NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1243936875|emb|SOE22594|]
View 

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase [Spirosomataceae bacterium TFI 002]

Protein Classification

zinc-binding alcohol dehydrogenase family protein( domain architecture ID 10169614)

zinc-binding alcohol dehydrogenase family protein similar to Escherichia coli L-galactonate-5-dehydrogenase that catalyzes the oxidation of L-galactonate to D-tagaturonate

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1-339 2.06e-170

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: 477.07  E-value: 2.06e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHsHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08261     1 MKALVCEKPGRLEV-VDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGE--GVAGLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSKLDFDQLALVETLGIGLHAVNRATI 160
Cdd:cd08261    78 GDRVVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRRAGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 161 TQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSlKNNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATG 240
Cdd:cd08261   158 TAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFA-RELGADDTINVGDEDVAARLRELTDGEGADVVIDATG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 241 NKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTAFETL 320
Cdd:cd08261   237 NPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPEALITHRFPFEDV 316

                         330
                  ....*....|....*....
gi 1243936875 321 PEVFPLWLNPEEDVIKAIV 339
Cdd:cd08261   317 PEAFDLWEAPPGGVIKVLI 335
 
Name Accession Description Interval E-value
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1-339 2.06e-170

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: 477.07  E-value: 2.06e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHsHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08261     1 MKALVCEKPGRLEV-VDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGE--GVAGLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSKLDFDQLALVETLGIGLHAVNRATI 160
Cdd:cd08261    78 GDRVVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRRAGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 161 TQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSlKNNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATG 240
Cdd:cd08261   158 TAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFA-RELGADDTINVGDEDVAARLRELTDGEGADVVIDATG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 241 NKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTAFETL 320
Cdd:cd08261   237 NPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPEALITHRFPFEDV 316

                         330
                  ....*....|....*....
gi 1243936875 321 PEVFPLWLNPEEDVIKAIV 339
Cdd:cd08261   317 PEAFDLWEAPPGGVIKVLI 335
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-342 1.65e-124

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: 360.99  E-value: 1.65e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIiTIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:COG1063     1 MKALVLHGPGDLRLEEVPDP-EPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGE--GVTGLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGV-HIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRA 158
Cdd:COG1063    78 GDRVVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPAANLVKvPDGLSDEAAALVEPLAVALHAVERA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 159 TITQNDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNLPTVIFD 237
Cdd:COG1063   158 GVKPGDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPERLELARELG-ADAVVNPREEDLVEAVRELTGGRGADVVIE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTAF 317
Cdd:COG1063   237 AVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPL 316

                         330       340
                  ....*....|....*....|....*
gi 1243936875 318 ETLPEVFPLWLNPEEDVIKAIVYLD 342
Cdd:COG1063   317 DDAPEAFEAAADRADGAIKVVLDPD 341
PRK10083 PRK10083
putative oxidoreductase; Provisional
 1-326 2.23e-61

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 199.58  E-value: 2.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEdIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGsyQNTRTLKI 80
Cdd:PRK10083    1 MKSIVIEKPNSLAIEERP-IPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVG--EGVDAARI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSKLDFDQLA-LVETLGIGLHAVNRAT 159
Cdd:PRK10083   78 GERVAVDPVISCGHCYPCSIGKPNVCTSLVVLGVHRDGGFSEYAVVPAKNAHRIPDAIADQYAvMVEPFTIAANVTGRTG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 160 ITQNDIVLIIGAGPIGLSTAQFAK-LSGAK-VLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERlsGNLPTVIFD 237
Cdd:PRK10083  158 PTEQDVALIYGAGPVGLTIVQVLKgVYNVKaVIVADRIDERLALAKESG-ADWVINNAQEPLGEALEEK--GIKPTLIID 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLAAQGAKIIFIG-------LFQGEVTfedpsfhKKEITLMSSRNSLPRdFKQIINLMETGKINTAPW 310
Cdd:PRK10083  235 AACHPSILEEAVTLASPAARIVLMGfssepseIVQQGIT-------GKELSIFSSRLNANK-FPVVIDWLSKGLIDPEKL 306

                         330
                  ....*....|....*.
gi 1243936875 311 LTHKTAFETLPEVFPL 326
Cdd:PRK10083  307 ITHTFDFQHVADAIEL 322
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 26-133 1.44e-45

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: 150.84  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  26 DEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVCQACKRGLSNC 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGP--GVTGLKVGDRVVVEPLIPCGKCEYCREGRYNL 78

                          90       100
                  ....*....|....*....|....*...
gi 1243936875 106 CENLQVLGVHIDGGMTEYMKLPQDKVHP 133
Cdd:pfam08240  79 CPNGRFLGYDRDGGFAEYVVVPERNLVP 106
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 166-200 8.25e-03

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


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 36.33  E-value: 8.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1243936875  166 VLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQ 200
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLR 57
 
Name Accession Description Interval E-value
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 1-339 2.06e-170

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: 477.07  E-value: 2.06e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHsHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08261     1 MKALVCEKPGRLEV-VDIPEPVPGAGEVLVRVKRVGICGSDLHIYHGRNPFASYPRILGHELSGEVVEVGE--GVAGLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSKLDFDQLALVETLGIGLHAVNRATI 160
Cdd:cd08261    78 GDRVVVDPYISCGECYACRKGRPNCCENLQVLGVHRDGGFAEYIVVPADALLVPEGLSLDQAALVEPLAIGAHAVRRAGV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 161 TQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSlKNNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATG 240
Cdd:cd08261   158 TAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFA-RELGADDTINVGDEDVAARLRELTDGEGADVVIDATG 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 241 NKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTAFETL 320
Cdd:cd08261   237 NPASMEEAVELVAHGGRVVLVGLSKGPVTFPDPEFHKKELTILGSRNATREDFPDVIDLLESGKVDPEALITHRFPFEDV 316

                         330
                  ....*....|....*....
gi 1243936875 321 PEVFPLWLNPEEDVIKAIV 339
Cdd:cd08261   317 PEAFDLWEAPPGGVIKVLI 335
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 1-342 1.65e-124

