-SEEKVDFCKKLAAIILIrYPDE 195
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 19-339 9.24e-09

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 56.19  E-value: 9.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  19 RPEPAADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVGDDVAGFEVGDRVAINPTV-PCNACSYCKR 96
Cdd:PLN02178   26 RRENGENDVTVKILFCGVCHSDLHTIKNHWGFSRyPIIPGHEIVGIATKVGKNVTKFKEGDRVGVGVIIgSCQSCESCNQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  97 GETHLCE------NNTSIGGageTILDGAFAEYVRVPAINVEDIGEMSFEHAAlaEPLACC---------VHGVEEvdvK 161
Cdd:PLN02178  106 DLENYCPkvvftyNSRSSDG---TRNQGGYSDVIVVDHRFVLSIPDGLPSDSG--APLLCAgitvyspmkYYGMTK---E 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 162 PGDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVDPNEDDPEAAIPAAAGGPVDVGAEAIGLV 241
Cdd:PLN02178  178 SGKRLGVNGLGGLGHIAVKIGKAFGLRVTVISRSSEKEREAIDRLGADSFLVTTDSQKMKEAVGTMDFIIDTVSAEHALL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 242 PTIeqanAVTAPGGSTLVFGVPDQEATMEISPFDVFFDEVGyrGSFSLTTEDFERAVTLLRYGRVDADalvTERIGLEDL 321
Cdd:PLN02178  258 PLF----SLLKVSGKLVALGLPEKPLDLPIFPLVLGRKMVG--GSQIGGMKETQEMLEFCAKHKIVSD---IELIKMSDI 328

                         330
                  ....*....|....*...
gi 1806958860 322 PTAFERMGNAEGLKKVVV 339
Cdd:PLN02178  329 NSAMDRLAKSDVRYRFVI 346
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 12-213 7.55e-08

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: 53.41  E-value: 7.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  12 IAVEERERPEPAADEVLVQVGACGVCMTDYHMYHGTF--AVETPLVLGHESAGTVAEVGDDVAGFEVGDRVAinptvpcn 89
Cdd:cd08250    18 TSIVDVPVPLPGPGEVLVKNRFVGINASDINFTAGRYdpGVKPPFDCGFEGVGEVVAVGEGVTDFKVGDAVA-------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  90 acsyckrgethlcenntsiggageTILDGAFAEYVRVPAINVEDIGEMSfehaalAEPLACCVHGV------EEV-DVKP 162
Cdd:cd08250    90 ------------------------TMSFGAFAEYQVVPARHAVPVPELK------PEVLPLLVSGLtasialEEVgEMKS 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1806958860 163 GDSVAIIGA-GPIGLLLLQAFRNAGAAPIVVSElDDERRELAAELGADAVVD 213
Cdd:cd08250   140 GETVLVTAAaGGTGQFAVQLAKLAGCHVIGTCS-SDEKAEFLKSLGCDRPIN 190
PRK10754 PRK10754
NADPH:quinone reductase;
20-218 9.15e-08

NADPH:quinone reductase;


Pssm-ID: 182701 [Multi-domain]  Cd Length: 327  Bit Score: 52.81  E-value: 9.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  20 PEPAADEVLVQVGACGVCMTDYHMYHGTFAVET-PLVLGHESAGTVAEVGDDVAGFEVGDRVAinptvpcnacsYCKRGE 98
Cdd:PRK10754   24 ADPAENEVQVENKAIGINYIDTYIRSGLYPPPSlPSGLGTEAAGVVSKVGSGVKHIKVGDRVV-----------YAQSAL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  99 thlcenntsiggagetildGAFAEYVRVPAINVEDIGE-MSFEHAAlaeplACCVHGV-------EEVDVKPGDSVAI-I 169
Cdd:PRK10754   93 -------------------GAYSSVHNVPADKAAILPDaISFEQAA-----ASFLKGLtvyyllrKTYEIKPDEQFLFhA 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1806958860 170 GAGPIGLLLLQAFRNAGAAPI--VVSeldDERRELAAELGADAVVDPNEDD 218
Cdd:PRK10754  149 AAGGVGLIACQWAKALGAKLIgtVGS---AQKAQRAKKAGAWQVINYREEN 196
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 13-320 1.87e-07

