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Conserved domains on  [gi|2756312334|ref|WP_354671694|]
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alcohol dehydrogenase catalytic domain-containing protein [Staphylococcus aureus]

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: 509.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334   1 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPMSLVHEAVGEVVFDSKGVFEK 80
Cdd:cd08237     1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  81 GTKVVMVPNTPTEKHNVIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKS 160
Cdd:cd08237    81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 161 IPLKTSFGIWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ 240
Cdd:cd08237   161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLALLKGHEINVCTMQDI 320
Cdd:cd08237   241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                         330       340
                  ....*....|....*....|.
gi 2756312334 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: 509.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334   1 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPMSLVHEAVGEVVFDSKGVFEK 80
Cdd:cd08237     1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  81 GTKVVMVPNTPTEKHNVIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKS 160
Cdd:cd08237    81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 161 IPLKTSFGIWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ 240
Cdd:cd08237   161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLALLKGHEINVCTMQDI 320
Cdd:cd08237   241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                         330       340
                  ....*....|....*....|.
gi 2756312334 321 VQAFEMDLSTSWGKTVLKWTI 341
Cdd:cd08237   321 HRAFESDLTNSWGKTVMEWEV 341
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 26-340 9.85e-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: 142.97  E-value: 9.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP--------TEKH 95
Cdd:COG1063    25 GEVLVRVTAVGICGSDLHIYRGGYP----FVRPPLVLGHEFVGEVVEVGEGVtgLKVGDRVVVEPNIPcgecrycrRGRY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  96 NvIAENYlasSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKsiplktsFG----IWG 171
Cdd:COG1063   101 N-LCENL---QFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERAGVK-------PGdtvlVIG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 172 DGNLGYITAILLRkLYPEAKIYVFGKTDYKLS-----------HFSFVDDIFTVNQIPDDLKIDHAFECVGgkgSQVALQ 240
Cdd:COG1063   170 AGPIGLLAALAAR-LAGAARVIVVDRNPERLElarelgadavvNPREEDLVEAVRELTGGRGADVVIEAVG---APAALE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLAllkGHEInvcTMQDI 320
Cdd:COG1063   246 QALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLI---THRF---PLDDA 319

                         330       340
                  ....*....|....*....|..
gi 2756312334 321 VQAFEM--DLSTSWGKTVLKWT 340
Cdd:COG1063   320 PEAFEAaaDRADGAIKVVLDPD 341
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 28-130 3.16e-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: 56.46  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYTGRRdenvLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEK------HNvia 99
Cdd:pfam08240   3 VLVKVKAAGICGSDLHIYKGGN----PPVKLPLILGHEFAGEVVEVGPGVtgLKVGDRVVVEPLIPCGKceycreGR--- 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2756312334 100 ENYLASSYFRSSGYDGFMQDYVVMAHDRIVP 130
Cdd:pfam08240  76 YNLCPNGRFLGYDRDGGFAEYVVVPERNLVP 106
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 26-293 7.93e-09

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 56.20  E-value: 7.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAAD----QRYYTgrrdenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVV---MVPNTPTEKHN 96
Cdd:PRK13771   26 DEVVIKVNYAGLCYRDllqlQGFYP--------RMKYPVILGHEVVGTVEEVGENVkgFKPGDRVAsllYAPDGTCEYCR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  97 VIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELV-SVSYHAIQRFE--RKSIPLKTSFGiwgdG 173
Cdd:PRK13771   98 SGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVtGMVYRGLRRAGvkKGETVLVTGAG----G 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 174 NLGyITAILLRKLY---------PEAKIYVFGKtdyklshfsFVDDIFTVNQIPDDLK----IDHAFECVGGKgsqvALQ 240
Cdd:PRK13771  174 GVG-IHAIQVAKALgakviavtsSESKAKIVSK---------YADYVIVGSKFSEEVKkiggADIVIETVGTP----TLE 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVNTRL--VLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:PRK13771  240 ESLRSLNMGGKIIQIGNVDPSPTYSLRLgyIILKDIEIIGHISATKRDVEEALKL 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: 509.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334   1 MINQVYQLVAPRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYTGRRDENVLRKKLPMSLVHEAVGEVVFDSKGVFEK 80
Cdd:cd08237     1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  81 GTKVVMVPNTPTEKHNVIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKS 160
Cdd:cd08237    81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 161 IPLKTSFGIWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKIDHAFECVGGKGSQVALQ 240
Cdd:cd08237   161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLALLKGHEINVCTMQDI 320
Cdd:cd08237   241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                         330       340
                  ....*....|....*....|.
gi 2756312334 321 VQAFEMDLSTSWGKTVLKWTI 341
Cdd:cd08237   321 HRAFESDLTNSWGKTVMEWEV 341
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 26-340 9.85e-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: 142.97  E-value: 9.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP--------TEKH 95
Cdd:COG1063    25 GEVLVRVTAVGICGSDLHIYRGGYP----FVRPPLVLGHEFVGEVVEVGEGVtgLKVGDRVVVEPNIPcgecrycrRGRY 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  96 NvIAENYlasSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFERKsiplktsFG----IWG 171
Cdd:COG1063   101 N-LCENL---QFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVERAGVK-------PGdtvlVIG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 172 DGNLGYITAILLRkLYPEAKIYVFGKTDYKLS-----------HFSFVDDIFTVNQIPDDLKIDHAFECVGgkgSQVALQ 240
Cdd:COG1063   170 AGPIGLLAALAAR-LAGAARVIVVDRNPERLElarelgadavvNPREEDLVEAVRELTGGRGADVVIEAVG---APAALE 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLAllkGHEInvcTMQDI 320
Cdd:COG1063   246 QALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLI---THRF---PLDDA 319