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: 360.99  E-value: 1.65e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIiTIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:COG1063     1 MKALVLHGPGDLRLEEVPDP-EPGPGEVLVRVTAVGICGSDLHIYRGGYPFVRPPLVLGHEFVGEVVEVGE--GVTGLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGV-HIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRA 158
Cdd:COG1063    78 GDRVVVEPNIPCGECRYCRRGRYNLCENLQFLGIaGRDGGFAEYVRVPAANLVKvPDGLSDEAAALVEPLAVALHAVERA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 159 TITQNDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNLPTVIFD 237
Cdd:COG1063   158 GVKPGDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPERLELARELG-ADAVVNPREEDLVEAVRELTGGRGADVVIE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTAF 317
Cdd:COG1063   237 AVGAPAALEQALDLVRPGGTVVLVGVPGGPVPIDLNALVRKELTLRGSRNYTREDFPEALELLASGRIDLEPLITHRFPL 316

                         330       340
                  ....*....|....*....|....*
gi 1243936875 318 ETLPEVFPLWLNPEEDVIKAIVYLD 342
Cdd:COG1063   317 DDAPEAFEAAADRADGAIKVVLDPD 341
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 1-339 4.42e-87

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: 265.63  E-value: 4.42e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHshKE-DIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFtYPRILGHELGAEVVEIGSyqNTRTLK 79
Cdd:cd08236     1 MKALVLTGPGDLRY--EDiPKPEPGPGEVLVKVKACGICGSDIPRYLGTGAYH-PPLVLGHEFSGTVEEVGS--GVDDLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  80 IGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRA 158
Cdd:cd08236    76 VGDRVAVNPLLPCGKCEYCKKGEYSLCSNYDYIGSRRDGAFAEYVSVPARNLIKiPDHVDYEEAAMIEPAAVALHAVRLA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 159 TITQNDIVLIIGAGPIGLSTAQFAKLSGAK-VLIADLNAKRLQFSLKNNlADEVIELNDRLTSQmLKERLSGNLPTVIFD 237
Cdd:cd08236   156 GITLGDTVVVIGAGTIGLLAIQWLKILGAKrVIAVDIDDEKLAVARELG-ADDTINPKEEDVEK-VRELTEGRGADLVIE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHK---KEITLMSSRNSL-----PRDFKQIINLMETGKINTAP 309
Cdd:cd08236   234 AAGSPATIEQALALARPGGKVVLVGIPYGDVTLSEEAFEKilrKELTIQGSWNSYsapfpGDEWRTALDLLASGKIKVEP 313

                         330       340       350
                  ....*....|....*....|....*....|
gi 1243936875 310 WLTHKTAFETLPEVFPLWLNPEEDVIKAIV 339
Cdd:cd08236   314 LITHRLPLEDGPAAFERLADREEFSGKVLL 343
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-340 1.06e-84

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: 259.38  E-value: 1.06e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHshKE-DIITIGSDEVLVKIKRIGICGTDYHAFRGRqPFFTYPRILGHELGAEVVEIGSyqNTRTLK 79
Cdd:cd08234     1 MKALVYEGPGELEV--EEvPVPEPGPDEVLIKVAACGICGTDLHIYEGE-FGAAPPLVPGHEFAGVVVAVGS--KVTGFK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  80 IGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRA 158
Cdd:cd08234    76 VGDRVAVDPNIYCGECFYCRRGRPNLCENLTAVGVTRNGGFAEYVVVPAKQVYKiPDNLSFEEAALAEPLSCAVHGLDLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 159 TITQNDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVIElndrlTSQMLKERLSGNLPT---V 234
Cdd:cd08234   156 GIKPGDSVLVFGAGPIGLLLAQLLKLNGAsRVTVAEPNEEKLELAKKLG-ATETVD-----PSREDPEAQKEDNPYgfdV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 235 IFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSF--HKKEITLMSSRnSLPRDFKQIINLMETGKINTAPWLT 312
Cdd:cd08234   230 VIEATGVPKTLEQAIEYARRGGTVLVFGVYAPDARVSISPFeiFQKELTIIGSF-INPYTFPRAIALLESGKIDVKGLVS 308

                         330       340
                  ....*....|....*....|....*...
gi 1243936875 313 HKTAFETLPEVFPLWLNPEedVIKAIVY 340
Cdd:cd08234   309 HRLPLEEVPEALEGMRSGG--ALKVVVV 334
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 1-340 1.66e-79

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: 246.35  E-value: 1.66e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHshkEDIIT--IGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTL 78
Cdd:cd08235     1 MKAAVLHGPNDVRL---EEVPVpePGPGEVLVKVRACGICGTDVKKIRGGHTDLKPPRILGHEIAGEIVEVGD--GVTGF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  79 KIGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKV------HPSSKLDFDQLALVETLGIGL 152
Cdd:cd08235    76 KVGDRVFVAPHVPCGECHYCLRGNENMCPNYKKFGNLYDGGFAEYVRVPAWAVkrggvlKLPDNVSFEEAALVEPLACCI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 HAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNL 231
Cdd:cd08235   156 NAQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGArKVIVSDLNEFRLEFAKKLG-ADYTIDAAEEDLVEKVRELTDGRG 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 232 PTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFE-DPS-FHKKEITLMSSRNSLPRDFKQIINLMETGKINTAP 309
Cdd:cd08235   235 ADVVIVATGSPEAQAQALELVRKGGRILFFGGLPKGSTVNiDPNlIHYREITITGSYAASPEDYKEALELIASGKIDVKD 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1243936875 310 WLTHKTAFETLPEVFPLWLNPEEdvIKAIVY 340
Cdd:cd08235   315 LITHRFPLEDIEEAFELAADGKS--LKIVIT 343
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 3-340 4.24e-77

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: 240.09  E-value: 4.24e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   3 SIILNEPGTLShSHKEDIITIGSDEVLVKIKRIGICGTDYHAFR-GR-------QPFftyprILGHELGAEVVEIGSyqN 74
Cdd:cd05285     1 AAVLHGPGDLR-LEERPIPEPGPGEVLVRVRAVGICGSDVHYYKhGRigdfvvkEPM-----VLGHESAGTVVAVGS--G 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  75 TRTLKIGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVH-IDGGMTEYMKLPQDKVH--PSSkLDFDQLALVETLGIG 151
Cdd:cd05285    73 VTHLKVGDRVAIEPGVPCRTCEFCKSGRYNLCPDMRFAATPpVDGTLCRYVNHPADFCHklPDN-VSLEEGALVEPLSVG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 152 LHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSlKNNLADEVI---ELNDRLTSQMLKERL 227
Cdd:cd05285   152 VHACRRAGVRPGDTVLVFGAGPIGLLTAAVAKAFGAtKVVVTDIDPSRLEFA-KELGATHTVnvrTEDTPESAEKIAELL 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 228 SGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSS---RNslprDFKQIINLMETGK 304
Cdd:cd05285   231 GGKGPDVVIECTGAESCIQTAIYATRPGGTVVLVGMGKPEVTLPLSAASLREIDIRGVfryAN----TYPTAIELLASGK 306