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 51.99  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  13 AVEERERPEPAADEVLVQVGACGVCMTDYHmyhgtFAVETP--LVLGHESAGTVAEVGDDVAGFEVGDRVAinptvpcna 90
Cdd:cd08270    15 RLGEVPDPQPAPHEALVRVAAISLNRGELK-----FAAERPdgAVPGWDAAGVVERAAADGSGPAVGARVV--------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  91 csyckrgethlcenntsigGAGEtilDGAFAEYVRVPAINVEDIGE-MSFEHAAlAEPLA--CCVHGVEEVDVKPGDSVA 167
Cdd:cd08270    81 -------------------GLGA---MGAWAELVAVPTGWLAVLPDgVSFAQAA-TLPVAgvTALRALRRGGPLLGRRVL 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 168 IIGA-GPIGLLLLQAFRNAGAApIVVSELDDERRELAAELGA-DAVVDPNEDDPEAaipaaaggpVDVGAEAIGlVPTIE 245
Cdd:cd08270   138 VTGAsGGVGRFAVQLAALAGAH-VVAVVGSPARAEGLRELGAaEVVVGGSELSGAP---------VDLVVDSVG-GPQLA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 246 QANAVTAPGGSTLVFGVpdqeATMEISPFDvFFDEVGYRGSFSLTT----------EDFERAVTLLRYGRVDAdalvteR 315
Cdd:cd08270   207 RALELLAPGGTVVSVGS----SSGEPAVFN-PAAFVGGGGGRRLYTfflydgeplaADLARLLGLVAAGRLDP------R 275


                  ....*
gi 1806958860 316 IGLED 320
Cdd:cd08270   276 IGWRG 280
AST1_like cd08247
AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group ...
 25-213 4.85e-07

AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast; This group contains members identified in targeting of yeast membrane proteins ATPase. AST1 is a cytoplasmic protein associated with the periplasmic membrane in yeast, identified as a multicopy suppressor of pma1 mutants which cause temperature sensitive growth arrest due to the inability of ATPase to target to the cell surface. This family is homologous to the medium chain family of dehydrogenases and reductases. 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.


Pssm-ID: 176209 [Multi-domain]  Cd Length: 352  Bit Score: 50.73  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  25 DEVLVQVGACGVCMTDYHMYHG-TFAV-ETPLVLGHESAGTVAEVGDDVA-GFEVGDRVainptvpcnacsyckrgethl 101
Cdd:cd08247    29 NEIVVKVHAAALNPVDLKLYNSyTFHFkVKEKGLGRDYSGVIVKVGSNVAsEWKVGDEV--------------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 102 CENNTSIGGAgetilDGAFAEYVRV-PAINVEDI----GEMSFEHAAlAEPL----ACCVHGVEEVDVKPGDSVAIIGAG 172
Cdd:cd08247    88 CGIYPHPYGG-----QGTLSQYLLVdPKKDKKSItrkpENISLEEAA-AWPLvlgtAYQILEDLGQKLGPDSKVLVLGGS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1806958860 173 -PIGLLLLQAFRNAGAAPIVVSELDDERRELAAELGADAVVD 213
Cdd:cd08247   162 tSVGRFAIQLAKNHYNIGTVVGTCSSRSAELNKKLGADHFID 203
oxido_YhdH TIGR02823
putative quinone oxidoreductase, YhdH/YhfP family; This model represents a subfamily of ...
 53-339 6.97e-06

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


Pssm-ID: 274315 [Multi-domain]  Cd Length: 323  Bit Score: 47.17  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  53 PLVLGHESAGTVAEvgDDVAGFEVGDRVAINptvpcnacSYcKRGETHlcenntsiggagetilDGAFAEYVRVPAINVE 132
Cdd:TIGR02823  57 PMIPGIDAAGTVVS--SEDPRFREGDEVIVT--------GY-GLGVSH----------------DGGYSQYARVPADWLV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 133 DIGE-MSFEHAAL-------AeplACCVHGVEEVDVKPGD-SVAIIGA-GPIGLLLLQAFRNAGAAPIVVSELDDErREL 202
Cdd:TIGR02823 110 PLPEgLSLREAMAlgtagftA---ALSVMALERNGLTPEDgPVLVTGAtGGVGSLAVAILSKLGYEVVASTGKAEE-EDY 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 203 AAELGADAVVDPNE--DDPEAAIPAAAGGPVD-VGAEAI-GLVPTIEQANAVTAPGgstLVFGvPDQEATmeISPFD--- 275
Cdd:TIGR02823 186 LKELGASEVIDREDlsPPGKPLEKERWAGAVDtVGGHTLaNVLAQLKYGGAVAACG---LAGG-PDLPTT--VLPFIlrg 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806958860 276 ---VFFDEVGYrgSFSLTTEDFERAVTLLRYGRVDAdalVTERIGLEDLPTAFERMGNAEGLKKVVV 339
Cdd:TIGR02823 260 vslLGIDSVYC--PMALREAAWQRLATDLKPRNLES---ITREITLEELPEALEQILAGQHRGRTVV 321
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
140-338 3.41e-05