                         330       340
                  ....*....|....*....|..
gi 2756312334 321 VQAFEM--DLSTSWGKTVLKWT 340
Cdd:COG1063   320 PEAFEAaaDRADGAIKVVLDPD 341
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 27-294 3.32e-27

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: 107.79  E-value: 3.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  27 HVIVRPLYLSICAADQRYYTGRRDEnvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEKHNVIAEnYLA 104
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPP---PPKLPLILGHEGAGVVVEVGPGVtgVKVGDRVVVLPNLGCGTCELCRE-LCP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 105 SSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLST-ISYTELVSVSYHAIQRFeRKSIPLKTsFGIWGDGNLGYITAILL 183
Cdd:cd05188    77 GGGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEaALLPEPLATAYHALRRA-GVLKPGDT-VLVLGAGGVGLLAAQLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 184 RKLYpeAKIYVFGKTDYKLS------HFSFVD----DIFTVNQIPDDLKIDHAFECVGGKGsqvALQQIVEHISPEGSIA 253
Cdd:cd05188   155 KAAG--ARVIVTDRSDEKLElakelgADHVIDykeeDLEEELRLTGGGGADVVIDAVGGPE---TLAQALRLLRPGGRIV 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2756312334 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 5.26e-21

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: 91.92  E-value: 5.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  37 ICAADQRYYTGrrdENVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMV-PNTPTEKHNVIA--ENYLASSYFRSS 111
Cdd:cd08254    38 VCHSDLHILDG---GVPTLTKLPLTLGHEIAGTVVEVGAGVtnFKVGDRVAVPaVIPCGACALCRRgrGNLCLNQGMPGL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 112 GYDGFMQDYVVMAHDRIVPLPNDIDLSTISY-TELVSVSYHAIQRfeRKSIPLKTSFGIWGDGNLGyITAILLRKLYpEA 190
Cdd:cd08254   115 GIDGGFAEYIVVPARALVPVPDGVPFAQAAVaTDAVLTPYHAVVR--AGEVKPGETVLVIGLGGLG-LNAVQIAKAM-GA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 191 KIYVF----GKTDYKLSH------FSFVDDIFTVNQIPDDLKIDHAFECVggkGSQVALQQIVEHISPEGSIALLGVSEL 260
Cdd:cd08254   191 AVIAVdikeEKLELAKELgadevlNSLDDSPKDKKAAGLGGGFDVIFDFV---GTQPTFEDAQKAVKPGGRIVVVGLGRD 267

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2756312334 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 5.65e-19

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: 86.51  E-value: 5.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAAD-QRYY-TGRRdenvlrkKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEK 94
Cdd:cd08236    25 GEVLVKVKACGICGSDiPRYLgTGAY-------HPPLVLGHEFSGTVEEVGSGVddLAVGDRVAVNPLLPcgkceycKKG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  95 HNVIAENYlasSYFRSSgYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFErksIPLKTSFGIWGDGN 174
Cdd:cd08236    98 EYSLCSNY---DYIGSR-RDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAAVALHAVRLAG---ITLGDTVVVIGAGT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 175 LGyITAILLRKLYPEAKIYVFGKTDYKLS---HFSFvDDIF--------TVNQIPDDLKIDHAFECVggkGSQVALQQIV 243
Cdd:cd08236   171 IG-LLAIQWLKILGAKRVIAVDIDDEKLAvarELGA-DDTInpkeedveKVRELTEGRGADLVIEAA---GSPATIEQAL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 244 EHISPEGSIALLGVSELPV---EVNTRLVLEKGLTLIGS--SRSGS---KDFEQVVDLYRKypdivEKLAL--LKGHEIn 313
Cdd:cd08236   246 ALARPGGKVVLVGIPYGDVtlsEEAFEKILRKELTIQGSwnSYSAPfpgDEWRTALDLLAS-----GKIKVepLITHRL- 319

