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Conserved domains on  [gi|926233843|emb|CUC41047|]
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ribitol-5-phosphate 2-dehydrogenase [Staphylococcus aureus]

Protein Classification

ribitol-5-phosphate dehydrogenase( domain architecture ID 10169517)

ribitol-5-phosphate 2-dehydrogenase (NADP(+)) catalyzes the NADPH dependent reduction of D-ribulose 5-phosphate to D-ribitol 5-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 1-339 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: 530.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   1 MINQVYQLVAPRQFEVTYNNVDIYSDYVIVRPLYMSICAADQRYYTGSRDENVLSQKLPMSLIHEGVGEVVFDSKGVFNK 80
Cdd:cd08237    1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  81 GTKVVMVPNTPTEKDDVIAENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEKKS 160
Cdd:cd08237   81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 161 ISNKNTFGIWGDGNLGYITAILLRKLYPESKIYVFGKTDYKLSHFSFVDDVFFINKIPEGLTFDHAFECVGGRGSQSAIN 240
Cdd:cd08237  161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 241 QMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLYIQYPDIVDKLALLKGQEFEIATINDL 320
Cdd:cd08237  241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                        330
                 ....*....|....*....
gi 926233843 321 TEAFEADLSTSWGKTVLKW 339
Cdd:cd08237  321 HRAFESDLTNSWGKTVMEW 339
 
Name Accession Description Interval E-value
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 1-339 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: 530.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   1 MINQVYQLVAPRQFEVTYNNVDIYSDYVIVRPLYMSICAADQRYYTGSRDENVLSQKLPMSLIHEGVGEVVFDSKGVFNK 80
Cdd:cd08237    1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  81 GTKVVMVPNTPTEKDDVIAENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEKKS 160
Cdd:cd08237   81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 161 ISNKNTFGIWGDGNLGYITAILLRKLYPESKIYVFGKTDYKLSHFSFVDDVFFINKIPEGLTFDHAFECVGGRGSQSAIN 240
Cdd:cd08237  161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 241 QMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLYIQYPDIVDKLALLKGQEFEIATINDL 320
Cdd:cd08237  241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                        330
                 ....*....|....*....
gi 926233843 321 TEAFEADLSTSWGKTVLKW 339
Cdd:cd08237  321 HRAFESDLTNSWGKTVMEW 339
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 8-339 2.23e-39

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: 141.81  E-value: 2.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   8 LVAPRQFEVTynNVD---IYSDYVIVRPLYMSICAADQRYYTGSRDEnvlsQKLPMSLIHEGVGEVVFDSKGV--FNKGT 82
Cdd:COG1063    6 LHGPGDLRLE--EVPdpePGPGEVLVRVTAVGICGSDLHIYRGGYPF----VRPPLVLGHEFVGEVVEVGEGVtgLKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  83 KVVMVPNTP-------TEKDDVIAENYlksSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRR 155
Cdd:COG1063   80 RVVVEPNIPcgecrycRRGRYNLCENL---QFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVER 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 156 FEKKsisnkntFG----IWGDGNLGYITAILLRkLYPESKIYVFGKTDYKLS-----------HFSFVDDVFFINKIPEG 220
Cdd:COG1063  157 AGVK-------PGdtvlVIGAGPIGLLAALAAR-LAGAARVIVVDRNPERLElarelgadavvNPREEDLVEAVRELTGG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 221 LTFDHAFECVGgrgSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLyIQYPDI 300
Cdd:COG1063  229 RGADVVIEAVG---APAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALEL-LASGRI 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 926233843 301 -VDKLAllkGQEFeiaTINDLTEAFEA--DLSTSWGKTVLKW 339
Cdd:COG1063  305 dLEPLI---THRF---PLDDAPEAFEAaaDRADGAIKVVLDP 340
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
214-293 6.76e-10

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 56.46  E-value: 6.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  214 INKIPEGLTFDHAFECVGgrgSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDL 293
Cdd:pfam00107  50 IKELTGGKGVDVVFDCVG---SPATLEQALKLLRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDL 126
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 25-293 1.12e-07

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 52.73  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  25 SDYVIVRPLYMSICAAD----QRYYTGSrdenvlsqKLPMSLIHEGVGEVVFDSKGV--FNKGTKVV---MVPNTPTEKD 95
Cdd:PRK13771  25 KDEVVIKVNYAGLCYRDllqlQGFYPRM--------KYPVILGHEVVGTVEEVGENVkgFKPGDRVAsllYAPDGTCEYC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  96 DVIAENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSL-HAIRRFEkksISNKNTFGIWGDGN 174
Cdd:PRK13771  97 RSGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVyRGLRRAG---VKKGETVLVTGAGG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 175 LGYITAILLRKLY---------PESKIYVFGK-TDYKLSHFSFVDDVffiNKIPEGltfDHAFECVGGrgsqSAINQMID 244
Cdd:PRK13771 174 GVGIHAIQVAKALgakviavtsSESKAKIVSKyADYVIVGSKFSEEV---KKIGGA---DIVIETVGT----PTLEESLR 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 926233843 245 YISPEGSIALLGVSEFPVEVNTRL--VLEKGLTLIGSSRSGSKDFQDVVDL 293
Cdd:PRK13771 244 SLNMGGKIIQIGNVDPSPTYSLRLgyIILKDIEIIGHISATKRDVEEALKL 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 ...
 1-339 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: 530.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   1 MINQVYQLVAPRQFEVTYNNVDIYSDYVIVRPLYMSICAADQRYYTGSRDENVLSQKLPMSLIHEGVGEVVFDSKGVFNK 80
Cdd:cd08237    1 MINQVYRLVRPKFFEVTYEEENLREDWVIVRPTYLSICHADQRYYQGNRSPEALKKKLPMALIHEGIGVVVSDPTGTYKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  81 GTKVVMVPNTPTEKDDVIAENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEKKS 160
Cdd:cd08237   81 GTKVVMVPNTPVEKDEIIPENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKLPDNVDPEVAAFTELVSVGVHAISRFEQIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 161 ISNKNTFGIWGDGNLGYITAILLRKLYPESKIYVFGKTDYKLSHFSFVDDVFFINKIPEGLTFDHAFECVGGRGSQSAIN 240
Cdd:cd08237  161 HKDRNVIGVWGDGNLGYITALLLKQIYPESKLVVFGKHQEKLDLFSFADETYLIDDIPEDLAVDHAFECVGGRGSQSAIN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 241 QMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLYIQYPDIVDKLALLKGQEFEIATINDL 320
Cdd:cd08237  241 QIIDYIRPQGTIGLMGVSEYPVPINTRMVLEKGLTLVGSSRSTREDFERAVELLSRNPEVAEYLRKLVGGVFPVRSINDI 320