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1243936875 305 INTAPWLTHKTAFETLPEVFPLWLNPEEDVIKAIVY 340
Cdd:cd05285   307 VDVKPLITHRFPLEDAVEAFETAAKGKKGVIKVVIE 342
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 27-300 6.03e-72

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


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 224.51  E-value: 6.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  27 EVLVKIKRIGICGTDYHAFRGRQPFF-TYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVCQACKRglsnC 105
Cdd:cd05188     1 EVLVRVEAAGLCGTDLHIRRGGYPPPpKLPLILGHEGAGVVVEVGP--GVTGVKVGDRVVVLPNLGCGTCELCRE----L 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 106 CENLQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLALV-ETLGIGLHAVNRA-TITQNDIVLIIGAGPIGLSTAQFA 182
Cdd:cd05188    75 CPGGGILGEGLDGGFAEYVVVPADNLVPlPDGLSLEEAALLpEPLATAYHALRRAgVLKPGDTVLVLGAGGVGLLAAQLA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 183 KLSGAKVLIADLNAKRLQFsLKNNLADEVIELNDRLTSQMLKErLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIG 262
Cdd:cd05188   155 KAAGARVIVTDRSDEKLEL-AKELGADHVIDYKEEDLEEELRL-TGGGGADVVIDAVGGPETLAQALRLLRPGGRIVVVG 232

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1243936875 263 LFQGEVTFEDPS-FHKKEITLMSSRNSLPRDFKQIINLM 300
Cdd:cd05188   233 GTSGGPPLDDLRrLLFKELTIIGSTGGTREDFEEALDLL 271
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 18-339 9.58e-69

(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: 218.95  E-value: 9.58e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  18 EDIIT--IGSDEVLVKIKRIGICGTDYHAFRG--------RQPFFT---YPRILGHELGAEVVEIGSyqNTRTLKIGDKV 84
Cdd:cd08233    15 EEVPEppVKPGEVKIKVAWCGICGSDLHEYLDgpifipteGHPHLTgetAPVTLGHEFSGVVVEVGS--GVTGFKVGDRV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  85 SIEPYINCRVCQACKRGLSNCCENLQVLGVH-IDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRATITQ 162
Cdd:cd08233    93 VVEPTIKCGTCGACKRGLYNLCDSLGFIGLGgGGGGFAEYVVVPAYHVHKlPDNVPLEEAALVEPLAVAWHAVRRSGFKP 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 163 NDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKnNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATGN 241
Cdd:cd08233   173 GDTALVLGAGPIGLLTILALKAAGAsKIIVSEPSEARRELAEE-LGATIVLDPTEVDVVAEVRKLTGGGGVDVSFDCAGV 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 242 KKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTA----- 316
Cdd:cd08233   252 QATLDTAIDALRPRGTAVNVAIWEKPISFNPNDLVLKEKTLTGSICYTREDFEEVIDLLASGKIDAEPLITSRIPlediv 331

                         330       340
                  ....*....|....*....|....*.
gi 1243936875 317 ---FETLpevfplwLNPEEDVIKAIV 339
Cdd:cd08233   332 ekgFEEL-------INDKEQHVKILV 350
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 1-338 1.50e-67

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 214.98  E-value: 1.50e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:COG1064     1 MKAAVLTEPGGPLELEEVPRPEPGPGEVLVKVEACGVCHSDLHVAEGEWPVPKLPLVPGHEIVGRVVAVGP--GVTGFKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLA-LVETLGIGLHAVNRA 158
Cdd:COG1064    79 GDRVGVGWVDSCGTCEYCRSGRENLCENGRFTGYTTDGGYAEYVVVPARFLVKlPDGLDPAEAApLLCAGITAYRALRRA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 159 TITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKnnL-ADEVIELNDRLTSQMLKERLSgnlPTVIFD 237
Cdd:COG1064   159 GVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARE--LgADHVVNSSDEDPVEAVRELTG---ADVVID 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKIntapwlthktAF 317
Cdd:COG1064   234 TVGAPATVNAALALLRRGGRLVLVGLPGGPIPLPPFDLILKERSIRGSLIGTRADLQEMLDLAAEGKI----------KP 303

                         330       340
                  ....*....|....*....|.
gi 1243936875 318 ETlpEVFPLwlnpeEDVIKAI 338
Cdd:COG1064   304 EV--ETIPL-----EEANEAL 317
PRK10083 PRK10083
putative oxidoreductase; Provisional
 1-326 2.23e-61

putative oxidoreductase; Provisional


Pssm-ID: 182229 [Multi-domain]  Cd Length: 339  Bit Score: 199.58  E-value: 2.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEdIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGsyQNTRTLKI 80
Cdd:PRK10083    1 MKSIVIEKPNSLAIEERP-IPQPAAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVG--EGVDAARI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSKLDFDQLA-LVETLGIGLHAVNRAT 159
Cdd:PRK10083   78 GERVAVDPVISCGHCYPCSIGKPNVCTSLVVLGVHRDGGFSEYAVVPAKNAHRIPDAIADQYAvMVEPFTIAANVTGRTG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 160 ITQNDIVLIIGAGPIGLSTAQFAK-LSGAK-VLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERlsGNLPTVIFD 237
Cdd:PRK10083  158 PTEQDVALIYGAGPVGLTIVQVLKgVYNVKaVIVADRIDERLALAKESG-ADWVINNAQEPLGEALEEK--GIKPTLIID 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLAAQGAKIIFIG-------LFQGEVTfedpsfhKKEITLMSSRNSLPRdFKQIINLMETGKINTAPW 310
Cdd:PRK10083  235 AACHPSILEEAVTLASPAARIVLMGfssepseIVQQGIT-------GKELSIFSSRLNANK-FPVVIDWLSKGLIDPEKL 306