                         330       340
                  ....*....|....*....|....*.
gi 2756312334 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 ...
 28-294 1.78e-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: 82.20  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYTG-------RRDENVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEKHN-V 97
Cdd:cd08233    27 VKIKVAWCGICGSDLHEYLDgpifiptEGHPHLTGETAPVTLGHEFSGVVVEVGSGVtgFKVGDRVVVEPTIKCGTCGaC 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  98 IAENYLASSYFRS---SGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRfeRKSIPLKTSFgIWGDGN 174
Cdd:cd08233   107 KRGLYNLCDSLGFiglGGGGGGFAEYVVVPAYHVHKLPDNVPLEEAALVEPLAVAWHAVRR--SGFKPGDTAL-VLGAGP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 175 LGyITAILLRKLYPEAKIYVF--GKTDYKLSHFSFVDDIF---------TVNQIPDDLKIDHAFECVggkGSQVALQQIV 243
Cdd:cd08233   184 IG-LLTILALKAAGASKIIVSepSEARRELAEELGATIVLdptevdvvaEVRKLTGGGGVDVSFDCA---GVQATLDTAI 259

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2756312334 244 EHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLY 294
Cdd:cd08233   260 DALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGSICYTREDFEEVIDLL 310
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 23-293 8.30e-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: 76.59  E-value: 8.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  23 IYGNHVIVRPLYLSICAADQRYYTGRrDENVlrkKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPT--EKHNVI 98
Cdd:cd08258    24 PGPGEVLIKVAAAGICGSDLHIYKGD-YDPV---ETPVVLGHEFSGTIVEVGPDVegWKVGDRVVSETTFSTcgRCPYCR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  99 AENYLASSYFRSSGY--DGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIqrFERKSIPLKTSFGIWGDGNLG 176
Cdd:cd08258   100 RGDYNLCPHRKGIGTqaDGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAVHAV--AERSGIRPGDTVVVFGPGPIG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 177 YITAILLRKLypEAKIYVFGKTD----YKLSHFSFVDDIFT--------VNQIPDDLKIDHAFECvggKGSQVALQQIVE 244
Cdd:cd08258   178 LLAAQVAKLQ--GATVVVVGTEKdevrLDVAKELGADAVNGgeedlaelVNEITDGDGADVVIEC---SGAVPALEQALE 252

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2756312334 245 HISPEGSIALLGV-SELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:cd08258   253 LLRKGGRIVQVGIfGPLAASIDVERIIQKELSVIGSRSSTPASWETALRL 302
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 26-315 1.61e-15

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: 76.46  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAADQRYYTGRrdeNVLrKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP--------TEKH 95
Cdd:cd08261    25 GEVLVRVKRVGICGSDLHIYHGR---NPF-ASYPRILGHELSGEVVEVGEGVagLKVGDRVVVDPYIScgecyacrKGRP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  96 NVIAENYLASSYfRssgyDGFMQDYVVMAHDRiVPLPNDIDLSTISYTELVSVSYHAIQR--FERKSIPLktsfgIWGDG 173
Cdd:cd08261   101 NCCENLQVLGVH-R----DGGFAEYIVVPADA-LLVPEGLSLDQAALVEPLAIGAHAVRRagVTAGDTVL-----VVGAG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 174 NLGYITAILLRKLYpeAKIYVFGKTDYKLS-----------HFSFVDDIFTVNQIPDDLKIDHAFECVGgkgSQVALQQI 242
Cdd:cd08261   170 PIGLGVIQVAKARG--ARVIVVDIDDERLEfarelgaddtiNVGDEDVAARLRELTDGEGADVVIDATG---NPASMEEA 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 243 VEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYP--------------DIVEKLALLK 308
Cdd:cd08261   245 VELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKvdpealithrfpfeDVPEAFDLWE 324


                  ....*..
gi 2756312334 309 GHEINVC 315
Cdd:cd08261   325 APPGGVI 331
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 28-293 1.21e-14

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: 73.81  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYT-GRRDENVLRKklPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP--------TEKHN 96
Cdd:cd08232    24 VRVRVAAGGICGSDLHYYQhGGFGTVRLRE--PMVLGHEVSGVVEAVGPGVtgLAPGQRVAVNPSRPcgtcdycrAGRPN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  97 ViaenYLASSYFRSSGY----DGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFErkSIPLKTSFgIWGD 172
Cdd:cd08232   102 L----CLNMRFLGSAMRfphvQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNRAG--DLAGKRVL-VTGA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 173 GNLGYITAILLRKLyPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDL--------KIDHAFECvggKGSQVALQQIVE 244
Cdd:cd08232   175 GPIGALVVAAARRA-GAAEIVATDLADAPLAVARAMGADETVNLARDPLaayaadkgDFDVVFEA---SGAPAALASALR 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2756312334 245 HISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSkDFEQVVDL 293
Cdd:cd08232   251 VVRPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSFRFDD-EFAEAVRL 298
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 28-264 3.24e-13