                        330
                 ....*....|....*....
gi 926233843 321 TEAFEADLSTSWGKTVLKW 339
Cdd:cd08237  321 HRAFESDLTNSWGKTVMEW 339
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 8-339 2.23e-39

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: 141.81  E-value: 2.23e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   8 LVAPRQFEVTynNVD---IYSDYVIVRPLYMSICAADQRYYTGSRDEnvlsQKLPMSLIHEGVGEVVFDSKGV--FNKGT 82
Cdd:COG1063    6 LHGPGDLRLE--EVPdpePGPGEVLVRVTAVGICGSDLHIYRGGYPF----VRPPLVLGHEFVGEVVEVGEGVtgLKVGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  83 KVVMVPNTP-------TEKDDVIAENYlksSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRR 155
Cdd:COG1063   80 RVVVEPNIPcgecrycRRGRYNLCENL---QFLGIAGRDGGFAEYVRVPAANLVKVPDGLSDEAAALVEPLAVALHAVER 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 156 FEKKsisnkntFG----IWGDGNLGYITAILLRkLYPESKIYVFGKTDYKLS-----------HFSFVDDVFFINKIPEG 220
Cdd:COG1063  157 AGVK-------PGdtvlVIGAGPIGLLAALAAR-LAGAARVIVVDRNPERLElarelgadavvNPREEDLVEAVRELTGG 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 221 LTFDHAFECVGgrgSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLyIQYPDI 300
Cdd:COG1063  229 RGADVVIEAVG---APAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALEL-LASGRI 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 926233843 301 -VDKLAllkGQEFeiaTINDLTEAFEA--DLSTSWGKTVLKW 339
Cdd:COG1063  305 dLEPLI---THRF---PLDDAPEAFEAaaDRADGAIKVVLDP 340
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 28-294 1.30e-28

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


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 111.64  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQRYYTGSRDENVlsqKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTEKDDVIAEnYLKS 105
Cdd:cd05188    2 VLVRVEAAGLCGTDLHIRRGGYPPPP---KLPLILGHEGAGVVVEVGPGVtgVKVGDRVVVLPNLGCGTCELCRE-LCPG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 106 SYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSI-ISYTELVTVSLHAIRRFEKksISNKNTFGIWGDGNLGYITAILLR 184
Cdd:cd05188   78 GGILGEGLDGGFAEYVVVPADNLVPLPDGLSLEEaALLPEPLATAYHALRRAGV--LKPGDTVLVLGAGGVGLLAAQLAK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 185 KLYpeSKIYVFGKTDYKLS------HFSFVD----DVFFINKIPEGLTFDHAFECVGGrgsQSAINQMIDYISPEGSIAL 254
Cdd:cd05188  156 AAG--ARVIVTDRSDEKLElakelgADHVIDykeeDLEEELRLTGGGGADVVIDAVGG---PETLAQALRLLRPGGRIVV 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 926233843 255 LGV-SEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLY 294
Cdd:cd05188  231 VGGtSGGPPLDDLRRLLFKELTIIGSTGGTREDFEEALDLL 271
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 28-294 1.36e-21

(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: 93.76  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQRYYTG-------SRDENVLSQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTEKDD-V 97
Cdd:cd08233   27 VKIKVAWCGICGSDLHEYLDgpifiptEGHPHLTGETAPVTLGHEFSGVVVEVGSGVtgFKVGDRVVVEPTIKCGTCGaC 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  98 IAENYLKSSYFRS---SGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRR--FEKKSisnknTFGIWGD 172
Cdd:cd08233  107 KRGLYNLCDSLGFiglGGGGGGFAEYVVVPAYHVHKLPDNVPLEEAALVEPLAVAWHAVRRsgFKPGD-----TALVLGA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 173 GNLGyITAILLRKLYPESKIYVF--GKTDYKLSHFSFVDDVF---------FINKIPEGLTFDHAFECVggrGSQSAINQ 241
Cdd:cd08233  182 GPIG-LLTILALKAAGASKIIVSepSEARRELAEELGATIVLdptevdvvaEVRKLTGGGGVDVSFDCA---GVQATLDT 257

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 926233843 242 MIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLY 294
Cdd:cd08233  258 AIDALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGSICYTREDFEEVIDLL 310
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 26-337 2.09e-20