                         330
                  ....*....|....*.
gi 1243936875 311 LTHKTAFETLPEVFPL 326
Cdd:PRK10083  307 ITHTFDFQHVADAIEL 322
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 1-331 1.55e-59

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: 194.76  E-value: 1.55e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAF------RGRqpfFTYPRILGHELGAEVVEIGSyqN 74
Cdd:cd05281     1 MKAIVKTKAGPGAELVEVPVPKPGPGEVLIKVLAASICGTDVHIYewdewaQSR---IKPPLIFGHEFAGEVVEVGE--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  75 TRTLKIGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSK-LDFDQLALVETLGIGLH 153
Cdd:cd05281    76 VTRVKVGDYVSAETHIVCGKCYQCRTGNYHVCQNTKILGVDTDGCFAEYVVVPEENLWKNDKdIPPEIASIQEPLGNAVH 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 154 AVNRATITQNDiVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNlADEVIE-LNDRLTSqmLKERLSGNL 231
Cdd:cd05281   156 TVLAGDVSGKS-VLITGCGPIGLMAIAVAKAAGASLVIAsDPNPYRLELAKKMG-ADVVINpREEDVVE--VKSVTDGTG 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 232 PTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFE---DPSFHKKEITLMSSRnslpRDF---KQIINLMETGKI 305
Cdd:cd05281   232 VDVVLEMSGNPKAIEQGLKALTPGGRVSILGLPPGPVDIDlnnLVIFKGLTVQGITGR----KMFetwYQVSALLKSGKV 307

                         330       340
                  ....*....|....*....|....*.
gi 1243936875 306 NTAPWLTHKTAFETLPEVFPLWLNPE 331
Cdd:cd05281   308 DLSPVITHKLPLEDFEEAFELMRSGK 333
Zn_ADH4 cd08258
Alcohol dehydrogenases of the MDR family; This group shares the zinc coordination sites of the ...
 22-303 8.79e-58

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: 189.06  E-value: 8.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  22 TIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEP-YINCRVCQACKR 100
Cdd:cd08258    23 EPGPGEVLIKVAAAGICGSDLHIYKGDYDPVETPVVLGHEFSGTIVEVGP--DVEGWKVGDRVVSETtFSTCGRCPYCRR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 101 GLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSK-LDFDQLALVETLGIGLHAVN-RATITQNDIVLIIGAGPIGLST 178
Cdd:cd08258   101 GDYNLCPHRKGIGTQADGGFAEYVLVPEESLHELPEnLSLEAAALTEPLAVAVHAVAeRSGIRPGDTVVVFGPGPIGLLA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 179 AQFAKLSGAKVLIADLNAKRLQFSLKNNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATGNKKSMETSFSLAAQGAKI 258
Cdd:cd08258   181 AQVAKLQGATVVVVGTEKDEVRLDVAKELGADAVNGGEEDLAELVNEITDGDGADVVIECSGAVPALEQALELLRKGGRI 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1243936875 259 IFIGLF---QGEVTFEDPSFHkkEITLMSSRNSLPRDFKQIINLMETG 303
Cdd:cd08258   261 VQVGIFgplAASIDVERIIQK--ELSVIGSRSSTPASWETALRLLASG 306
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 1-339 1.67e-55

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: 184.40  E-value: 1.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd05278     1 MKALVYLGPGKIGLEEVPDPKIQGPHDAIVRVTATSICGSDLHIYRGGVPGAKHGMILGHEFVGEVVEVGS--DVKRLKP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQV---LGVHIDGGMTEYMKLPQDKVH----PSSKLDFDQLALVETLGIGLH 153
Cdd:cd05278    79 GDRVSVPCITFCGRCRFCRRGYHAHCENGLWgwkLGNRIDGGQAEYVRVPYADMNlakiPDGLPDEDALMLSDILPTGFH 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 154 AVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNLP 232
Cdd:cd05278   159 GAELAGIKPGSTVAVIGAGPVGLCAVAGARLLGAARIIAvDSNPERLDLAKEAG-ATDIINPKNGDIVEQILELTGGRGV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 233 TVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPS-FHKKEITLM----SSRNSLPRdfkqIINLMETGKINT 307
Cdd:cd05278   238 DCVIEAVGFEETFEQAVKVVRPGGTIANVGVYGKPDPLPLLGeWFGKNLTFKtglvPVRARMPE----LLDLIEEGKIDP 313

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1243936875 308 APWLTHKTAFETLPEVFPLWLNPEEDVIKAIV 339
Cdd:cd05278   314 SKLITHRFPLDDILKAYRLFDNKPDGCIKVVI 345
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 24-324 1.02e-52

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: 177.05  E-value: 1.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQPFFTY-PRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVCQACKRGL 102
Cdd:cd08254    25 GPGEVLVKVKAAGVCHSDLHILDGGVPTLTKlPLTLGHEIAGTVVEVGA--GVTNFKVGDRVAVPAVIPCGACALCRRGR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 103 SNCCENLQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLAL----VETlgiGLHAVNRA-TITQNDIVLIIGAGPIGL 176
Cdd:cd08254   103 GNLCLNQGMPGLGIDGGFAEYIVVPARALVPvPDGVPFAQAAVatdaVLT---PYHAVVRAgEVKPGETVLVIGLGGLGL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 177 STAQFAKLSGAKVLIADLNAKRLQFSLKNNlADEVIElNDRLTSQMLKERLSGNLPTVIFDATGNKKSMETSFSLAAQGA 256
Cdd:cd08254   180 NAVQIAKAMGAAVIAVDIKEEKLELAKELG-ADEVLN-SLDDSPKDKKAAGLGGGFDVIFDFVGTQPTFEDAQKAVKPGG 257

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243936875 257 KIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTApwlTHKTAFETLPEVF 324
Cdd:cd08254   258 RIVVVGLGRDKLTVDLSDLIARELRIIGSFGGTPEDLPEVLDLIAKGKLDPQ---VETRPLDEIPEVL 322
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 24-339 2.30e-49