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: 69.61  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYTGRrdenVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTE-----KHNVIA- 99
Cdd:cd05278    28 AIVRVTATSICGSDLHIYRGG----VPGAKHGMILGHEFVGEVVEVGSDVkrLKPGDRVSVPCITFCGrcrfcRRGYHAh 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 100 -ENYLASSYFrSSGYDGFMQDYVVMAH-DR-IVPLPNDI---DLSTISytELVSVSYHAIqrfERKSIPLKTSFGIWGDG 173
Cdd:cd05278   104 cENGLWGWKL-GNRIDGGQAEYVRVPYaDMnLAKIPDGLpdeDALMLS--DILPTGFHGA---ELAGIKPGSTVAVIGAG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 174 NLGyITAILLRKLYPEAKIYVFGKTDYKLSHFSFV--DDIFT------VNQIPDDLK---IDHAFECVGGKGSqvaLQQI 242
Cdd:cd05278   178 PVG-LCAVAGARLLGAARIIAVDSNPERLDLAKEAgaTDIINpkngdiVEQILELTGgrgVDCVIEAVGFEET---FEQA 253

                         250       260
                  ....*....|....*....|..
gi 2756312334 243 VEHISPEGSIALLGVSELPVEV 264
Cdd:cd05278   254 VKVVRPGGTIANVGVYGKPDPL 275
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 36-293 9.45e-13

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: 68.01  E-value: 9.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  36 SICAADQR-YYTGRRDenvlrKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTP-------TEKHNVIAENYLAS 105
Cdd:cd08235    35 GICGTDVKkIRGGHTD-----LKPPRILGHEIAGEIVEVGDGVtgFKVGDRVFVAPHVPcgechycLRGNENMCPNYKKF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 106 SYfrssGYD-GFMQDYVVMA----HDRIVPLPNDIDLSTISYTELVSVSYHAIqrfERKSIPLKTSFGIWGDGNLGYITA 180
Cdd:cd08235   110 GN----LYDgGFAEYVRVPAwavkRGGVLKLPDNVSFEEAALVEPLACCINAQ---RKAGIKPGDTVLVIGAGPIGLLHA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 181 iLLRKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLKiDHAFECVGGKGSQV---------ALQQIVEHISPEGS 251
Cdd:cd08235   183 -MLAKASGARKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLV-EKVRELTDGRGADVvivatgspeAQAQALELVRKGGR 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2756312334 252 IALLGV--SELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:cd08235   261 ILFFGGlpKGSTVNIDPNLIHYREITITGSYAASPEDYKEALEL 304
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 25-339 1.41e-12

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


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 67.63  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  25 GNHVIVRPLYLSICAADQRYYTGR-------RDENVLRkklpmslvHEAVGEVVFDSKGV-FEKGTKVVMV---PNTPTE 93
Cdd:cd08230    25 PGEVLVRTLEVGVCGTDREIVAGEygtappgEDFLVLG--------HEALGVVEEVGDGSgLSPGDLVVPTvrrPPGKCL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  94 KHNVIAENYLASSYFRS---SGYDGFMQDYVVMAHDRIVPLPNDI-DLSTIsyTELVSVSYHAIQRFERKSIPLKTSFG- 168
Cdd:cd08230    97 NCRIGRPDFCETGEYTErgiKGLHGFMREYFVDDPEYLVKVPPSLaDVGVL--LEPLSVVEKAIEQAEAVQKRLPTWNPr 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 169 ---IWGDGNLGYITAILLRKLYPEAkiYVFGKTDYKLSHFSFVDDI---------FTVNQIPDDLKIDHAFECVggkGSQ 236
Cdd:cd08230   175 ralVLGAGPIGLLAALLLRLRGFEV--YVLNRRDPPDPKADIVEELgatyvnsskTPVAEVKLVGEFDLIIEAT---GVP 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 237 VALQQIVEHISPEGSIALLGVS----ELPV---EVNTRLVLeKGLTLIGSSRSGSKDFEQVVD----LYRKYPDIVEKLa 305
Cdd:cd08230   250 PLAFEALPALAPNGVVILFGVPgggrEFEVdggELNRDLVL-GNKALVGSVNANKRHFEQAVEdlaqWKYRWPGVLERL- 327

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2756312334 306 LLKGHEINvctmqDIVQAFEMDLSTSWgKTVLKW 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 1.75e-12

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: 67.20  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYTGRRdENVLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMvpntptekHNVIA------ 99
Cdd:cd05284    28 VLVRVGGAGVCHSDLHVIDGVW-GGILPYKLPFTLGHENAGWVEEVGSGVdgLKEGDPVVV--------HPPWGcgtcry 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 100 -----ENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTIS-YTELVSVSYHAIQRFERKSIPLKTSfGIWGDG 173
Cdd:cd05284    99 crrgeENYCENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLDPVEAApLADAGLTAYHAVKKALPYLDPGSTV-VVIGVG 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 174 NLGYITAILLRKLYPeAKIYVFGKTDYKL-------SHFSFVDDIFT---VNQIPDDLKIDHAFECVggkGSQVALQQIV 243
Cdd:cd05284   178 GLGHIAVQILRALTP-ATVIAVDRSEEALklaerlgADHVLNASDDVveeVRELTGGRGADAVIDFV---GSDETLALAA 253

