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Conserved domains on  [gi|586176599|gb|EWP82568|]
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alcohol dehydrogenase [Staphylococcus aureus M1209]

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
MDR super family cl16912
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-341 0e+00

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.


The actual alignment was detected with superfamily member cd08237:

Pssm-ID: 450120 [Multi-domain]  Cd Length: 341  Bit Score: 511.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599   1 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPMSLVHEAVGEVVFDSKGVFEK 80
Cdd:cd08237    1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  81 GTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKS 160
Cdd:cd08237   81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 161 IPLKNSFGIWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ 240
Cdd:cd08237  161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLALLKGHEINVCTMQDI 320
Cdd:cd08237  241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                        330       340
                 ....*....|....*....|.
gi 586176599 321 VQAFEMDLSTSWGKTVLKWTI 341
Cdd:cd08237  321 HRAFESDLTNSWGKTVMEWEV 341
 
Name Accession Description Interval E-value
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 1-341 0e+00

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: 511.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599   1 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPMSLVHEAVGEVVFDSKGVFEK 80
Cdd:cd08237    1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  81 GTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKS 160
Cdd:cd08237   81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 161 IPLKNSFGIWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ 240
Cdd:cd08237  161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLALLKGHEINVCTMQDI 320
Cdd:cd08237  241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                        330       340
                 ....*....|....*....|.
gi 586176599 321 VQAFEMDLSTSWGKTVLKWTI 341
Cdd:cd08237  321 HRAFESDLTNSWGKTVMEWEV 341
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 26-340 2.27e-40

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: 144.51  E-value: 2.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEQHH 96
Cdd:COG1063   25 GEVLVRVTAVGICGSDLHIYRGGYP----FVRPPLVLGHEFVGEVVEVGEGVtgLKVGDRVVVEPNIPcgecrycRRGRY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  97 IIAENYlasSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKsiplknsFG----IWGD 172
Cdd:COG1063  101 NLCENL---QFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERAGVK-------PGdtvlVIGA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 173 GNLGYITAILLRkLYPEAKIYVFGKTDYKLS-----------HFSFVDDIFTVNQIPDDLKIDHAFECVGgkgSQVALQQ 241
Cdd:COG1063  171 GPIGLLAALAAR-LAGAARVIVVDRNPERLElarelgadavvNPREEDLVEAVRELTGGRGADVVIEAVG---APAALEQ 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 242 IVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLAllkGHEInvcTMQDIV 321
Cdd:COG1063  247 ALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLI---THRF---PLDDAP 320

                        330       340
                 ....*....|....*....|.
gi 586176599 322 QAFEM--DLSTSWGKTVLKWT 340
Cdd:COG1063  321 EAFEAaaDRADGAIKVVLDPD 341
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 28-130 1.86e-10

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: 57.23  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599   28 VIVRPLYLSICAADQRYYTGRRdenvLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEQHhii 98
Cdd:pfam08240   3 VLVKVKAAGICGSDLHIYKGGN----PPVKLPLILGHEFAGEVVEVGPGVtgLKVGDRVVVEPLIPcgkceycREGR--- 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 586176599   99 aENYLASSYFRSSGYDGFMQDYVVMAHDRIVP 130
Cdd:pfam08240  76 -YNLCPNGRFLGYDRDGGFAEYVVVPERNLVP 106
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 26-293 5.13e-08

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 53.89  E-value: 5.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAAD----QRYYTgrrdenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVV---MVPNTPTEQHH 96
Cdd:PRK13771  26 DEVVIKVNYAGLCYRDllqlQGFYP--------RMKYPVILGHEVVGTVEEVGENVkgFKPGDRVAsllYAPDGTCEYCR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  97 IIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELV-SVSYHAIQRFERKsiPLKNSFGIWGDGNL 175
Cdd:PRK13771  98 SGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVtGMVYRGLRRAGVK--KGETVLVTGAGGGV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 176 GyITAILLRKLY---------PEAKIYVFGKtdyklshfsFVDDIFTVNQIPDDLK----IDHAFECVGGKgsqvALQQI 242
Cdd:PRK13771 176 G-IHAIQVAKALgakviavtsSESKAKIVSK---------YADYVIVGSKFSEEVKkiggADIVIETVGTP----TLEES 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 586176599 243 VEHISPEGSIALLGVSELPVEVNTRL--VLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:PRK13771 242 LRSLNMGGKIIQIGNVDPSPTYSLRLgyIILKDIEIIGHISATKRDVEEALKL 294
 
Name Accession Description Interval E-value
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 1-341 0e+00

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: 511.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599   1 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPMSLVHEAVGEVVFDSKGVFEK 80
Cdd:cd08237    1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  81 GTKVVMVPNTPTEQHHIIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKS 160
Cdd:cd08237   81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 161 IPLKNSFGIWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ 240
Cdd:cd08237  161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLALLKGHEINVCTMQDI 320
Cdd:cd08237  241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                        330       340
                 ....*....|....*....|.
gi 586176599 321 VQAFEMDLSTSWGKTVLKWTI 341
Cdd:cd08237  321 HRAFESDLTNSWGKTVMEWEV 341
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 26-340 2.27e-40