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: 168.26  E-value: 2.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFR---------GRQPFFTYPR--ILGHELGAEVVEIGSyQNTRTLKIGDKVSIEPYINC 92
Cdd:cd08262    22 GPGQVLVKVLACGICGSDLHATAhpeamvddaGGPSLMDLGAdiVLGHEFCGEVVDYGP-GTERKLKVGTRVTSLPLLLC 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  93 RVCQACKRGLSNcceNLQvlgvhidGGMTEYMKLPQDK-VHPSSKLDFDQLALVETLGIGLHAVNRATITQNDIVLIIGA 171
Cdd:cd08262   101 GQGASCGIGLSP---EAP-------GGYAEYMLLSEALlLRVPDGLSMEDAALTEPLAVGLHAVRRARLTPGEVALVIGC 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 172 GPIGLSTAQFAKLSGAK-VLIADLNAKRLQFSLKNNlADEVIElnDRLTS-----QMLKERLSGNLPTVIFDATGNKKSM 245
Cdd:cd08262   171 GPIGLAVIAALKARGVGpIVASDFSPERRALALAMG-ADIVVD--PAADSpfaawAAELARAGGPKPAVIFECVGAPGLI 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 246 ETSFSLAAQGAKIIFIGLFQGEVTFEdPSFHK-KEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTAFETLPEVF 324
Cdd:cd08262   248 QQIIEGAPPGGRIVVVGVCMESDNIE-PALAIrKELTLQFSLGYTPEEFADALDALAEGKVDVAPMVTGTVGLDGVPDAF 326

                         330
                  ....*....|....*
gi 1243936875 325 PLWLNPEEDvIKAIV 339
Cdd:cd08262   327 EALRDPEHH-CKILV 340
Zn_ADH5 cd08259
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-307 2.57e-48

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: 165.18  E-value: 2.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIIL---NEPGTLSHShkeDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRT 77
Cdd:cd08259     1 MKAAILhkpNKPLQIEEV---PDPEPGPGEVLIKVKAAGVCYRDLLFWKGFFPRGKYPLILGHEIVGTVEEVGE--GVER 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  78 LKIGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVE-TLGIGLHAV 155
Cdd:cd08259    76 FKPGDRVILYYYIPCGKCEYCLSGEENLCRNRAEYGEEVDGGFAEYVKVPERSLVKlPDNVSDESAALAAcVVGTAVHAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 156 NRATITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVLIADLNAKRLQFsLKNNLADEVIELNDrlTSQMLKERLSGNlptV 234
Cdd:cd08259   156 KRAGVKKGDTVLVTGAgGGVGIHAIQLAKALGARVIAVTRSPEKLKI-LKELGADYVIDGSK--FSEDVKKLGGAD---V 229

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243936875 235 IFDATGnKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFH-KKEITLMSSRNSLPRDFKQIINLMETGKINT 307
Cdd:cd08259   230 VIELVG-SPTIEESLRSLNKGGRLVLIGNVTPDPAPLRPGLLiLKEIRIIGSISATKADVEEALKLVKEGKIKP 302
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 24-326 1.90e-47

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: 163.18  E-value: 1.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYH--------AFRGRQPFftyprILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVC 95
Cdd:cd08232    20 GPGEVRVRVAAGGICGSDLHyyqhggfgTVRLREPM-----VLGHEVSGVVEAVGP--GVTGLAPGQRVAVNPSRPCGTC 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  96 QACKRGLSNCCENLQVLGV-----HIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRATITQNDIVLII 169
Cdd:cd08232    93 DYCRAGRPNLCLNMRFLGSamrfpHVQGGFREYLVVDASQCVPlPDGLSLRRAALAEPLAVALHAVNRAGDLAGKRVLVT 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 170 GAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVIELNDRLTS--QMLKERlsgnlPTVIFDATGNKKSME 246
Cdd:cd08232   173 GAGPIGALVVAAARRAGAaEIVATDLADAPLAVARAMG-ADETVNLARDPLAayAADKGD-----FDVVFEASGAPAALA 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 247 TSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPrDFKQIINLMETGKINTAPWLTHKTAFETLPEVFPL 326
Cdd:cd08232   247 SALRVVRPGGTVVQVGMLGGPVPLPLNALVAKELDLRGSFRFDD-EFAEAVRLLAAGRIDVRPLITAVFPLEEAAEAFAL 325
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 24-329 3.88e-47

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: 162.49  E-value: 3.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRIL-GHELGAEVVEIGsyQNTRTLKIGDKVSIEPYINCRVCQACKRGL 102
Cdd:cd08239    23 GPGEVLLRVKASGLCGSDLHYYYHGHRAPAYQGVIpGHEPAGVVVAVG--PGVTHFRVGDRVMVYHYVGCGACRNCRRGW 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 103 SNCCEN-LQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLALV-ETLGIGLHAVNRATITQNDIVLIIGAGPIGLSTA 179
Cdd:cd08239   101 MQLCTSkRAAYGWNRDGGHAEYMLVPEKTLIPlPDDLSFADGALLlCGIGTAYHALRRVGVSGRDTVLVVGAGPVGLGAL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 180 QFAKLSGAKVLIA-DLNAKRLQFSLKNNlADEVIELNDrLTSQMLKERLSGNLPTVIFDATGNKKSMETSFSLAAQGAKI 258
Cdd:cd08239   181 MLARALGAEDVIGvDPSPERLELAKALG-ADFVINSGQ-DDVQEIRELTSGAGADVAIECSGNTAARRLALEAVRPWGRL 258

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1243936875 259 IFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTAPWLTHKTAFETLPEVFPLWLN 329
Cdd:cd08239   259 VLVGEGGELTIEVSNDLIRKQRTLIGSWYFSVPDMEECAEFLARHKLEVDRLVTHRFGLDQAPEAYALFAQ 329
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 19-302 2.07e-46

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 161.27  E-value: 2.07e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  19 DIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSYQNTRT----LKIGDKVSIEPYINCRV 94
Cdd:cd08231    19 PLPDLEPGAVLVRVRLAGVCGSDVHTVAGRRPRVPLPIILGHEGVGRVVALGGGVTTDVagepLKVGDRVTWSVGAPCGR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  95 CQACKRGLSNCCENLQVLGV-------HIDGGMTEYMKLPQD----KVHPSSKLDFDQLAlVETLGIGLHAVNRATITQ- 162
Cdd:cd08231    99 CYRCLVGDPTKCENRKKYGHeascddpHLSGGYAEHIYLPPGtaivRVPDNVPDEVAAPA-NCALATVLAALDRAGPVGa 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 163 NDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVI---ELNDRLTSQMLKERLSGNLPTVIFDA 238
Cdd:cd08231   178 GDTVVVQGAGPLGLYAVAAAKLAGArRVIVIDGSPERLELAREFG-ADATIdidELPDPQRRAIVRDITGGRGADVVIEA 256