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2756312334 244 EHISPEGSIALLGVSElPVEVNTRLVLEKGLTLIGS---SRSgskDFEQVVDLYR---------KYP--DIVEKLALLK 308
Cdd:cd05284   254 KLLAKGGRYVIVGYGG-HGRLPTSDLVPTEISVIGSlwgTRA---ELVEVVALAEsgkvkveitKFPleDANEALDRLR 328
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 26-326 6.12e-11

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 62.44  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMvpntptekHNVIA---- 99
Cdd:COG1064    26 GEVLVKVEACGVCHSDLHVAEGEWP----VPKLPLVPGHEIVGRVVAVGPGVtgFKVGDRVGV--------GWVDScgtc 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 100 -------ENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTI-SYTELVSVSYHAIQRFErksIPLKTSFGIWG 171
Cdd:COG1064    94 eycrsgrENLCENGRFTGYTTDGGYAEYVVVPARFLVKLPDGLDPAEAaPLLCAGITAYRALRRAG---VGPGDRVAVIG 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 172 DGNLGYITAILLRKLypEAKIYVFGKTDYKL--------SHFSFVDDIFTVNQIPDDLKIDHAFECVggkGSQVALQQIV 243
Cdd:COG1064   171 AGGLGHLAVQIAKAL--GAEVIAVDRSPEKLelarelgaDHVVNSSDEDPVEAVRELTGADVVIDTV---GAPATVNAAL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 244 EHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDLYRKYpdiveKLALlkghEINVCTMQDIVQA 323
Cdd:COG1064   246 ALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEG-----KIKP----EVETIPLEEANEA 316


                  ...
gi 2756312334 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 8.70e-11

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: 62.13  E-value: 8.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYT-GRRDENVLRKklPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEKhnviAENYLA 104
Cdd:cd05285    25 VLVRVRAVGICGSDVHYYKhGRIGDFVVKE--PMVLGHESAGTVVAVGSGVthLKVGDRVAIEPGVPCRT----CEFCKS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 105 SSY-------FRSS-GYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQrfeRKSIPLKTSFGIWGDGNLG 176
Cdd:cd05285    99 GRYnlcpdmrFAATpPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACR---RAGVRPGDTVLVFGAGPIG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 177 YITAILLrKLYPEAKIYVFGKTDYKLSHFSFVDDIFTVNQIPDDLK--------------IDHAFECVggkGSQVALQQI 242
Cdd:cd05285   176 LLTAAVA-KAFGATKVVVTDIDPSRLEFAKELGATHTVNVRTEDTPesaekiaellggkgPDVVIECT---GAESCIQTA 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 243 VEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRsgskdfeqvvdlYRK-YPDIVEklaLLKGHEINVCTM---- 317
Cdd:cd05285   252 IYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFR------------YANtYPTAIE---LLASGKVDVKPLithr 316

                         330       340
                  ....*....|....*....|....*..
gi 2756312334 318 ---QDIVQAFEMDLSTSwgKTVLKWTI 341
Cdd:cd05285   317 fplEDAVEAFETAAKGK--KGVIKVVI 341
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 26-293 1.19e-10

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: 61.95  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAADQRYYTGRRDenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEK-HNVIA--E 100
Cdd:cd08259    26 GEVLIKVKAAGVCYRDLLFWKGFFP----RGKYPLILGHEIVGTVEEVGEGVerFKPGDRVILYYYIPCGKcEYCLSgeE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 101 NYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELV-SVSYHAIqrfeRKSIPLKTSfgIW----GDGNL 175
Cdd:cd08259   102 NLCRNRAEYGEEVDGGFAEYVKVPERSLVKLPDNVSDESAALAACVvGTAVHAL----KRAGVKKGD--TVlvtgAGGGV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 176 GyITAILLRKLYpEAKIYVFGKTDYKLS--HFSFVDDIFTVNQIPDDLK----IDHAFECVGGKgsqvALQQIVEHISPE 249
Cdd:cd08259   176 G-IHAIQLAKAL-GARVIAVTRSPEKLKilKELGADYVIDGSKFSEDVKklggADVVIELVGSP----TIEESLRSLNKG 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2756312334 250 GSIALLG-VSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:cd08259   250 GRLVLIGnVTPDPAPLRPGLLILKEIRIIGSISATKADVEEALKL 294
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 28-130 3.16e-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: 56.46  E-value: 3.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYTGRRdenvLRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEK------HNvia 99
Cdd:pfam08240   3 VLVKVKAAGICGSDLHIYKGGN----PPVKLPLILGHEFAGEVVEVGPGVtgLKVGDRVVVEPLIPCGKceycreGR--- 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2756312334 100 ENYLASSYFRSSGYDGFMQDYVVMAHDRIVP 130
Cdd:pfam08240  76 YNLCPNGRFLGYDRDGGFAEYVVVPERNLVP 106
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
219-293 5.46e-10