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: 144.51  E-value: 2.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEQHH 96
Cdd:COG1063   25 GEVLVRVTAVGICGSDLHIYRGGYP----FVRPPLVLGHEFVGEVVEVGEGVtgLKVGDRVVVEPNIPcgecrycRRGRY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  97 IIAENYlasSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKsiplknsFG----IWGD 172
Cdd:COG1063  101 NLCENL---QFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERAGVK-------PGdtvlVIGA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 173 GNLGYITAILLRkLYPEAKIYVFGKTDYKLS-----------HFSFVDDIFTVNQIPDDLKIDHAFECVGgkgSQVALQQ 241
Cdd:COG1063  171 GPIGLLAALAAR-LAGAARVIVVDRNPERLElarelgadavvNPREEDLVEAVRELTGGRGADVVIEAVG---APAALEQ 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 242 IVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLAllkGHEInvcTMQDIV 321
Cdd:COG1063  247 ALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLI---THRF---PLDDAP 320

                        330       340
                 ....*....|....*....|.
gi 586176599 322 QAFEM--DLSTSWGKTVLKWT 340
Cdd:COG1063  321 EAFEAaaDRADGAIKVVLDPD 341
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 27-294 7.32e-28

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: 109.72  E-value: 7.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  27 HVIVRPLYLSICAADQRYYTGRRDEnvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEQHHIIAEnYLA 104
Cdd:cd05188    1 EVLVRVEAAGLCGTDLHIRRGGYPP---PPKLPLILGHEGAGVVVEVGPGVtgVKVGDRVVVLPNLGCGTCELCRE-LCP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 105 SSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLST-ISYTELVSVSYHAIqrFERKSIPLKNSFGIWGDGNLGYITAILL 183
Cdd:cd05188   77 GGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEaALLPEPLATAYHAL--RRAGVLKPGDTVLVLGAGGVGLLAAQLA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 184 RKLYpeAKIYVFGKTDYKLS------HFSFVD----DIFTVNQIPDDLKIDHAFECVGGKGsqvALQQIVEHISPEGSIA 253
Cdd:cd05188  155 KAAG--ARVIVTDRSDEKLElakelgADHVIDykeeDLEEELRLTGGGGADVVIDAVGGPE---TLAQALRLLRPGGRIV 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 586176599 254 LLGV-SELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLY 294
Cdd:cd05188  230 VVGGtSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 37-296 1.21e-20

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: 91.15  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  37 ICAADQRYYTGrrdENVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEQHHIIA---ENYLASSYFRSS 111
Cdd:cd08254   38 VCHSDLHILDG---GVPTLTKLPLTLGHEIAGTVVEVGAGVtnFKVGDRVAVPAVIPCGACALCRrgrGNLCLNQGMPGL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 112 GYDGFMQDYVVMAHDRIVPLPNDIDLSTISY-TELVSVSYHAIQRfeRKSIPLKNSFGIWGDGNLGyITAILLRKLYpEA 190
Cdd:cd08254  115 GIDGGFAEYIVVPARALVPVPDGVPFAQAAVaTDAVLTPYHAVVR--AGEVKPGETVLVIGLGGLG-LNAVQIAKAM-GA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 191 KIYVF----GKTDYKLSH------FSFVDDIFTVNQIPDDLKIDHAFECVggkGSQVALQQIVEHISPEGSIALLGVSEL 260
Cdd:cd08254  191 AVIAVdikeEKLELAKELgadevlNSLDDSPKDKKAAGLGGGFDVIFDFV---GTQPTFEDAQKAVKPGGRIVVVGLGRD 267

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 586176599 261 PVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRK 296
Cdd:cd08254  268 KLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAK 303
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 26-337 2.41e-18

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: 84.59  E-value: 2.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAAD-QRYY-TGRRdenvlrkKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP------TEQH 95
Cdd:cd08236   25 GEVLVKVKACGICGSDiPRYLgTGAY-------HPPLVLGHEFSGTVEEVGSGVddLAVGDRVAVNPLLPcgkceyCKKG 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  96 H-IIAENYlasSYFRSSgYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFErksIPLKNSFGIWGDGN 174
Cdd:cd08236   98 EySLCSNY---DYIGSR-RDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAAVALHAVRLAG---ITLGDTVVVIGAGT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 175 LGyITAILLRKLYPEAKIYVFGKTDYKLS---HFSFvDDIF--------TVNQIPDDLKIDHAFECVggkGSQVALQQIV 243
Cdd:cd08236  171 IG-LLAIQWLKILGAKRVIAVDIDDEKLAvarELGA-DDTInpkeedveKVRELTEGRGADLVIEAA---GSPATIEQAL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 244 EHISPEGSIALLGVSELPV---EVNTRLVLEKGLTLIGS--SRSGS---KDFEQVVDLYRKypdivEKLAL--LKGHEIn 313
Cdd:cd08236  246 ALARPGGKVVLVGIPYGDVtlsEEAFEKILRKELTIQGSwnSYSAPfpgDEWRTALDLLAS-----GKIKVepLITHRL- 319

                        330       340
                 ....*....|....*....|....*.
gi 586176599 314 vcTMQDIVQAFEM--DLSTSWGKTVL 337
Cdd:cd08236  320 --PLEDGPAAFERlaDREEFSGKVLL 343
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 28-314 2.90e-17