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: 90.36  E-value: 2.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  26 DYVIVRPLYMSICAAD-QRYYTGSRdenvlsQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTEKDDV----- 97
Cdd:cd08236   25 GEVLVKVKACGICGSDiPRYLGTGA------YHPPLVLGHEFSGTVEEVGSGVddLAVGDRVAVNPLLPCGKCEYckkge 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  98 --IAENYlksSYFRSSgHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEkksISNKNTFGIWGDGNL 175
Cdd:cd08236   99 ysLCSNY---DYIGSR-RDGAFAEYVSVPARNLIKIPDHVDYEEAAMIEPAAVALHAVRLAG---ITLGDTVVVIGAGTI 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 176 GyITAILLRKLYPESKIYVFGKTDYKLS----------HFSFVDDVFFINKIPEGLTFDHAFECVggrGSQSAINQMIDY 245
Cdd:cd08236  172 G-LLAIQWLKILGAKRVIAVDIDDEKLAvarelgaddtINPKEEDVEKVRELTEGRGADLVIEAA---GSPATIEQALAL 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 246 ISPEGSIALLGVSEFPV---EVNTRLVLEKGLTLIGSSRSGSKDFQDVvdlyiQYPDIVDKLA--LLKGQEF--EIATIN 318
Cdd:cd08236  248 ARPGGKVVLVGIPYGDVtlsEEAFEKILRKELTIQGSWNSYSAPFPGD-----EWRTALDLLAsgKIKVEPLitHRLPLE 322

                        330       340
                 ....*....|....*....|.
gi 926233843 319 DLTEAFE--ADLSTSWGKTVL 337
Cdd:cd08236  323 DGPAAFErlADREEFSGKVLL 343
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 26-294 1.52e-18

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: 84.99  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  26 DYVIVRPLYMSICAADQRYYTGsrdENVLSQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMV-PNTPTEKDDVIA--E 100
Cdd:cd08254   27 GEVLVKVKAAGVCHSDLHILDG---GVPTLTKLPLTLGHEIAGTVVEVGAGVtnFKVGDRVAVPaVIPCGACALCRRgrG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 101 NYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISY-TELVTVSLHAIRRfeKKSISNKNTFGIWGDGNLGyIT 179
Cdd:cd08254  104 NLCLNQGMPGLGIDGGFAEYIVVPARALVPVPDGVPFAQAAVaTDAVLTPYHAVVR--AGEVKPGETVLVIGLGGLG-LN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 180 AILLRKLYpESKIYVFGKTDYKL--------SHFSFVDDVFFINKIPEGL--TFDHAFECVggrGSQSAINQMIDYISPE 249
Cdd:cd08254  181 AVQIAKAM-GAAVIAVDIKEEKLelakelgaDEVLNSLDDSPKDKKAAGLggGFDVIFDFV---GTQPTFEDAQKAVKPG 256

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 926233843 250 GSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLY 294
Cdd:cd08254  257 GRIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLI 301
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 56-326 1.28e-12

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 67.83  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  56 QKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVmVPNtptekddVIA-----------ENYLKSSYFRSSGHDGFMQDFVL 122
Cdd:COG1064   52 PKLPLVPGHEIVGRVVAVGPGVtgFKVGDRVG-VGW-------VDScgtceycrsgrENLCENGRFTGYTTDGGYAEYVV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 123 LNHDRAVPLPDDIDLS---------IISYtelvtvslHAIRRFEkksISNKNTFGIWGDGNLGYITAILLRKLypESKIY 193
Cdd:COG1064  124 VPARFLVKLPDGLDPAeaapllcagITAY--------RALRRAG---VGPGDRVAVIGAGGLGHLAVQIAKAL--GAEVI 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 194 VFGKTDYKL--------SHFSFVDDVFFINKIPEGLTFDHAFECVggrGSQSAINQMIDYISPEGSIALLGVSEFPVEVN 265
Cdd:COG1064  191 AVDRSPEKLelarelgaDHVVNSSDEDPVEAVRELTGADVVIDTV---GAPATVNAALALLRRGGRLVLVGLPGGPIPLP 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 926233843 266 TRLVLEKGLTLIGSSRSGSKDFQDVVDLYIQ---YPDIvdklallkgQEFEIATINdltEAFEA 326
Cdd:COG1064  268 PFDLILKERSIRGSLIGTRADLQEMLDLAAEgkiKPEV---------ETIPLEEAN---EALER 319
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 8-326 1.75e-12

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


Pssm-ID: 176230 [Multi-domain]  Cd Length: 312  Bit Score: 67.00  E-value: 1.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   8 LVAPRQFEVTYNNV-DIYSDYVIVRPLYMSICAADQRYYTGSRDENVlSQKLPMSLIHEGVGEVVFDSKGV--FNKGTKV 84
Cdd:cd08269    1 LTGPGRFEVEEHPRpTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFV-YPAEPGGPGHEGWGRVVALGPGVrgLAVGDRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  85 VMVPntptekddviaenylkssyfrssgHDGFMQdFVLLNHDRAVPLPDDIDLSIISYTELVTVsLHAIRRFEkksISNK 164
Cdd:cd08269   80 AGLS------------------------GGAFAE-YDLADADHAVPLPSLLDGQAFPGEPLGCA-LNVFRRGW---IRAG 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 165 NTFGIWGDGNLGYITAILLrKLYPESKIYVFGKTDYKL---SHF----SFVDD----VFFINKIPEGLTFDHAFECVggr 233
Cdd:cd08269  131 KTVAVIGAGFIGLLFLQLA-AAAGARRVIAIDRRPARLalaRELgateVVTDDseaiVERVRELTGGAGADVVIEAV--- 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 234 GSQSAINQMIDYISPEGSIALLGVSEF-PVEVNTRLVLEKGLTLIGS----SRSGSKDFQDVVDLYIQYPDIVDKLALLk 308
Cdd:cd08269  207 GHQWPLDLAGELVAERGRLVIFGYHQDgPRPVPFQTWNWKGIDLINAverdPRIGLEGMREAVKLIADGRLDLGSLLTH- 285