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 56.46  E-value: 5.46e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2756312334 219 DDLKIDHAFECVGgkgSQVALQQIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:pfam00107  55 GGKGVDVVFDCVG---SPATLEQALKLLRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDL 126
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 7-293 3.21e-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: 57.54  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334   7 QLVAPRQFDVTynNVD---IYGNHVIVRPLYLSICAADQRYYTGRrdenvLRKKLPMSLVHEAVGEVVFDSKGV--FEKG 81
Cdd:cd08234     5 VYEGPGELEVE--EVPvpePGPDEVLIKVAACGICGTDLHIYEGE-----FGAAPPLVPGHEFAGVVVAVGSKVtgFKVG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  82 TKVVMVPNTPTEK-------HNVIAENYLAssyfRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQ 154
Cdd:cd08234    78 DRVAVDPNIYCGEcfycrrgRPNLCENLTA----VGVTRNGGFAEYVVVPAKQVYKIPDNLSFEEAALAEPLSCAVHGLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 155 RferksipLKTSFG----IWGDGNLGYITAILLrKLYPEAKIYVFGKTDYKL----SHFSFVddifTVNQIPDDLK---- 222
Cdd:cd08234   154 L-------LGIKPGdsvlVFGAGPIGLLLAQLL-KLNGASRVTVAEPNEEKLelakKLGATE----TVDPSREDPEaqke 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2756312334 223 -----IDHAFECVggkGSQVALQQIVEHISPEGSIALLGVS--ELPVEVNTRLVLEKGLTLIGsSRSGSKDFEQVVDL 293
Cdd:cd08234   222 dnpygFDVVIEAT---GVPKTLEQAIEYARRGGTVLVFGVYapDARVSISPFEIFQKELTIIG-SFINPYTFPRAIAL 295
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-325 6.51e-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: 56.48  E-value: 6.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYTGRrdenvlrKKLPMSLVHEAVGEVVfDSKGVFEKGTKVVMVPNtptekhnvIAENYlaSSY 107
Cdd:cd08242    27 ALVRVLLAGICNTDLEIYKGY-------YPFPGVPGHEFVGIVE-EGPEAELVGKRVVGEIN--------IACGR--CEY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 108 FRS--------------SGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTE-LVSvsyhAIQRFERKSIPLKTSFGIWGD 172
Cdd:cd08242    89 CRRglythcpnrtvlgiVDRDGAFAEYLTLPLENLHVVPDLVPDEQAVFAEpLAA----ALEILEQVPITPGDKVAVLGD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 173 GNLGYITAILLRKLypEAKIYVFGKTDYKLSHFSFVDdIFTVNQI---PDDLKIDHAFECVGgkgSQVALQQIVEHISPE 249
Cdd:cd08242   165 GKLGLLIAQVLALT--GPDVVLVGRHSEKLALARRLG-VETVLPDeaeSEGGGFDVVVEATG---SPSGLELALRLVRPR 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2756312334 250 GSIALLGVSELPVEVNTRLVLEKGLTLIGsSRSGskDFEQVVDLYRKypDIVEKLALLKGheinVCTMQDIVQAFE 325
Cdd:cd08242   239 GTVVLKSTYAGPASFDLTKAVVNEITLVG-SRCG--PFAPALRLLRK--GLVDVDPLITA----VYPLEEALEAFE 305
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 26-293 7.93e-09

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 56.20  E-value: 7.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAAD----QRYYTgrrdenvlRKKLPMSLVHEAVGEVVFDSKGV--FEKGTKVV---MVPNTPTEKHN 96
Cdd:PRK13771   26 DEVVIKVNYAGLCYRDllqlQGFYP--------RMKYPVILGHEVVGTVEEVGENVkgFKPGDRVAsllYAPDGTCEYCR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  97 VIAENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELV-SVSYHAIQRFE--RKSIPLKTSFGiwgdG 173
Cdd:PRK13771   98 SGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVtGMVYRGLRRAGvkKGETVLVTGAG----G 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 174 NLGyITAILLRKLY---------PEAKIYVFGKtdyklshfsFVDDIFTVNQIPDDLK----IDHAFECVGGKgsqvALQ 240
Cdd:PRK13771  174 GVG-IHAIQVAKALgakviavtsSESKAKIVSK---------YADYVIVGSKFSEEVKkiggADIVIETVGTP----TLE 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVNTRL--VLEKGLTLIGSSRSGSKDFEQVVDL 293
Cdd:PRK13771  240 ESLRSLNMGGKIIQIGNVDPSPTYSLRLgyIILKDIEIIGHISATKRDVEEALKL 294
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 114-339 4.32e-08