(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: 81.43  E-value: 2.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  28 VIVRPLYLSICAADQRYYTG-------RRDENVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEQ-HHI 97
Cdd:cd08233   27 VKIKVAWCGICGSDLHEYLDgpifiptEGHPHLTGETAPVTLGHEFSGVVVEVGSGVtgFKVGDRVVVEPTIKCGTcGAC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  98 IAENYLASSYFRS---SGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKsipLKNSFGIWGDGN 174
Cdd:cd08233  107 KRGLYNLCDSLGFiglGGGGGGFAEYVVVPAYHVHKLPDNVPLEEAALVEPLAVAWHAVRRSGFK---PGDTALVLGAGP 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 175 LGyITAILLRKLYPEAKIYVF--GKTDYKLSHFSFVDDIF---------TVNQIPDDLKIDHAFECVggkGSQVALQQIV 243
Cdd:cd08233  184 IG-LLTILALKAAGASKIIVSepSEARRELAEELGATIVLdptevdvvaEVRKLTGGGGVDVSFDCA---GVQATLDTAI 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 244 EHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLY------------RKYP--DIVEK--LALL 307
Cdd:cd08233  260 DALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGSICYTREDFEEVIDLLasgkidaeplitSRIPleDIVEKgfEELI 339


                 ....*..
gi 586176599 308 KGHEINV 314
Cdd:cd08233  340 NDKEQHV 346
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 23-293 4.85e-16

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: 77.36  E-value: 4.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  23 IYGNHVIVRPLYLSICAADQRYYTGRrDENVlrkKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPN-------TPTE 93
Cdd:cd08258   24 PGPGEVLIKVAAAGICGSDLHIYKGD-YDPV---ETPVVLGHEFSGTIVEVGPDVegWKVGDRVVSETTfstcgrcPYCR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  94 QHHiiaenYLASSYFRSSGY--DGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIqrFERKSIPLKNSFGIWG 171
Cdd:cd08258  100 RGD-----YNLCPHRKGIGTqaDGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAVHAV--AERSGIRPGDTVVVFG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 172 DGNLGYITAILLRKLypEAKIYVFGKTD----YKLSHFSFVDDIFT--------VNQIPDDLKIDHAFECvggKGSQVAL 239
Cdd:cd08258  173 PGPIGLLAAQVAKLQ--GATVVVVGTEKdevrLDVAKELGADAVNGgeedlaelVNEITDGDGADVVIEC---SGAVPAL 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 586176599 240 QQIVEHISPEGSIALLGV-SELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:cd08258  248 EQALELLRKGGRIVQVGIfGPLAASIDVERIIQKELSVIGSRSSTPASWETALRL 302
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 28-293 2.90e-15

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: 75.74  E-value: 2.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  28 VIVRPLYLSICAADQRYYT-GRRDENVLRKklPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP---------TEQH 95
Cdd:cd08232   24 VRVRVAAGGICGSDLHYYQhGGFGTVRLRE--PMVLGHEVSGVVEAVGPGVtgLAPGQRVAVNPSRPcgtcdycraGRPN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  96 HiiaenYLASSYFRSSGY----DGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFErkSIPLKNSFgIWG 171
Cdd:cd08232  102 L-----CLNMRFLGSAMRfphvQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNRAG--DLAGKRVL-VTG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 172 DGNLGYITAILLRKLyPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDL--------KIDHAFECvggKGSQVALQQIV 243
Cdd:cd08232  174 AGPIGALVVAAARRA-GAAEIVATDLADAPLAVARAMGADETVNLARDPLaayaadkgDFDVVFEA---SGAPAALASAL 249

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 586176599 244 EHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSkDFEQVVDL 293
Cdd:cd08232  250 RVVRPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSFRFDD-EFAEAVRL 298
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 28-264 4.93e-14

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: 71.92  E-value: 4.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  28 VIVRPLYLSICAADQRYYTGRrdenVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEQHHII 98
Cdd:cd05278   28 AIVRVTATSICGSDLHIYRGG----VPGAKHGMILGHEFVGEVVEVGSDVkrLKPGDRVSVPCITFcgrcrfcRRGYHAH 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  99 AENYLASSYFrSSGYDGFMQDYVVMAH-DR-IVPLPNDI---DLSTISytELVSVSYHAIqrfERKSIPLKNSFGIWGDG 173
Cdd:cd05278  104 CENGLWGWKL-GNRIDGGQAEYVRVPYaDMnLAKIPDGLpdeDALMLS--DILPTGFHGA---ELAGIKPGSTVAVIGAG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 174 NLGyITAILLRKLYPEAKIYVFGKTDYKLSHFSFV--DDIFT------VNQIPDDLK---IDHAFECVGGKGSqvaLQQI 242
Cdd:cd05278  178 PVG-LCAVAGARLLGAARIIAVDSNPERLDLAKEAgaTDIINpkngdiVEQILELTGgrgVDCVIEAVGFEET---FEQA 253

                        250       260
                 ....*....|....*....|..
gi 586176599 243 VEHISPEGSIALLGVSELPVEV 264
Cdd:cd05278  254 VKVVRPGGTIANVGVYGKPDPL 275
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 26-315 2.12e-13

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: 69.91  E-value: 2.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADQRYYTGRrdeNVLrKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEqhHIIA---- 99
Cdd:cd08261   25 GEVLVRVKRVGICGSDLHIYHGR---NPF-ASYPRILGHELSGEVVEVGEGVagLKVGDRVVVDPYISCG--ECYAcrkg 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 100 -ENYLASSYFRSSGYDGFMQDYVVMAHDRiVPLPNDIDLSTISYTELVSVSYHAIQR--FERKSIPLknsfgIWGDGNLG 176
Cdd:cd08261   99 rPNCCENLQVLGVHRDGGFAEYIVVPADA-LLVPEGLSLDQAALVEPLAIGAHAVRRagVTAGDTVL-----VVGAGPIG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 177 YITAILLRKLYpeAKIYVFGKTDYKLS-----------HFSFVDDIFTVNQIPDDLKIDHAFECVGgkgSQVALQQIVEH 245
Cdd:cd08261  173 LGVIQVAKARG--ARVIVVDIDDERLEfarelgaddtiNVGDEDVAARLRELTDGEGADVVIDATG---NPASMEEAVEL 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 246 ISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYP--------------DIVEKLALLKGHE 311
Cdd:cd08261  248 VAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKvdpealithrfpfeDVPEAFDLWEAPP 327