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 44.24  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 140 EHAALAEPLACCVHGVEEV-------DVKPgDSVAIIGAGPIGLLLLQAFRNAGAAPIVV----SELDDERRELAAELGA 208
Cdd:pfam16912   2 DVGFLVEPLSIVEKAIEHAeasrsrfEWRP-RSALVLGNGPLGLLALAMLRVQRGFDRVYclgrRDRPDPTIDLVEELGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 209 ---DAVVDPNEDDPEaaipaaAGGPVDVGAEAIGLVPTIEQANAVTAPGGSTLVFGVP-DQEATMEISPF--DVFFDEVG 282
Cdd:pfam16912  81 tyvDSRETPVDEIPA------AHEPMDLVYEATGYAPHAFEAIDALAPNGVAALLGVPtSWTFEIDGGALhrELVLHNKA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1806958860 283 YRGSFSLTTEDFERAV-TLLRYGRVDADALVTERIGLEDLPTAFERmgNAEGLKKVV 338
Cdd:pfam16912 155 LVGSVNANRRHFEAAAdTLAAAPEWFLDALVTGVVPLDEFEEAFED--GDDDIKTVV 209
ETR cd08290
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ...
 20-80 3.31e-04

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: 42.21  E-value: 3.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1806958860  20 PEPAADEVLVQVGACGVCMTDYHMYHGT------FAVETPLVLGHESAGTVAEVGDDVAGFEVGDRV 80
Cdd:cd08290    25 PPGPPNEVLVKMLAAPINPADINQIQGVypikppTTPEPPAVGGNEGVGEVVKVGSGVKSLKPGDWV 91
MDR_yhfp_like cd08289
Yhfp putative quinone oxidoreductases; yhfp putative quinone oxidoreductases (QOR). QOR ...
 25-220 3.58e-04

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


Pssm-ID: 176249 [Multi-domain]  Cd Length: 326  Bit Score: 41.93  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860  25 DEVLVQVGACGVCMTD--YHMYHGTFAVETPLVLGHESAGTVAEVGDdvAGFEVGDRVAinptvpcnACSYcKRGETHlc 102
Cdd:cd08289    28 GDVLIRVAYSSVNYKDglASIPGGKIVKRYPFIPGIDLAGTVVESND--PRFKPGDEVI--------VTSY-DLGVSH-- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806958860 103 enntsiggagetilDGAFAEYVRVPAINVEDIGE-------MSFEHAALAEPLAccVHGVEEVDVKP-GDSVAIIGA-GP 173
Cdd:cd08289    95 --------------HGGYSEYARVPAEWVVPLPKgltlkeaMILGTAGFTAALS--IHRLEENGLTPeQGPVLVTGAtGG 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1806958860 174 IGLLLLQAFRNAGAApIVVSELDDERRELAAELGADAVVDPNEDDPE 220
Cdd:cd08289   159 VGSLAVSILAKLGYE-VVASTGKADAADYLKKLGAKEVIPREELQEE 204
hemA PRK00045
glutamyl-tRNA reductase; Reviewed
 163-211 3.25e-03

glutamyl-tRNA reductase; Reviewed


Pssm-ID: 234592 [Multi-domain]  Cd Length: 423  Bit Score: 39.01  E-value: 3.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1806958860 163 GDSVAIIGAGPIGLLLLQAFRNAGAAPIVVSELDDER-RELAAELGADAV 211
Cdd:PRK00045  182 GKKVLVIGAGEMGELVAKHLAEKGVRKITVANRTLERaEELAEEFGGEAI 231
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 166-216 3.91e-03

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 38.51  E-value: 3.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1806958860 166 VAIIGAGPIGLLLLQAFRNAGAAP--IVVSELDDERRE-LAAELGADAVVDPNE 216
Cdd:COG0345     5 IGFIGAGNMGSAIIKGLLKSGVPPedIIVSDRSPERLEaLAERYGVRVTTDNAE 58
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 166-200 5.70e-03

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 38.24  E-value: 5.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1806958860 166 VAIIGAGPIGLLLLQAFRNAGAAPIVVselddERR 200
Cdd:PRK08243    5 VAIIGAGPAGLLLGQLLHLAGIDSVVL-----ERR 34
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 156-192 7.08e-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: 7.08e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1806958860 156 EEVDVKPGDSVAIIGAGPIGLLLLQAFRNAGAAPIVV 192
Cdd:COG0446   117 EALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLV 153
 
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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