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: 53.86  E-value: 4.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 114 DGFMQDYVVMAHDRIVPLPNDIDLST---ISYTelVSVSYHAIQRFERKsipLKTSFGIWGDGNLGYITAILLRKLYPEA 190
Cdd:cd08239   116 DGGHAEYMLVPEKTLIPLPDDLSFADgalLLCG--IGTAYHALRRVGVS---GRDTVLVVGAGPVGLGALMLARALGAED 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 191 KIYV------------FGKTDYKLSHFSFVDDIFTVNQipdDLKIDHAFECvggKGSQVALQQIVEHISPEGSIALLGV- 257
Cdd:cd08239   191 VIGVdpsperlelakaLGADFVINSGQDDVQEIRELTS---GAGADVAIEC---SGNTAARRLALEAVRPWGRLVLVGEg 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 258 SELPVEVNTRLVLeKGLTLIGSSRSGSKDFEQVVDLYRKYPDIVEKLAllkGHEINVctmQDIVQAFEMDLSTSWGKTVL 337
Cdd:cd08239   265 GELTIEVSNDLIR-KQRTLIGSWYFSVPDMEECAEFLARHKLEVDRLV---THRFGL---DQAPEAYALFAQGESGKVVF 337


                  ..
gi 2756312334 338 KW 339
Cdd:cd08239   338 VF 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 2756312334 169 IWGDGNLGYITAILLRKLYPEAKIYVFGKTDYKLSHFSFVDDI---------FTVNQIPD-DLKIDHAFECVGGkgSQVA 238
Cdd:pfam16912  36 VLGNGPLGLLALAMLRVQRGFDRVYCLGRRDRPDPTIDLVEELgatyvdsreTPVDEIPAaHEPMDLVYEATGY--APHA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 239 LQQIvEHISPEGSIALLGVS-----ELPV-EVNTRLVLEKgLTLIGSSRSGSKDFEQVVDLYRKYPDiveklALLKGHEI 312
Cdd:pfam16912 114 FEAI-DALAPNGVAALLGVPtswtfEIDGgALHRELVLHN-KALVGSVNANRRHFEAAADTLAAAPE-----WFLDALVT 186

                         170       180
                  ....*....|....*....|....*.
gi 2756312334 313 NVCTMQDIVQAFEmdlstsWGKTVLK 338
Cdd:pfam16912 187 GVVPLDEFEEAFE------DGDDDIK 206
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 10-152 6.33e-07

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 50.45  E-value: 6.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  10 APRQFDVTYNNVDIYGNHVIVRPLYLSICAADQRYYT-GRRDENVLrkKLPMSLVHEAVGEVV-FDSKGVFEkGTKVVMV 87
Cdd:PRK09880   12 GKKDVAVTEQEIEWNNNGTLVQITRGGICGSDLHYYQeGKVGNFVI--KAPMVLGHEVIGKIVhSDSSGLKE-GQTVAIN 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2756312334  88 PNTPTEK------HNviaENYLAS-SYFRSSGYD-----GFMQdYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHA 152
Cdd:PRK09880   89 PSKPCGHckyclsHN---ENQCTTmRFFGSAMYFphvdgGFTR-YKVVDTAQCIPYPEKADEKVMAFAEPLAVAIHA 161
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 28-326 1.48e-05

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 46.31  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  28 VIVRPLYLSICAADQRYYTGRRDENVLRKKlPMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEKHNVIAENYL-- 103
Cdd:PLN02702   44 VRVRMKAVGICGSDVHYLKTMRCADFVVKE-PMVIGHECAGIIEEVGSEVkhLVVGDRVALEPGISCWRCNLCKEGRYnl 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 104 --ASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQrfeRKSIPLKTSFGIWGDGNLGYITaI 181
Cdd:PLN02702  123 cpEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACR---RANIGPETNVLVMGAGPIGLVT-M 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 182 LLRKLYPEAKIYVFGKTDYKLSHFSFV--DDIFTVNQIPDDL-------------KIDHAFECVG-GKGSQVALqqivEH 245
Cdd:PLN02702  199 LAARAFGAPRIVIVDVDDERLSVAKQLgaDEIVLVSTNIEDVeseveeiqkamggGIDVSFDCVGfNKTMSTAL----EA 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 246 ISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSSRsgskdfeqvvdlYRK-YPDIVEklaLLKGHEINV---------C 315
Cdd:PLN02702  275 TRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGVFR------------YRNtWPLCLE---FLRSGKIDVkplithrfgF 339

                         330
                  ....*....|.
gi 2756312334 316 TMQDIVQAFEM 326
Cdd:PLN02702  340 SQKEVEEAFET 350
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 26-176 1.55e-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: 43.00  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAADqrYYTGRRDENVLRKKlpMSLVHEAVGEVVFDSKGV--FEKGTKVVMVPNTPTEKHNVIAENYL 103
Cdd:cd08285    25 NDAIVRPTAVAPCTSD--VHTVWGGAPGERHG--MILGHEAVGVVEEVGSEVkdFKPGDRVIVPAITPDWRSVAAQRGYP 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 104 ASSYFRSSGY------DGFMQDYVVM--AHDRIVPLPNDIDLSTISY-TELVSVSYHAiqrFERKSIPLKTSFGIWGDGN 174
Cdd:cd08285   101 SQSGGMLGGWkfsnfkDGVFAEYFHVndADANLAPLPDGLTDEQAVMlPDMMSTGFHG---AELANIKLGDTVAVFGIGP 177