                 ....
gi 586176599 312 INVC 315
Cdd:cd08261  328 GGVI 331
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 25-339 9.48e-13

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


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 68.40  E-value: 9.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  25 GNHVIVRPLYLSICAADQRYYTGR-------RDENVLRkklpmslvHEAVGEVVFDSKGV-FEKGTKVVMV---PNTPTE 93
Cdd:cd08230   25 PGEVLVRTLEVGVCGTDREIVAGEygtappgEDFLVLG--------HEALGVVEEVGDGSgLSPGDLVVPTvrrPPGKCL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  94 QHHIIAENYLASSYFRS---SGYDGFMQDYVVMAHDRIVPLPNDI-DLSTIsyTELVSV---SYHAIQRFERKSIPL--K 164
Cdd:cd08230   97 NCRIGRPDFCETGEYTErgiKGLHGFMREYFVDDPEYLVKVPPSLaDVGVL--LEPLSVvekAIEQAEAVQKRLPTWnpR 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 165 NSFgIWGDGNLGYITAILLRKLYPEAkiYVFGKTDYKLSHFSFVDDI---------FTVNQIPDDLKIDHAFECVggkGS 235
Cdd:cd08230  175 RAL-VLGAGPIGLLAALLLRLRGFEV--YVLNRRDPPDPKADIVEELgatyvnsskTPVAEVKLVGEFDLIIEAT---GV 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 236 QVALQQIVEHISPEGSIALLGVS----ELPV---EVNTRLVLeKGLTLIGSSRSGSKDFEQVVD----LYRKYPDIVEKL 304
Cdd:cd08230  249 PPLAFEALPALAPNGVVILFGVPgggrEFEVdggELNRDLVL-GNKALVGSVNANKRHFEQAVEdlaqWKYRWPGVLERL 327

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 586176599 305 aLLKGHEINvctmqDIVQAFEMDLSTSWgKTVLKW 339
Cdd:cd08230  328 -ITRRVPLE-----EFAEALTEKPDGEI-KVVIEW 355
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 28-308 9.78e-13

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: 67.97  E-value: 9.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  28 VIVRPLYLSICAADQRYYTGRRdENVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPnTPTEQH----HIIAEN 101
Cdd:cd05284   28 VLVRVGGAGVCHSDLHVIDGVW-GGILPYKLPFTLGHENAGWVEEVGSGVdgLKEGDPVVVHP-PWGCGTcrycRRGEEN 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 102 YLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTIS-YTELVSVSYHAIqrfeRKSIPLKN---SFGIWGDGNLGY 177
Cdd:cd05284  106 YCENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLDPVEAApLADAGLTAYHAV----KKALPYLDpgsTVVVIGVGGLGH 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 178 ITAILLRKLYPeAKIYVFGKTDYKL-------SHFSFVDDIFT---VNQIPDDLKIDHAFECVggkGSQVALQQIVEHIS 247
Cdd:cd05284  182 IAVQILRALTP-ATVIAVDRSEEALklaerlgADHVLNASDDVveeVRELTGGRGADAVIDFV---GSDETLALAAKLLA 257

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586176599 248 PEGSIALLGVSElPVEVNTRLVLEKGLTLIGS---SRSgskDFEQVVDLYR---------KYP--DIVEKLALLK 308
Cdd:cd05284  258 KGGRYVIVGYGG-HGRLPTSDLVPTEISVIGSlwgTRA---ELVEVVALAEsgkvkveitKFPleDANEALDRLR 328
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 36-293 1.84e-12

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: 67.24  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  36 SICAADQR-YYTGRRDenvlrKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEQHHIIAENYLAS 105
Cdd:cd08235   35 GICGTDVKkIRGGHTD-----LKPPRILGHEIAGEIVEVGDGVtgFKVGDRVFVAPHVPcgechycLRGNENMCPNYKKF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 106 SYfrssGYD-GFMQDYVVMA----HDRIVPLPNDIDLSTISYTELVSVSYHAIqrfERKSIPLKNSFGIWGDGNLGYITA 180
Cdd:cd08235  110 GN----LYDgGFAEYVRVPAwavkRGGVLKLPDNVSFEEAALVEPLACCINAQ---RKAGIKPGDTVLVIGAGPIGLLHA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 181 iLLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKiDHAFECVGGKGSQV---------ALQQIVEHISPEGS 251
Cdd:cd08235  183 -MLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLV-EKVRELTDGRGADVvivatgspeAQAQALELVRKGGR 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 586176599 252 IALLGV--SELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:cd08235  261 ILFFGGlpKGSTVNIDPNLIHYREITITGSYAASPEDYKEALEL 304
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 26-293 1.93e-11

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: 64.26  E-value: 1.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEQ-HHIIA--E 100
Cdd:cd08259   26 GEVLIKVKAAGVCYRDLLFWKGFFP----RGKYPLILGHEIVGTVEEVGEGVerFKPGDRVILYYYIPCGKcEYCLSgeE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 101 NYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELV-SVSYHAIqrfeRKSIPLKNSfgIW----GDGNL 175
Cdd:cd08259  102 NLCRNRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVvGTAVHAL----KRAGVKKGD--TVlvtgAGGGV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 176 GyITAILLRKLYpEAKIYVFGKTDYKLS--HFSFVDDIFTVNQIPDDLK----IDHAFECVGGKgsqvALQQIVEHISPE 249
Cdd:cd08259  176 G-IHAIQLAKAL-GARVIAVTRSPEKLKilKELGADYVIDGSKFSEDVKklggADVVIELVGSP----TIEESLRSLNKG 249