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1243936875 239 TGNKKSMETSFSLAAQGAKIIFIGLF--QGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMET 302
Cdd:cd08231   257 SGHPAAVPEGLELLRRGGTYVLVGSVapAGTVPLDPERIVRKNLTIIGVHNYDPSHLYRAVRFLER 322
ADH_N pfam08240
Alcohol dehydrogenase GroES-like domain; This is the catalytic domain of alcohol ...
 26-133 1.44e-45

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: 150.84  E-value: 1.44e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  26 DEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVCQACKRGLSNC 105
Cdd:pfam08240   1 GEVLVKVKAAGICGSDLHIYKGGNPPVKLPLILGHEFAGEVVEVGP--GVTGLKVGDRVVVEPLIPCGKCEYCREGRYNL 78

                          90       100
                  ....*....|....*....|....*...
gi 1243936875 106 CENLQVLGVHIDGGMTEYMKLPQDKVHP 133
Cdd:pfam08240  79 CPNGRFLGYDRDGGFAEYVVVPERNLVP 106
FDH_like_2 cd08284
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; ...
 1-326 5.59e-45

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 2; Glutathione-dependent formaldehyde dehydrogenases (FDHs) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. These tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176244 [Multi-domain]  Cd Length: 344  Bit Score: 157.03  E-value: 5.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPfFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08284     1 MKAVVFKGPGDVRVEEVPIPQIQDPTDAIVKVTAAAICGSDLHIYRGHIP-STPGFVLGHEFVGEVVEVGP--EVRTLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLG----VHIDGGMTEY----------MKLPQDKVhpssklDFDQLALVE 146
Cdd:cd08284    78 GDRVVSPFTIACGECFYCRRGQSGRCAKGGLFGyagsPNLDGAQAEYvrvpfadgtlLKLPDGLS------DEAALLLGD 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 147 TLGIGLHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKnnLADEVIELNDRLTSQMLKE 225
Cdd:cd08284   152 ILPTGYFGAKRAQVRPGDTVAVIGCGPVGLCAVLSAQVLGAARVFAvDPVPERLERAAA--LGAEPINFEDAEPVERVRE 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 226 RLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGE-VTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGK 304
Cdd:cd08284   230 ATEGRGADVVLEAVGGAAALDLAFDLVRPGGVISSVGVHTAEeFPFPGLDAYNKNLTLRFGRCPVRSLFPELLPLLESGR 309

                         330       340
                  ....*....|....*....|..
gi 1243936875 305 INTAPWLTHKTAFETLPEVFPL 326
Cdd:cd08284   310 LDLEFLIDHRMPLEEAPEAYRL 331
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 22-270 6.16e-44

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 154.21  E-value: 6.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  22 TIGSDEVLVKIKRIGICGTDYHAF------RGRQPfftYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVC 95
Cdd:PRK05396   22 EPGPNDVLIKVKKTAICGTDVHIYnwdewaQKTIP---VPMVVGHEFVGEVVEVGS--EVTGFKVGDRVSGEGHIVCGHC 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  96 QACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKV--HPSSkLDFDQLALVETLGIGLHAVNRATITQNDiVLIIGAGP 173
Cdd:PRK05396   97 RNCRAGRRHLCRNTKGVGVNRPGAFAEYLVIPAFNVwkIPDD-IPDDLAAIFDPFGNAVHTALSFDLVGED-VLITGAGP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 174 IGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNLPTVIFDATGNKKSMETSFSLA 252
Cdd:PRK05396  175 IGIMAAAVAKHVGArHVVITDVNEYRLELARKMG-ATRAVNVAKEDLRDVMAELGMTEGFDVGLEMSGAPSAFRQMLDNM 253

                         250
                  ....*....|....*...
gi 1243936875 253 AQGAKIIFIGLFQGEVTF 270
Cdd:PRK05396  254 NHGGRIAMLGIPPGDMAI 271
6_hydroxyhexanoate_dh_like cd08240
6-hydroxyhexanoate dehydrogenase; 6-hydroxyhexanoate dehydrogenase, an enzyme of the ...
 1-309 1.42e-43

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: 153.54  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRG------------RQPFFTYPRILGHELGAEVVE 68
Cdd:cd08240     1 MKAAAVVEPGKPLEEVEIDTPKPPGTEVLVKVTACGVCHSDLHIWDGgydlgggktmslDDRGVKLPLVLGHEIVGEVVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  69 IGSyqNTRTLKIGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPqdkvHPSSKLDFDQLALVE-- 146
Cdd:cd08240    81 VGP--DAADVKVGDKVLVYPWIGCGECPVCLAGDENLCAKGRALGIFQDGGYAEYVIVP----HSRYLVDPGGLDPALaa 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 147 TL---GIGLH-AVNRATITQND-IVLIIGAGPIGLSTAQFAK-LSGAKVLIADLNAKRLQFSLKNNlADEVIELNDRLTS 220
Cdd:cd08240   155 TLacsGLTAYsAVKKLMPLVADePVVIIGAGGLGLMALALLKaLGPANIIVVDIDEAKLEAAKAAG-ADVVVNGSDPDAA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 221 QMLKERLSGNLPTVIfDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLM 300
Cdd:cd08240   234 KRIIKAAGGGVDAVI-DFVNNSATASLAFDILAKGGKLVLVGLFGGEATLPLPLLPLRALTIQGSYVGSLEELRELVALA 312


                  ....*....
gi 1243936875 301 ETGKINTAP 309
Cdd:cd08240   313 KAGKLKPIP 321
PLN02702 PLN02702
L-idonate 5-dehydrogenase
 23-317 1.58e-43