                  ..
gi 2756312334 175 LG 176
Cdd:cd08285   178 VG 179
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 234-340 2.49e-04

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 42.50  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 234 GSQVALQQIVEHISPEGSIALLGVSELPVEVNTRLVLEKGLTLIGSsrSGSKDFE---QVVDLYRKYPDivekLALLKGH 310
Cdd:PRK05396  241 GAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWNKVIFKGLTIKGI--YGREMFEtwyKMSALLQSGLD----LSPIITH 314

                          90       100       110
                  ....*....|....*....|....*....|
gi 2756312334 311 EInvcTMQDIVQAFEMDLSTSWGKTVLKWT 340
Cdd:PRK05396  315 RF---PIDDFQKGFEAMRSGQSGKVILDWD 341
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 2756312334 214 VNQIPDDLKIDHAFECVGGKgsqvALQQIVEHISPEGSIALLGV-SELPVEVNTRLVLEKGLTLIGSS-RSGSK-----D 286
Cdd:COG0604   200 VRALTGGRGVDVVLDTVGGD----TLARSLRALAPGGRLVSIGAaSGAPPPLDLAPLLLKGLTLTGFTlFARDPaerraA 275

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2756312334 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 2756312334 224 DHAFECVggkGSQVALQQIVEHISPEGSIALLGVS----ELPVEVNTRLVLEKGL--TLIGSSRsGSKDFEQVVDLYR 295
Cdd:COG1062   245 DYAFETT---GNPAVIRQALEALRKGGTVVVVGLAppgaEISLDPFQLLLTGRTIrgSYFGGAV-PRRDIPRLVDLYR 318
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 25-202 1.25e-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: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  25 GNHVIVRPLYLSICAAD----QRYY---TGRRDENVLRK-KLPMSLVHEAVGEVVF---DSKGVfEKGTKVVMVP----- 88
Cdd:cd08240    25 GTEVLVKVTACGVCHSDlhiwDGGYdlgGGKTMSLDDRGvKLPLVLGHEIVGEVVAvgpDAADV-KVGDKVLVYPwigcg 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  89 --NTPTEKHnviaENYLASSYFRSSGYDGFMQDYVVMAHDRIVPLPNDIDLSTISyTELVS--VSYHAIqrfeRKSIPL- 163
Cdd:cd08240   104 ecPVCLAGD----ENLCAKGRALGIFQDGGYAEYVIVPHSRYLVDPGGLDPALAA-TLACSglTAYSAV----KKLMPLv 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2756312334 164 -KTSFGIWGDGNLGYITAILLRKLYPeAKIYVFGKTDYKL 202
Cdd:cd08240   175 aDEPVVIIGAGGLGLMALALLKALGP-ANIIVVDIDEAKL 213
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 26-337 2.28e-03

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: 39.52  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334  26 NHVIVRPLYLSICAADQRYYtgRRDE-NVLRKKLPMSLVHEAVGEVVfdskgvfEKGTKVVMVpntpTEKHNVIAENYLA 104
Cdd:cd05281    26 GEVLIKVLAASICGTDVHIY--EWDEwAQSRIKPPLIFGHEFAGEVV-------EVGEGVTRV----KVGDYVSAETHIV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 105 --SSYFRSSG--------------YDGFMQDYVVMAHDRIVPLPNDIDLSTISYTELVSVSYHAIQRFErksIPLKTSFg 168
Cdd:cd05281    93 cgKCYQCRTGnyhvcqntkilgvdTDGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVLAGD---VSGKSVL- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 169 IWGDGNLGyITAILLRKLYPEAKIYVFGKTDY--KLSHFSFVDDIFTVNQIpDDLKIDHAFECVGG------KGSQVALQ 240
Cdd:cd05281   169 ITGCGPIG-LMAIAVAKAAGASLVIASDPNPYrlELAKKMGADVVINPREE-DVVEVKSVTDGTGVdvvlemSGNPKAIE 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2756312334 241 QIVEHISPEGSIALLGVSELPVEVN-TRLVLEKGLTLIGSsrSGSKDFE---QVVdlyrkypdiveklALLKGHEIN--- 313
Cdd:cd05281   247 QGLKALTPGGRVSILGLPPGPVDIDlNNLVIFKGLTVQGI--TGRKMFEtwyQVS-------------ALLKSGKVDlsp 311

                         330       340
                  ....*....|....*....|....*...
gi 2756312334 314 VCT----MQDIVQAFEMDLSTSWGKTVL 337
Cdd:cd05281   312 VIThklpLEDFEEAFELMRSGKCGKVVL 339
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 2756312334  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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