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 586176599 250 GSIALLG-VSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:cd08259  250 GRLVLIGnVTPDPAPLRPGLLILKEIRIIGSISATKADVEEALKL 294
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 26-326 1.50e-10

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 61.28  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMvpntpteqHHIIA---- 99
Cdd:COG1064   26 GEVLVKVEACGVCHSDLHVAEGEWP----VPKLPLVPGHEIVGRVVAVGPGVtgFKVGDRVGV--------GWVDScgtc 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 100 -------ENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTI-SYTELVSVSYHAIQRFErksIPLKNSFGIWG 171
Cdd:COG1064   94 eycrsgrENLCENGRFTGYTTDGGYAEYVVVPARFLVKLPDGLDPAEAaPLLCAGITAYRALRRAG---VGPGDRVAVIG 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 172 DGNLGYITAILLRKLypEAKIYVFGKTDYKL--------SHFSFVDDIFTVNQIPDDLKIDHAFECVggkGSQVALQQIV 243
Cdd:COG1064  171 AGGLGHLAVQIAKAL--GAEVIAVDRSPEKLelarelgaDHVVNSSDEDPVEAVRELTGADVVIDTV---GAPATVNAAL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 244 EHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYpdiveKLALlkghEINVCTMQDIVQA 323
Cdd:COG1064  246 ALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEG-----KIKP----EVETIPLEEANEA 316


                 ...
gi 586176599 324 FEM 326
Cdd:COG1064  317 LER 319
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 28-341 1.78e-10

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: 61.36  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  28 VIVRPLYLSICAADQRYYT-GRRDENVLRKklPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEQhhiiAENYLA 104
Cdd:cd05285   25 VLVRVRAVGICGSDVHYYKhGRIGDFVVKE--PMVLGHESAGTVVAVGSGVthLKVGDRVAIEPGVPCRT----CEFCKS 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 105 SSY-------FRSS-GYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQrfeRKSIPLKNSFGIWGDGNLG 176
Cdd:cd05285   99 GRYnlcpdmrFAATpPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACR---RAGVRPGDTVLVFGAGPIG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 177 YITAILLrKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLK--------------IDHAFECVggkGSQVALQQI 242
Cdd:cd05285  176 LLTAAVA-KAFGATKVVVTDIDPSRLEFAKELGATHTVNVRTEDTPesaekiaellggkgPDVVIECT---GAESCIQTA 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 243 VEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRsgskdfeqvvdlYRK-YPDIVEklaLLKGHEINVCTM---- 317
Cdd:cd05285  252 IYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFR------------YANtYPTAIE---LLASGKVDVKPLithr 316

                        330       340
                 ....*....|....*....|....*..
gi 586176599 318 ---QDIVQAFEMDLSTSwgKTVLKWTI 341
Cdd:cd05285  317 fplEDAVEAFETAAKGK--KGVIKVVI 341
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 28-130 1.86e-10

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: 57.23  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599   28 VIVRPLYLSICAADQRYYTGRRdenvLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEQHhii 98
Cdd:pfam08240   3 VLVKVKAAGICGSDLHIYKGGN----PPVKLPLILGHEFAGEVVEVGPGVtgLKVGDRVVVEPLIPcgkceycREGR--- 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 586176599   99 aENYLASSYFRSSGYDGFMQDYVVMAHDRIVP 130
Cdd:pfam08240  76 -YNLCPNGRFLGYDRDGGFAEYVVVPERNLVP 106
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
219-293 4.81e-10

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 56.85  E-value: 4.81e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586176599  219 DDLKIDHAFECVGgkgSQVALQQIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:pfam00107  55 GGKGVDVVFDCVG---SPATLEQALKLLRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDL 126
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-325 2.45e-09

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


Pssm-ID: 176204 [Multi-domain]  Cd Length: 319  Bit Score: 57.64  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  28 VIVRPLYLSICAADQRYYTGRrdenvlrKKLPMSLVHEAVGEVVfDSKGVFEKGTKVVMVPNTPTEQ---------HHII 98
Cdd:cd08242   27 ALVRVLLAGICNTDLEIYKGY-------YPFPGVPGHEFVGIVE-EGPEAELVGKRVVGEINIACGRceycrrglyTHCP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  99 AENYLASSyfrssGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTE-LVSvsyhAIQRFERKSIPLKNSFGIWGDGNLGY 177
Cdd:cd08242   99 NRTVLGIV-----DRDGAFAEYLTLPLENLHVVPDLVPDEQAVFAEpLAA----ALEILEQVPITPGDKVAVLGDGKLGL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 178 ITAILLRKLypEAKIYVFGKTDYKLSHFSFVDdIFTVNQI---PDDLKIDHAFECVGgkgSQVALQQIVEHISPEGSIAL 254
Cdd:cd08242  170 LIAQVLALT--GPDVVLVGRHSEKLALARRLG-VETVLPDeaeSEGGGFDVVVEATG---SPSGLELALRLVRPRGTVVL 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586176599 255 LGVSELPVEVNTRLVLEKGLTLIGsSRSGskDFEQVVDLYRKypDIVEKLALLKGheinVCTMQDIVQAFE 325
Cdd:cd08242  244 KSTYAGPASFDLTKAVVNEITLVG-SRCG--PFAPALRLLRK--GLVDVDPLITA----VYPLEEALEAFE 305
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 7-293 6.64e-09