                        330
                 ....*....|....*...
gi 926233843 309 gqEFeiaTINDLTEAFEA 326
Cdd:cd08269  286 --EF---PLEELGDAFEA 298
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 28-293 2.17e-12

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: 66.88  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQRYYT-GSRDENVLSQklPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTEKDDVIAE---N 101
Cdd:cd08232   24 VRVRVAAGGICGSDLHYYQhGGFGTVRLRE--PMVLGHEVSGVVEAVGPGVtgLAPGQRVAVNPSRPCGTCDYCRAgrpN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 102 YLKSSYFRSSG----H-DGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEkkSISNKNTFgIWGDGNLG 176
Cdd:cd08232  102 LCLNMRFLGSAmrfpHvQGGFREYLVVDASQCVPLPDGLSLRRAALAEPLAVALHAVNRAG--DLAGKRVL-VTGAGPIG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 177 YITAILLRKLyPESKIYVFGKTDYKLSHFSFV--DDVffINKIPEGL--------TFDHAFECvggRGSQSAINQMIDYI 246
Cdd:cd08232  179 ALVVAAARRA-GAAEIVATDLADAPLAVARAMgaDET--VNLARDPLaayaadkgDFDVVFEA---SGAPAALASALRVV 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 926233843 247 SPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSkDFQDVVDL 293
Cdd:cd08232  253 RPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSFRFDD-EFAEAVRL 298
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 28-257 2.73e-12

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: 66.91  E-value: 2.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQRYYTGSrdenVLSQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTE-----KDDVIA- 99
Cdd:cd05278   28 AIVRVTATSICGSDLHIYRGG----VPGAKHGMILGHEFVGEVVEVGSDVkrLKPGDRVSVPCITFCGrcrfcRRGYHAh 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 100 -ENYLKSSYFrSSGHDGFMQDFVLLNH-DR-AVPLPDDI---DLSIISytELVTVSLHAIRRFEkksISNKNTFGIWGDG 173
Cdd:cd05278  104 cENGLWGWKL-GNRIDGGQAEYVRVPYaDMnLAKIPDGLpdeDALMLS--DILPTGFHGAELAG---IKPGSTVAVIGAG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 174 NLGyITAILLRKLYPESKIYVFGKTDYKLSHFSFVDDVFFIN-----------KIPEGLTFDHAFECVGGrgsQSAINQM 242
Cdd:cd05278  178 PVG-LCAVAGARLLGAARIIAVDSNPERLDLAKEAGATDIINpkngdiveqilELTGGRGVDCVIEAVGF---EETFEQA 253

                        250
                 ....*....|....*
gi 926233843 243 IDYISPEGSIALLGV 257
Cdd:cd05278  254 VKVVRPGGTIANVGV 268
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 57-293 6.33e-11

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group contains proteins that share the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenase family. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176220 [Multi-domain]  Cd Length: 332  Bit Score: 62.72  E-value: 6.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  57 KLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTEK-DDVIA--ENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPL 131
Cdd:cd08259   53 KYPLILGHEIVGTVEEVGEGVerFKPGDRVILYYYIPCGKcEYCLSgeENLCRNRAEYGEEVDGGFAEYVKVPERSLVKL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 132 PDDIDLSIISYTELVT-VSLHAIRRF-EKKSISNKNTFGIWGDGnlgyITAILLRKLYPESKIYVfGKTDYKLS--HFSF 207
Cdd:cd08259  133 PDNVSDESAALAACVVgTAVHALKRAgVKKGDTVLVTGAGGGVG----IHAIQLAKALGARVIAV-TRSPEKLKilKELG 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 208 VDDVFFINKIPE----GLTFDHAFECVGGRgsqsAINQMIDYISPEGSIALLG-VSEFPVEVNTRLVLEKGLTLIGSSRS 282
Cdd:cd08259  208 ADYVIDGSKFSEdvkkLGGADVVIELVGSP----TIEESLRSLNKGGRLVLIGnVTPDPAPLRPGLLILKEIRIIGSISA 283

                        250
                 ....*....|.
gi 926233843 283 GSKDFQDVVDL 293
Cdd:cd08259  284 TKADVEEALKL 294
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 23-293 6.34e-11

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: 62.33  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  23 IYSDYVIVRPLYMSICAADQRYYTGSrDENVlsqKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPT--EKDDVI 98
Cdd:cd08258   24 PGPGEVLIKVAAAGICGSDLHIYKGD-YDPV---ETPVVLGHEFSGTIVEVGPDVegWKVGDRVVSETTFSTcgRCPYCR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  99 AENYLKSSYFRSSGH--DGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIrrFEKKSISNKNTFGIWGDGNLG 176
Cdd:cd08258  100 RGDYNLCPHRKGIGTqaDGGFAEYVLVPEESLHELPENLSLEAAALTEPLAVAVHAV--AERSGIRPGDTVVVFGPGPIG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 177 YITAILLRKLYPESKIYVFGKTDYKL----------SHFSFVDDVFFINKIPEGLTFDHAFECvggRGSQSAINQMIDYI 246
Cdd:cd08258  178 LLAAQVAKLQGATVVVVGTEKDEVRLdvakelgadaVNGGEEDLAELVNEITDGDGADVVIEC---SGAVPALEQALELL 254