L-idonate 5-dehydrogenase


Pssm-ID: 215378 [Multi-domain]  Cd Length: 364  Bit Score: 153.78  E-value: 1.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  23 IGSDEVLVKIKRIGICGTDYHAFRG-RQPFF--TYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVCQACK 99
Cdd:PLN02702   39 LGPHDVRVRMKAVGICGSDVHYLKTmRCADFvvKEPMVIGHECAGIIEEVGS--EVKHLVVGDRVALEPGISCWRCNLCK 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 100 RGLSNCCENLQVLG---VHidGGMTEYMklpqdkVHPSS-------KLDFDQLALVETLGIGLHAVNRATITQNDIVLII 169
Cdd:PLN02702  117 EGRYNLCPEMKFFAtppVH--GSLANQV------VHPADlcfklpeNVSLEEGAMCEPLSVGVHACRRANIGPETNVLVM 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 170 GAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSlKNNLADEVIELNDRLTSQM-----LKERLSGNLpTVIFDATGNKK 243
Cdd:PLN02702  189 GAGPIGLVTMLAARAFGApRIVIVDVDDERLSVA-KQLGADEIVLVSTNIEDVEseveeIQKAMGGGI-DVSFDCVGFNK 266

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243936875 244 SMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMS---SRNSLPrdfkQIINLMETGKINTAPWLTHKTAF 317
Cdd:PLN02702  267 TMSTALEATRAGGKVCLVGMGHNEMTVPLTPAAAREVDVVGvfrYRNTWP----LCLEFLRSGKIDVKPLITHRFGF 339
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-325 4.24e-42

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


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 149.29  E-value: 4.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08260     1 MRAAVYEEFGEPLEIREVPDPEPPPDGVVVEVEACGVCRSDWHGWQGHDPDVTLPHVPGHEFAGVVVEVGE--DVSRWRV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIePYIN-CRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQ---DKVHPSSKLDFDQLALvetLGIGL---- 152
Cdd:cd08260    79 GDRVTV-PFVLgCGTCPYCRAGDSNVCEHQVQPGFTHPGSFAEYVAVPRadvNLVRLPDDVDFVTAAG---LGCRFataf 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 HA-VNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNL 231
Cdd:cd08260   155 RAlVHQARVKPGEWVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELG-AVATVNASEVEDVAAAVRDLTGGG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 232 PTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGE---VTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINTA 308
Cdd:cd08260   234 AHVSVDALGIPETCRNSVASLRKRGRHVQVGLTLGEeagVALPMDRVVARELEIVGSHGMPAHRYDAMLALIASGKLDPE 313

                         330
                  ....*....|....*..
gi 1243936875 309 PWLTHKTAFETLPEVFP 325
Cdd:cd08260   314 PLVGRTISLDEAPDALA 330
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 22-334 1.06e-41

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


Pssm-ID: 176218 [Multi-domain]  Cd Length: 350  Bit Score: 148.32  E-value: 1.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  22 TIGSDEVLVKIKRIGICGTDYHAFRG---------RQPFFTYPRILGHELGAEVVEIGSYQNTRTLKIGDKVSIEPYINC 92
Cdd:cd08256    21 RPGPGEILVKVEACGICAGDIKCYHGapsfwgdenQPPYVKPPMIPGHEFVGRVVELGEGAEERGVKVGDRVISEQIVPC 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  93 RVCQACKRGLSNCCENLQVLGVH--IDGGMTEYMKLPQD----KVHPSSKLDfdQLALVETLGIGLHAVNRATITQNDIV 166
Cdd:cd08256   101 WNCRFCNRGQYWMCQKHDLYGFQnnVNGGMAEYMRFPKEaivhKVPDDIPPE--DAILIEPLACALHAVDRANIKFDDVV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 167 LIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNLPTVIFDATGNKKSM 245
Cdd:cd08256   179 VLAGAGPLGLGMIGAARLKNPKKLIVlDLKDERLALARKFG-ADVVLNPPEVDVVEKIKELTGGYGCDIYIEATGHPSAV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 246 ETSFSLAAQGAKIIFIGLFQGEVTFeDPSF--HKKEITLMSSRNSlPRDFKQIINLMETGKINTAPWLTHKTAFETLPEV 323
Cdd:cd08256   258 EQGLNMIRKLGRFVEFSVFGDPVTV-DWSIigDRKELDVLGSHLG-PYCYPIAIDLIASGRLPTDGIVTHQFPLEDFEEA 335

                         330
                  ....*....|.
gi 1243936875 324 FPLWLNPEEDV 334
Cdd:cd08256   336 FELMARGDDSI 346
arabinose_DH_like cd05284
D-arabinose dehydrogenase; This group contains arabinose dehydrogenase (AraDH) and related ...
 19-305 1.16e-39

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: 142.70  E-value: 1.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  19 DIITIGSDEVLVKIKRIGICGTDYH----AFRGRQPFfTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRV 94
Cdd:cd05284    19 PVPEPGPGQVLVRVGGAGVCHSDLHvidgVWGGILPY-KLPFTLGHENAGWVEEVGS--GVDGLKEGDPVVVHPPWGCGT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  95 CQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDK-VHPSSKLDFDQLALVETLGI-GLHAVNRA--TITQNDIVLIIG 170
Cdd:cd05284    96 CRYCRRGEENYCENARFPGIGTDGGFAEYLLVPSRRlVKLPRGLDPVEAAPLADAGLtAYHAVKKAlpYLDPGSTVVVIG 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 171 AGPIGLSTAQFAK-LSGAKVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQmLKERLSGNLPTVIFDATGNKKSMETSF 249
Cdd:cd05284   176 VGGLGHIAVQILRaLTPATVIAVDRSEEALKLAERLG-ADHVLNASDDVVEE-VRELTGGRGADAVIDFVGSDETLALAA 253

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1243936875 250 SLAAQGAKIIFIGLFqGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKI 305
Cdd:cd05284   254 KLLAKGGRYVIVGYG-GHGRLPTSDLVPTEISVIGSLWGTRAELVEVVALAESGKV 308
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 25-339 2.01e-39