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: 56.38  E-value: 6.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599   7 QLVAPRQFDVTynNVD---IYGNHVIVRPLYLSICAADQRYYTGRrdenvLRKKLPMSLVHEAVGEVVFDSKGV--FEKG 81
Cdd:cd08234    5 VYEGPGELEVE--EVPvpePGPDEVLIKVAACGICGTDLHIYEGE-----FGAAPPLVPGHEFAGVVVAVGSKVtgFKVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  82 TKVVMVPNTPT---------EQHHiiAENYLAssyfRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHA 152
Cdd:cd08234   78 DRVAVDPNIYCgecfycrrgRPNL--CENLTA----VGVTRNGGFAEYVVVPAKQVYKIPDNLSFEEAALAEPLSCAVHG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 153 IQRFErksIPLKNSFGIWGDGNLGYITAILLrKLYPEAKIYVFGKTDYKL----SHFSFVddifTVNQIPDDLK------ 222
Cdd:cd08234  152 LDLLG---IKPGDSVLVFGAGPIGLLLAQLL-KLNGASRVTVAEPNEEKLelakKLGATE----TVDPSREDPEaqkedn 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586176599 223 ---IDHAFECVggkGSQVALQQIVEHISPEGSIALLGVS--ELPVEVNTRLVLEKGLTLIGsSRSGSKDFEQVVDL 293
Cdd:cd08234  224 pygFDVVIEAT---GVPKTLEQAIEYARRGGTVLVFGVYapDARVSISPFEIFQKELTIIG-SFINPYTFPRAIAL 295
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 37-339 7.38e-09

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: 56.17  E-value: 7.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  37 ICAADQRYYtgrRDENVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTkVVMVpntpteqHHIIA----EN------YLA 104
Cdd:cd08239   36 LCGSDLHYY---YHGHRAPAYQGVIPGHEPAGVVVAVGPGVthFRVGD-RVMV-------YHYVGcgacRNcrrgwmQLC 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 105 SSYFRSSGY--DGFMQDYVVMAHDRIVPLPNDIDLST---ISYTelVSVSYHAIQRFERKsipLKNSFGIWGDGNLGYIT 179
Cdd:cd08239  105 TSKRAAYGWnrDGGHAEYMLVPEKTLIPLPDDLSFADgalLLCG--IGTAYHALRRVGVS---GRDTVLVVGAGPVGLGA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 180 AILLRKLYPEAKIYV------------FGKTDYKLSHFSFVDDIFTVNQipdDLKIDHAFECvggKGSQVALQQIVEHIS 247
Cdd:cd08239  180 LMLARALGAEDVIGVdpsperlelakaLGADFVINSGQDDVQEIRELTS---GAGADVAIEC---SGNTAARRLALEAVR 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 248 PEGSIALLGV-SELPVEVNTRLVLeKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLAllkGHEINVctmQDIVQAFEM 326
Cdd:cd08239  254 PWGRLVLVGEgGELTIEVSNDLIR-KQRTLIGSWYFSVPDMEECAEFLARHKLEVDRLV---THRFGL---DQAPEAYAL 326

                        330
                 ....*....|...
gi 586176599 327 DLSTSWGKTVLKW 339
Cdd:cd08239  327 FAQGESGKVVFVF 339
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
169-338 4.49e-08

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 52.72  E-value: 4.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  169 IWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDI---------FTVNQIPD-DLKIDHAFECVGGkgSQVA 238
Cdd:pfam16912  36 VLGNGPLGLLALAMLRVQRGFDRVYCLGRRDRPDPTIDLVEELgatyvdsreTPVDEIPAaHEPMDLVYEATGY--APHA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  239 LQQIvEHISPEGSIALLGVS-----ELPV-EVNTRLVLEKgLTLIGSSRSGSKDFEQVVDLYRKYPDiveklALLKGHEI 312
Cdd:pfam16912 114 FEAI-DALAPNGVAALLGVPtswtfEIDGgALHRELVLHN-KALVGSVNANRRHFEAAADTLAAAPE-----WFLDALVT 186

                         170       180
                  ....*....|....*....|....*.
gi 586176599  313 NVCTMQDIVQAFEmdlstsWGKTVLK 338
Cdd:pfam16912 187 GVVPLDEFEEAFE------DGDDDIK 206
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 26-293 5.13e-08

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 53.89  E-value: 5.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAAD----QRYYTgrrdenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVV---MVPNTPTEQHH 96
Cdd:PRK13771  26 DEVVIKVNYAGLCYRDllqlQGFYP--------RMKYPVILGHEVVGTVEEVGENVkgFKPGDRVAsllYAPDGTCEYCR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  97 IIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELV-SVSYHAIQRFERKsiPLKNSFGIWGDGNL 175
Cdd:PRK13771  98 SGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVtGMVYRGLRRAGVK--KGETVLVTGAGGGV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 176 GyITAILLRKLY---------PEAKIYVFGKtdyklshfsFVDDIFTVNQIPDDLK----IDHAFECVGGKgsqvALQQI 242
Cdd:PRK13771 176 G-IHAIQVAKALgakviavtsSESKAKIVSK---------YADYVIVGSKFSEEVKkiggADIVIETVGTP----TLEES 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 586176599 243 VEHISPEGSIALLGVSELPVEVNTRL--VLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:PRK13771 242 LRSLNMGGKIIQIGNVDPSPTYSLRLgyIILKDIEIIGHISATKRDVEEALKL 294
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 10-152 2.13e-07