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 926233843 247 SPEGSIALLGV-SEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDL 293
Cdd:cd08258  255 RKGGRIVQVGIfGPLAASIDVERIIQKELSVIGSRSSTPASWETALRL 302
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 28-339 8.65e-11

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: 62.24  E-value: 8.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQR-------YYTGSRDENVLSqklpmsliHEGVGEVVFDSKGV-FNKGTKVVMV---PNTPTEKDD 96
Cdd:cd08230   28 VLVRTLEVGVCGTDREivageygTAPPGEDFLVLG--------HEALGVVEEVGDGSgLSPGDLVVPTvrrPPGKCLNCR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  97 VIAENYLKSSYFRS---SGHDGFMQDFVLLNHDRAVPLPDDID--------LSII--SYTELVTVSLHAIRRFEKKSIsn 163
Cdd:cd08230  100 IGRPDFCETGEYTErgiKGLHGFMREYFVDDPEYLVKVPPSLAdvgvllepLSVVekAIEQAEAVQKRLPTWNPRRAL-- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 164 kntfgIWGDGNLGYITAILLRKLYPEskIYVFGKTDYKLSHFSFVDD--VFFINKIPEGLT-------FDHAFECVggrG 234
Cdd:cd08230  178 -----VLGAGPIGLLAALLLRLRGFE--VYVLNRRDPPDPKADIVEElgATYVNSSKTPVAevklvgeFDLIIEAT---G 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 235 SQSAINQMIDYISPEGSIALLGVS----EFPV---EVNTRLVLeKGLTLIGSSRSGSKDFQDVVD----LYIQYPDIVDK 303
Cdd:cd08230  248 VPPLAFEALPALAPNGVVILFGVPgggrEFEVdggELNRDLVL-GNKALVGSVNANKRHFEQAVEdlaqWKYRWPGVLER 326

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 926233843 304 LALlkgqefEIATINDLTEAFEADLSTSWgKTVLKW 339
Cdd:cd08230  327 LIT------RRVPLEEFAEALTEKPDGEI-KVVIEW 355
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 28-294 9.84e-11

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: 62.19  E-value: 9.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQRYYTGsRDENVLSQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPntptekddVIA------ 99
Cdd:cd05284   28 VLVRVGGAGVCHSDLHVIDG-VWGGILPYKLPFTLGHENAGWVEEVGSGVdgLKEGDPVVVHP--------PWGcgtcry 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 100 -----ENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIIS-YTELVTVSLHAIRRFEKKsISNKNTFGIWGDG 173
Cdd:cd05284   99 crrgeENYCENARFPGIGTDGGFAEYLLVPSRRLVKLPRGLDPVEAApLADAGLTAYHAVKKALPY-LDPGSTVVVIGVG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 174 NLGYITAILLRKLYPeSKIYVFGKTDYKLSH---------FSFVDDVF-FINKIPEGLTFDHAFECVggrGSQSAINQMI 243
Cdd:cd05284  178 GLGHIAVQILRALTP-ATVIAVDRSEEALKLaerlgadhvLNASDDVVeEVRELTGGRGADAVIDFV---GSDETLALAA 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 926233843 244 DYISPEGSIALLGVSEfPVEVNTRLVLEKGLTLIGS---SRSgskDFQDVVDLY 294
Cdd:cd05284  254 KLLAKGGRYVIVGYGG-HGRLPTSDLVPTEISVIGSlwgTRA---ELVEVVALA 303
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 7-279 1.01e-10

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: 62.16  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   7 QLVAPRQFEVTynNVD---IYSDYVIVRPLYMSICAADQRYYTGsrdENVLsqKLPMSLIHEGVGEVVFDSKGV--FNKG 81
Cdd:cd08234    5 VYEGPGELEVE--EVPvpePGPDEVLIKVAACGICGTDLHIYEG---EFGA--APPLVPGHEFAGVVVAVGSKVtgFKVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  82 TKVVMVPNTPTEKDDviaenYLKSSY------FRSSGH--DGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAI 153
Cdd:cd08234   78 DRVAVDPNIYCGECF-----YCRRGRpnlcenLTAVGVtrNGGFAEYVVVPAKQVYKIPDNLSFEEAALAEPLSCAVHGL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 154 RRFEKKSISNKNtfgIWGDGNLGYITAILLrKLYPESKIYVFGKTDYKL----SHFSFV-------DDVFFINKIPEGlt 222
Cdd:cd08234  153 DLLGIKPGDSVL---VFGAGPIGLLLAQLL-KLNGASRVTVAEPNEEKLelakKLGATEtvdpsreDPEAQKEDNPYG-- 226

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 926233843 223 FDHAFECVggrGSQSAINQMIDYISPEGSIALLGVS--EFPVEVNTRLVLEKGLTLIGS 279
Cdd:cd08234  227 FDVVIEAT---GVPKTLEQAIEYARRGGTVLVFGVYapDARVSISPFEIFQKELTIIGS 282
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 113-339 3.40e-10

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: 60.41  E-value: 3.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 113 HDGFMQDFVLLNHDRAVPLPDdiDLSIISYTEL---VTVSLHAIRRFEkksISNKNTFGIWGDGNLGYITAILLRKLYPE 189
Cdd:cd08239  115 RDGGHAEYMLVPEKTLIPLPD--DLSFADGALLlcgIGTAYHALRRVG---VSGRDTVLVVGAGPVGLGALMLARALGAE 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 190 SKIYV------------FGKTDYKLSHfsfVDDVFFINKIPEGLTFDHAFECVGGRgsqSAINQMIDYISPEGSIALLGV 257
Cdd:cd08239  190 DVIGVdpsperlelakaLGADFVINSG---QDDVQEIRELTSGAGADVAIECSGNT---AARRLALEAVRPWGRLVLVGE 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 258 -SEFPVEVNTRLVLeKGLTLIGSSRSGSKDFQDVVDLYIQYPDIVDKLAllkGQEFEIAtinDLTEAFEADLSTSWGKTV 336
Cdd:cd08239  264 gGELTIEVSNDLIR-KQRTLIGSWYFSVPDMEECAEFLARHKLEVDRLV---THRFGLD---QAPEAYALFAQGESGKVV 336