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 52.00  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  10 APRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYT-GRRDENVLrkKLPMSLVHEAVGEVV-FDSKGVFEkGTKVVMV 87
Cdd:PRK09880  12 GKKDVAVTEQEIEWNNNGTLVQITRGGICGSDLHYYQeGKVGNFVI--KAPMVLGHEVIGKIVhSDSSGLKE-GQTVAIN 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586176599  88 PNTPTEQ------HHiiaENYLAS-SYFRSSGYD-----GFMQdYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHA 152
Cdd:PRK09880  89 PSKPCGHckyclsHN---ENQCTTmRFFGSAMYFphvdgGFTR-YKVVDTAQCIPYPEKADEKVMAFAEPLAVAIHA 161
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 26-292 6.09e-07

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: 50.38  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADqrYYTGRRDENVLRKKLPMSLV---------HEAVGEVVF---DSKGVFEKGTKVVMVPNTPTE 93
Cdd:cd08262   24 GQVLVKVLACGICGSD--LHATAHPEAMVDDAGGPSLMdlgadivlgHEFCGEVVDygpGTERKLKVGTRVTSLPLLLCG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  94 QHHiiaenylASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERK--SIPLknsfgIWG 171
Cdd:cd08262  102 QGA-------SCGIGLSPEAPGGYAEYMLLSEALLLRVPDGLSMEDAALTEPLAVGLHAVRRARLTpgEVAL-----VIG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 172 DGNLGyITAILLRKLYPEAKIYVfgktdyklSHFS--------------FVDDI----FTVNQIPDD----LKIDHAFEC 229
Cdd:cd08262  170 CGPIG-LAVIAALKARGVGPIVA--------SDFSperralalamgadiVVDPAadspFAAWAAELAraggPKPAVIFEC 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586176599 230 VGGKGsqvALQQIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTL---IGSSRSgskDFEQVVD 292
Cdd:cd08262  241 VGAPG---LIQQIIEGAPPGGRIVVVGVCMESDNIEPALAIRKELTLqfsLGYTPE---EFADALD 300
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 9-325 1.11e-05

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: 46.48  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599   9 VAPRQFDVtynnVDIYGNHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGVFE--------K 80
Cdd:cd08231   13 LEIREVPL----PDLEPGAVLVRVRLAGVCGSDVHTVAGRRP----RVPLPIILGHEGVGRVVALGGGVTTdvageplkV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  81 GTKVVMVPNTPTEQ--HHIIAENYL-ASSYF----RSSGYD----GFMQDYVVMAHDRIVPLPNDI--DLSTISYTELVS 147
Cdd:cd08231   85 GDRVTWSVGAPCGRcyRCLVGDPTKcENRKKygheASCDDPhlsgGYAEHIYLPPGTAIVRVPDNVpdEVAAPANCALAT 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 148 VsYHAIQRFERksIPLKNSFGIWGDGNLGyITAILLRKLYPEAKIYVFGKTDYKL---SHFSfVDDIFTVNQIPDDLKID 224
Cdd:cd08231  165 V-LAALDRAGP--VGAGDTVVVQGAGPLG-LYAVAAAKLAGARRVIVIDGSPERLelaREFG-ADATIDIDELPDPQRRA 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 225 HAFECVGGKGSQV---------ALQQIVEHISPEGSIALLGV--SELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:cd08231  240 IVRDITGGRGADVvieasghpaAVPEGLELLRRGGTYVLVGSvaPAGTVPLDPERIVRKNLTIIGVHNYDPSHLYRAVRF 319

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 586176599 294 ----YRKYPdivekLALLKGHEInvcTMQDIVQAFE 325
Cdd:cd08231  320 lertQDRFP-----FAELVTHRY---PLEDINEALE 347
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 26-176 2.36e-04

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 42.61  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADqrYYTGRRDENVLRKKlpMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEQHHIIAENYL 103
Cdd:cd08285   25 NDAIVRPTAVAPCTSD--VHTVWGGAPGERHG--MILGHEAVGVVEEVGSEVkdFKPGDRVIVPAITPDWRSVAAQRGYP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 104 ASSYFRSSGY------DGFMQDYVVM--AHDRIVPLPNDIDLSTISY-TELVSVSYHAiqrFERKSIPLKNSFGIWGDGN 174
Cdd:cd08285  101 SQSGGMLGGWkfsnfkDGVFAEYFHVndADANLAPLPDGLTDEQAVMlPDMMSTGFHG---AELANIKLGDTVAVFGIGP 177


                 ..
gi 586176599 175 LG 176
Cdd:cd08285  178 VG 179
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 234-340 2.51e-04

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 42.50  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 234 GSQVALQQIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSsrSGSKDFE---QVVDLYRKYPDivekLALLKGH 310
Cdd:PRK05396 241 GAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWNKVIFKGLTIKGI--YGREMFEtwyKMSALLQSGLD----LSPIITH 314

                         90       100       110
                 ....*....|....*....|....*....|
gi 586176599 311 EInvcTMQDIVQAFEMDLSTSWGKTVLKWT 340
Cdd:PRK05396 315 RF---PIDDFQKGFEAMRSGQSGKVILDWD 341
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 28-326 5.24e-04

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 41.30  E-value: 5.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  28 VIVRPLYLSICAADQRYYTGRRDENVLRKKlPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEQHHIIAENYL-- 103
Cdd:PLN02702  44 VRVRMKAVGICGSDVHYLKTMRCADFVVKE-PMVIGHECAGIIEEVGSEVkhLVVGDRVALEPGISCWRCNLCKEGRYnl 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 104 --ASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQrfeRKSIPLKNSFGIWGDGNLGYITaI 181
Cdd:PLN02702 123 cpEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACR---RANIGPETNVLVMGAGPIGLVT-M 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 182 LLRKLYPEAKIYVFGKTDYKLSHFSFV--DDIFTVNQIPDDL-------------KIDHAFECVG-GKGSQVALqqivEH 245
Cdd:PLN02702 199 LAARAFGAPRIVIVDVDDERLSVAKQLgaDEIVLVSTNIEDVeseveeiqkamggGIDVSFDCVGfNKTMSTAL----EA 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 246 ISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRsgskdfeqvvdlYRK-YPDIVEklaLLKGHEINV---------C 315
Cdd:PLN02702 275 TRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFR------------YRNtWPLCLE---FLRSGKIDVkplithrfgF 339

                        330
                 ....*....|.
gi 586176599 316 TMQDIVQAFEM 326
Cdd:PLN02702 340 SQKEVEEAFET 350
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 214-338 6.12e-04

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: 41.29  E-value: 6.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 214 VNQIPDDLKIDHAFECVGGKgsqvALQQIVEHISPEGSIALLGV-SELPVEVNTRLVLEKGLTLIGSS-RSGSK-----D 286
Cdd:COG0604  200 VRALTGGRGVDVVLDTVGGD----TLARSLRALAPGGRLVSIGAaSGAPPPLDLAPLLLKGLTLTGFTlFARDPaerraA 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 586176599 287 FEQVVDLYRKypdivEKLALLKGHEInvcTMQDIVQAFE-MDLSTSWGKTVLK 338
Cdd:COG0604  276 LAELARLLAA-----GKLRPVIDRVF---PLEEAAEAHRlLESGKHRGKVVLT 320
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
224-295 8.35e-04

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 40.84  E-value: 8.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586176599 224 DHAFECVggkGSQVALQQIVEHISPEGSIALLGVS----ELPVEVNTRLVLEKGL--TLIGSSRsGSKDFEQVVDLYR 295
Cdd:COG1062  245 DYAFETT---GNPAVIRQALEALRKGGTVVVVGLAppgaEISLDPFQLLLTGRTIrgSYFGGAV-PRRDIPRLVDLYR 318
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 26-337 9.30e-04

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: 40.68  E-value: 9.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  26 NHVIVRPLYLSICAADQRYYtgRRDE-NVLRKKLPMSLVHEAVGEVVFDSKGVfekgtKVVMVPNTPTEQHHIIAEnyla 104
Cdd:cd05281   26 GEVLIKVLAASICGTDVHIY--EWDEwAQSRIKPPLIFGHEFAGEVVEVGEGV-----TRVKVGDYVSAETHIVCG---- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 105 SSYFRSSG--------------YDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFErksIPLKnSFGIW 170
Cdd:cd05281   95 KCYQCRTGnyhvcqntkilgvdTDGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVLAGD---VSGK-SVLIT 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 171 GDGNLGyITAILLRKLYPEAKIYVFGKTDY--KLSHFSFVDDIFTVNQIpDDLKIDHAFECVGG------KGSQVALQQI 242
Cdd:cd05281  171 GCGPIG-LMAIAVAKAAGASLVIASDPNPYrlELAKKMGADVVINPREE-DVVEVKSVTDGTGVdvvlemSGNPKAIEQG 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599 243 VEHISPEGSIALLGVSELPVEVN-TRLVLEKGLTLIGSsrSGSKDFE---QVVdlyrkypdiveklALLKGHEIN---VC 315
Cdd:cd05281  249 LKALTPGGRVSILGLPPGPVDIDlNNLVIFKGLTVQGI--TGRKMFEtwyQVS-------------ALLKSGKVDlspVI 313

                        330       340
                 ....*....|....*....|....*.
gi 586176599 316 T----MQDIVQAFEMDLSTSWGKTVL 337
Cdd:cd05281  314 ThklpLEDFEEAFELMRSGKCGKVVL 339
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 25-202 1.38e-03

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: 40.29  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  25 GNHVIVRPLYLSICAAD----QRYY---TGRRDENVLRK-KLPMSLVHEAVGEVVF---DSKGVfEKGTKVVMVP----- 88
Cdd:cd08240   25 GTEVLVKVTACGVCHSDlhiwDGGYdlgGGKTMSLDDRGvKLPLVLGHEIVGEVVAvgpDAADV-KVGDKVLVYPwigcg 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176599  89 --NTPTEQHhiiaENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISyTELVS--VSYHAIqrfeRKSIPL- 163
Cdd:cd08240  104 ecPVCLAGD----ENLCAKGRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAA-TLACSglTAYSAV----KKLMPLv 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 586176599 164 -KNSFGIWGDGNLGYITAILLRKLYPeAKIYVFGKTDYKL 202
Cdd:cd08240  175 aDEPVVIIGAGGLGLMALALLKALGP-ANIIVVDIDEAKL 213
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 28-87 5.85e-03

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: 38.13  E-value: 5.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586176599  28 VIVRPLYLSICAADQRYYTGRRDenvlrKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMV 87
Cdd:cd08281   36 VLVKIAAAGLCHSDLSVINGDRP-----RPLPMALGHEAAGVVVEVGEGVtdLEVGDHVVLV 92
 
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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