                 ...
gi 926233843 337 LKW 339
Cdd:cd08239  337 FVF 339
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 28-294 5.42e-10

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: 59.90  E-value: 5.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQRYYTGSrdeNVLsQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPntptekddviaenylks 105
Cdd:cd08261   27 VLVRVKRVGICGSDLHIYHGR---NPF-ASYPRILGHELSGEVVEVGEGVagLKVGDRVVVDP----------------- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 106 syFRSSGH----------------------DGFMQDFVLLNHDrAVPLPDDIDLSIISYTELVTVSLHAIRRfekKSISN 163
Cdd:cd08261   86 --YISCGEcyacrkgrpnccenlqvlgvhrDGGFAEYIVVPAD-ALLVPEGLSLDQAALVEPLAIGAHAVRR---AGVTA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 164 KNTFGIWGDGNLGYITAILLRKLYpeSKIYVFGKTDYKLSHFS--FVDDVFF---------INKIPEGLTFDHAFECVGg 232
Cdd:cd08261  160 GDTVLVVGAGPIGLGVIQVAKARG--ARVIVVDIDDERLEFARelGADDTINvgdedvaarLRELTDGEGADVVIDATG- 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 926233843 233 rgSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDLY 294
Cdd:cd08261  237 --NPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLL 296
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
214-293 6.76e-10

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 56.46  E-value: 6.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  214 INKIPEGLTFDHAFECVGgrgSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRSGSKDFQDVVDL 293
Cdd:pfam00107  50 IKELTGGKGVDVVFDCVG---SPATLEQALKLLRPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDL 126
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 26-293 8.39e-10

Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 59.43  E-value: 8.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  26 DYVIVRPLYMSICAADQRYYT-GSRDENVLSQklPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTEKDdviaENY 102
Cdd:cd05285   23 GEVLVRVRAVGICGSDVHYYKhGRIGDFVVKE--PMVLGHESAGTVVAVGSGVthLKVGDRVAIEPGVPCRTC----EFC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 103 LKSSY-------FRSS-GHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRfekKSIsnknTFG----IW 170
Cdd:cd05285   97 KSGRYnlcpdmrFAATpPVDGTLCRYVNHPADFCHKLPDNVSLEEGALVEPLSVGVHACRR---AGV----RPGdtvlVF 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 171 GDGNLGYITAILLrKLYPESKIYV-------------FGKTD-YKLSHFSFVDDVFFINKIPEGLTFDHAFECVggrGSQ 236
Cdd:cd05285  170 GAGPIGLLTAAVA-KAFGATKVVVtdidpsrlefakeLGATHtVNVRTEDTPESAEKIAELLGGKGPDVVIECT---GAE 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 926233843 237 SAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSSRsGSKDFQDVVDL 293
Cdd:cd05285  246 SCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVFR-YANTYPTAIEL 301
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 27-283 4.28e-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: 56.87  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  27 YVIVRPLYMSICAADQRYYTGSRdenvlsqKLPMSLIHEGVGEVVfDSKGVFNKGTKVVMVPNTPTEKDDVIAENYLKSS 106
Cdd:cd08242   26 EALVRVLLAGICNTDLEIYKGYY-------PFPGVPGHEFVGIVE-EGPEAELVGKRVVGEINIACGRCEYCRRGLYTHC 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 107 YFRS----SGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTE-LVTvslhAIRRFEKKSISNKNTFGIWGDGNLGYITAI 181
Cdd:cd08242   98 PNRTvlgiVDRDGAFAEYLTLPLENLHVVPDLVPDEQAVFAEpLAA----ALEILEQVPITPGDKVAVLGDGKLGLLIAQ 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 182 LLRKLYPesKIYVFGKTDYKLSHFSFVDDVFFIN--KIPEGLTFDHAFECVggrGSQSAINQMIDYISPEGSIALLGVSE 259
Cdd:cd08242  174 VLALTGP--DVVLVGRHSEKLALARRLGVETVLPdeAESEGGGFDVVVEAT---GSPSGLELALRLVRPRGTVVLKSTYA 248

                        250       260
                 ....*....|....*....|....
gi 926233843 260 FPVEVNTRLVLEKGLTLIGsSRSG 283
Cdd:cd08242  249 GPASFDLTKAVVNEITLVG-SRCG 271
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 26-130 3.67e-08

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: 50.68  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843   26 DYVIVRPLYMSICAADQRYYTGsrdeNVLSQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTP-------TEKDD 96
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKG----GNPPVKLPLILGHEFAGEVVEVGPGVtgLKVGDRVVVEPLIPcgkceycREGRY 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 926233843   97 VIAENYlkssYFRSSGHDGFMQDFVLLNHDRAVP 130
Cdd:pfam08240  77 NLCPNG----RFLGYDRDGGFAEYVVVPERNLVP 106
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 25-293 1.12e-07

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 52.73  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  25 SDYVIVRPLYMSICAAD----QRYYTGSrdenvlsqKLPMSLIHEGVGEVVFDSKGV--FNKGTKVV---MVPNTPTEKD 95
Cdd:PRK13771  25 KDEVVIKVNYAGLCYRDllqlQGFYPRM--------KYPVILGHEVVGTVEEVGENVkgFKPGDRVAsllYAPDGTCEYC 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  96 DVIAENYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSL-HAIRRFEkksISNKNTFGIWGDGN 174
Cdd:PRK13771  97 RSGEEAYCKNRLGYGEELDGFFAEYAKVKVTSLVKVPPNVSDEGAVIVPCVTGMVyRGLRRAG---VKKGETVLVTGAGG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 175 LGYITAILLRKLY---------PESKIYVFGK-TDYKLSHFSFVDDVffiNKIPEGltfDHAFECVGGrgsqSAINQMID 244
Cdd:PRK13771 174 GVGIHAIQVAKALgakviavtsSESKAKIVSKyADYVIVGSKFSEEV---KKIGGA---DIVIETVGT----PTLEESLR 243

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 926233843 245 YISPEGSIALLGVSEFPVEVNTRL--VLEKGLTLIGSSRSGSKDFQDVVDL 293
Cdd:PRK13771 244 SLNMGGKIIQIGNVDPSPTYSLRLgyIILKDIEIIGHISATKRDVEEALKL 294
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 28-326 4.33e-07

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


Pssm-ID: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 50.77  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADqryyTGSRD--ENVLSQKLPMSLI---------HEGVGEVVFDSKGVFNK---GTKVVMVPNTPTE 93
Cdd:cd08262   26 VLVKVLACGICGSD----LHATAhpEAMVDDAGGPSLMdlgadivlgHEFCGEVVDYGPGTERKlkvGTRVTSLPLLLCG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  94 kddviaeNYLKSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRfekKSISNKNTFGIWGDG 173
Cdd:cd08262  102 -------QGASCGIGLSPEAPGGYAEYMLLSEALLLRVPDGLSMEDAALTEPLAVGLHAVRR---ARLTPGEVALVIGCG 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 174 NLGyITAILLRKLYPESKIYVfgktdyklSHFS--------------FVD---DVFFINKIPE-----GLTFDHAFECVG 231
Cdd:cd08262  172 PIG-LAVIAALKARGVGPIVA--------SDFSperralalamgadiVVDpaaDSPFAAWAAElaragGPKPAVIFECVG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 232 GRGsqsAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTL---IGSSRSgskDFQDVVDLYIQYPdiVDKLALLK 308
Cdd:cd08262  243 APG---LIQQIIEGAPPGGRIVVVGVCMESDNIEPALAIRKELTLqfsLGYTPE---EFADALDALAEGK--VDVAPMVT 314

                        330
                 ....*....|....*...
gi 926233843 309 GqefeIATINDLTEAFEA 326
Cdd:cd08262  315 G----TVGLDGVPDAFEA 328
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 234-339 3.20e-06

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 48.28  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 234 GSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKGLTLIGSsrSGSKDF----------QDVVDLyiqYPDIVDK 303
Cdd:PRK05396 241 GAPSAFRQMLDNMNHGGRIAMLGIPPGDMAIDWNKVIFKGLTIKGI--YGREMFetwykmsallQSGLDL---SPIITHR 315

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 926233843 304 LALlkgQEFEiatindltEAFEADLSTSWGKTVLKW 339
Cdd:PRK05396 316 FPI---DDFQ--------KGFEAMRSGQSGKVILDW 340
Glu_dehyd_C pfam16912
Glucose dehydrogenase C-terminus;
169-338 3.76e-06

Glucose dehydrogenase C-terminus;


Pssm-ID: 407146 [Multi-domain]  Cd Length: 211  Bit Score: 46.94  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  169 IWGDGNLGYITAILLRKLYPESKIYVFGKTD---------------YKLSHFSFVDDvffinkIPE-GLTFDHAFECVgg 232
Cdd:pfam16912  36 VLGNGPLGLLALAMLRVQRGFDRVYCLGRRDrpdptidlveelgatYVDSRETPVDE------IPAaHEPMDLVYEAT-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  233 rGSQSAINQMIDYISPEGSIALLGVS---EFPV---EVNTRLVLEKgLTLIGSSRSGSKDFQDVVDLYIQYP-DIVDKLa 305
Cdd:pfam16912 108 -GYAPHAFEAIDALAPNGVAALLGVPtswTFEIdggALHRELVLHN-KALVGSVNANRRHFEAAADTLAAAPeWFLDAL- 184

                         170       180       190
                  ....*....|....*....|....*....|...
gi 926233843  306 llkgqefeIATINDLTEAFEAdlsTSWGKTVLK 338
Cdd:pfam16912 185 --------VTGVVPLDEFEEA---FEDGDDDIK 206
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
223-326 5.58e-05

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 44.30  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 223 FDHAFECVggrGSQSAINQMIDYISPEGSIALLGVS----EFPVEVNTRLVLEKGL--TLIGSSRsGSKDFQDVVDLYIQ 296
Cdd:COG1062  244 VDYAFETT---GNPAVIRQALEALRKGGTVVVVGLAppgaEISLDPFQLLLTGRTIrgSYFGGAV-PRRDIPRLVDLYRA 319

                         90       100       110
                 ....*....|....*....|....*....|..
gi 926233843 297 --YPdiVDKLAllkGQEFEIATINdltEAFEA 326
Cdd:COG1062  320 grLP--LDELI---TRRYPLDEIN---EAFDD 343
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 28-337 1.73e-04

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 42.99  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  28 VIVRPLYMSICAADQRYYtgsrDENVLSQ---KLPMSLIHEGVGEVVFDSKGVfnKGTKVvmvpntpteKDDVIAENYL- 103
Cdd:cd05281   28 VLIKVLAASICGTDVHIY----EWDEWAQsriKPPLIFGHEFAGEVVEVGEGV--TRVKV---------GDYVSAETHIv 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 104 -KSSYFRSSG--H------------DGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEkksISNKNTFg 168
Cdd:cd05281   93 cGKCYQCRTGnyHvcqntkilgvdtDGCFAEYVVVPEENLWKNDKDIPPEIASIQEPLGNAVHTVLAGD---VSGKSVL- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 169 IWGDGNLGyITAILLRKLYPESKIYVFGKTDYKLS-----------HfSFVDDVFFINKIPEGLTFDHAFECvggRGSQS 237
Cdd:cd05281  169 ITGCGPIG-LMAIAVAKAAGASLVIASDPNPYRLElakkmgadvviN-PREEDVVEVKSVTDGTGVDVVLEM---SGNPK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 238 AINQMIDYISPEGSIALLGVSEFPVEVN-TRLVLEKGLTLIGSsrSGSKDFQ--DVVDLYIQY------PDIVDKlalLK 308
Cdd:cd05281  244 AIEQGLKALTPGGRVSILGLPPGPVDIDlNNLVIFKGLTVQGI--TGRKMFEtwYQVSALLKSgkvdlsPVITHK---LP 318

                        330       340
                 ....*....|....*....|....*....
gi 926233843 309 GQEFEiatindltEAFEADLSTSWGKTVL 337
Cdd:cd05281  319 LEDFE--------EAFELMRSGKCGKVVL 339
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 224-336 2.21e-04

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


Pssm-ID: 176239 [Multi-domain]  Cd Length: 365  Bit Score: 42.49  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 224 DHAFECVGgrgSQSAINQMIDYISPEGSIALLGVS----EFPVEVNTRLVleKGLTLIGSSR--SGSKDF-QDVVDLYIQ 296
Cdd:cd08278  256 DYALDTTG---VPAVIEQAVDALAPRGTLALVGAPppgaEVTLDVNDLLV--SGKTIRGVIEgdSVPQEFiPRLIELYRQ 330

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 926233843 297 --YPdiVDKLAllkgQEFEIATINdltEAFEADLStswGKTV 336
Cdd:cd08278  331 gkFP--FDKLV----TFYPFEDIN---QAIADSES---GKVI 360
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
26-279 1.06e-03

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 40.59  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843  26 DYVIVRPLYMSICAAD-QRYYTGSrdenvlSQKLPMSLIHEGVGEVVFDSKGV--FNKGTKVVMVPNTPTEKDDVIAENY 102
Cdd:PRK10309  26 DDVLVKVASSGLCGSDiPRIFKNG------AHYYPITLGHEFSGYVEAVGSGVddLHPGDAVACVPLLPCFTCPECLRGF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 103 L---KSSYFRSSGHDGFMQDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRfeKKSISNKNTFgIWGDGNLGYIT 179
Cdd:PRK10309 100 YslcAKYDFIGSRRDGGNAEYIVVKRKNLFALPTDMPIEDGAFIEPITVGLHAFHL--AQGCEGKNVI-IIGAGTIGLLA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 180 AILLRKLYPES--------KIYVFGKT---DYKLSHFSFVDDVffINKIPEGLTFDHAFecVGGRGSQSAINQMIDYISP 248
Cdd:PRK10309 177 IQCAVALGAKSvtaidinsEKLALAKSlgaMQTFNSREMSAPQ--IQSVLRELRFDQLI--LETAGVPQTVELAIEIAGP 252

                        250       260       270
                 ....*....|....*....|....*....|....
gi 926233843 249 EGSIALLGVSEFPVEVNTR---LVLEKGLTLIGS 279
Cdd:PRK10309 253 RAQLALVGTLHHDLHLTSAtfgKILRKELTVIGS 286
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 207-338 2.19e-03

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: 39.36  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 207 FVDDVffiNKIPEGLTFDHAFECVGGrgsqSAINQMIDYISPEGSIALLGV-SEFPVEVNTRLVLEKGLTLIGSS-RSGS 284
Cdd:COG0604  196 FAERV---RALTGGRGVDVVLDTVGG----DTLARSLRALAPGGRLVSIGAaSGAPPPLDLAPLLLKGLTLTGFTlFARD 268

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 285 K-----DFQDVVDLYIQypdivDKLALLKGQEFEIAtinDLTEAFEADLS-TSWGKTVLK 338
Cdd:COG0604  269 PaerraALAELARLLAA-----GKLRPVIDRVFPLE---EAAEAHRLLESgKHRGKVVLT 320
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 118-283 2.53e-03

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


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 39.18  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 118 QDFVLLNHDRAVPLPDDIDLSIISYTELVTVSLHAIRRFEkksISNKNTFGIWGDGNLGYITAILLrKLYPESKIYVFGK 197
Cdd:cd08255   55 AERVVVPANLLVPLPDGLPPERAALTALAATALNGVRDAE---PRLGERVAVVGLGLVGLLAAQLA-KAAGAREVVGVDP 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 926233843 198 TDYKL----SHFSFVDDVFFINKIPEGLTFDHAFECvggRGSQSAINQMIDYISPEGSIALLGVSEFPVEVNTRLVLEKG 273
Cdd:cd08255  131 DAARRelaeALGPADPVAADTADEIGGRGADVVIEA---SGSPSALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKR 207

                        170
                 ....*....|
gi 926233843 274 LTLIgSSRSG 283
Cdd:cd08255  208 LPIR-SSQVY 216
 
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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