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 143.06  E-value: 2.01e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  25 SDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVCQACKRGLSN 104
Cdd:cd08283    25 PTDAIVRVTATAICGSDLHLYHGYIPGMKKGDILGHEFMGVVEEVGP--EVRNLKVGDRVVVPFTIACGECFYCKRGLYS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 105 CCEN------LQVLGVH--------------IDGGMTEYMKLPQDKVHP---SSKLDFDQ-LALVETLGIGLHAVNRATI 160
Cdd:cd08283   103 QCDNtnpsaeMAKLYGHagagifgyshltggYAGGQAEYVRVPFADVGPfkiPDDLSDEKaLFLSDILPTGYHAAELAEV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 161 TQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNLAdEVIELND-RLTSQMLKERLSGNLPTVIFDA 238
Cdd:cd08283   183 KPGDTVAVWGCGPVGLFAARSAKLLGAERVIAiDRVPERLEMARSHLGA-ETINFEEvDDVVEALRELTGGRGPDVCIDA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 239 TGnkksMETSFSLAAQ-------------------------GAKIIFIGLFQGEV-TFEDPSFHKKEITLMSSRNSLPRD 292
Cdd:cd08283   262 VG----MEAHGSPLHKaeqallkletdrpdalreaiqavrkGGTVSIIGVYGGTVnKFPIGAAMNKGLTLRMGQTHVQRY 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1243936875 293 FKQIINLMETGKINTAPWLTHKTAFETLPEVFPLWLNPEEDVIKAIV 339
Cdd:cd08283   338 LPRLLELIESGELDPSFIITHRLPLEDAPEAYKIFDKKEDGCIKVVL 384
FrmA COG1062
Zn-dependent alcohol/formaldehyde dehydrogenase [Energy production and conversion];
24-339 2.49e-39

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


Pssm-ID: 440682 [Multi-domain]  Cd Length: 355  Bit Score: 142.14  E-value: 2.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQPFfTYPRILGHELGAEVVEIGSyqNTRTLKIGDKV--SIEPYinCRVCQACKRG 101
Cdd:COG1062    15 RPGEVLVRIVAAGLCHSDLHVRDGDLPV-PLPAVLGHEGAGVVEEVGP--GVTGVAPGDHVvlSFIPS--CGHCRYCASG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 102 LSNCCEN---LQVLGVHIDG-------------------GMTEYMKLPQD---KVHPSskLDFDQLAL----VETlGIGl 152
Cdd:COG1062    90 RPALCEAgaaLNGKGTLPDGtsrlssadgepvghffgqsSFAEYAVVPERsvvKVDKD--VPLELAALlgcgVQT-GAG- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 hAV-NRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLK-------NNLADEVIELndrltsqmL 223
Cdd:COG1062   166 -AVlNTAKVRPGDTVAVFGLGGVGLSAVQGARIAGASRIIAvDPVPEKLELARElgathtvNPADEDAVEA--------V 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 224 KErLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGL--FQGEVTFEDPSFHKKEITLMSSR--NSLPR-DFKQIIN 298
Cdd:COG1062   237 RE-LTGGGVDYAFETTGNPAVIRQALEALRKGGTVVVVGLapPGAEISLDPFQLLLTGRTIRGSYfgGAVPRrDIPRLVD 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1243936875 299 LMETGKINTAPWLTHKTAFETLPEVFPLWLNPEedVIKAIV 339
Cdd:COG1062   316 LYRAGRLPLDELITRRYPLDEINEAFDDLRSGE--VIRPVI 354
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 1-324 3.19e-38

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 139.60  E-value: 3.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPG-TLSHshkEDIITI--GSDEVLVKIKRIGICGTDYHAFRGRQPFfTYPRILGHELGAEVVEIGSyqNTRT 77
Cdd:cd08279     1 MRAAVLHEVGkPLEI---EEVELDdpGPGEVLVRIAAAGLCHSDLHVVTGDLPA-PLPAVLGHEGAGVVEEVGP--GVTG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  78 LKIGDKVSIEPYINCRVCQACKRGLSNCCEN-LQVLGVHIDGGMT-------------------EYM--------KLPQD 129
Cdd:cd08279    75 VKPGDHVVLSWIPACGTCRYCSRGQPNLCDLgAGILGGQLPDGTRrftadgepvgamcglgtfaEYTvvpeasvvKIDDD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 130 kvhpsskLDFDQLALVE---TLGIGlHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLK- 204
Cdd:cd08279   155 -------IPLDRAALLGcgvTTGVG-AVVNTARVRPGDTVAVIGCGGVGLNAIQGARIAGASRIIAvDPVPEKLELARRf 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 205 ------NNLADEVIELNDRLTsqmlkerlSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDP--SFH 276
Cdd:cd08279   227 gathtvNASEDDAVEAVRDLT--------DGRGADYAFEAVGRAATIRQALAMTRKGGTAVVVGMGPPGETVSLPalELF 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1243936875 277 KKEITLMSSR---NSLPRDFKQIINLMETGKINTAPWLTHKTAFETLPEVF 324
Cdd:cd08279   299 LSEKRLQGSLygsANPRRDIPRLLDLYRAGRLKLDELVTRRYSLDEINEAF 349
Zn_ADH10 cd08263
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 1-339 4.86e-38

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


Pssm-ID: 176224 [Multi-domain]  Cd Length: 367  Bit Score: 139.04  E-value: 4.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPfFTYPRILGHELGAEVVEIG-SYQNTRTLK 79
Cdd:cd08263     1 MKAAVLKGPNPPLTIEEIPVPRPKEGEILIRVAACGVCHSDLHVLKGELP-FPPPFVLGHEISGEVVEVGpNVENPYGLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  80 IGDKVSIEPYINCRVCQACKRGLSNCCENL----------------------QVLGVHIDGGMTEYMKLPQDKVHPSSK- 136
Cdd:cd08263    80 VGDRVVGSFIMPCGKCRYCARGKENLCEDFfaynrlkgtlydgttrlfrldgGPVYMYSMGGLAEYAVVPATALAPLPEs 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 137 LDFDQLALVETLGIGLH-AVNRATITQ-NDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNlADEVIE 213
Cdd:cd08263   160 LDYTESAVLGCAGFTAYgALKHAADVRpGETVAVIGVGGVGSSAIQLAKAFGASPIIAvDVRDEKLAKAKELG-ATHTVN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 214 LNDRLTSQMLKERLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDP--SFHKKEITLMSSRNSLPR 291
Cdd:cd08263   239 AAKEDAVAAIREITGGRGVDVVVEALGKPETFKLALDVVRDGGRAVVVGLAPGGATAEIPitRLVRRGIKIIGSYGARPR 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1243936875 292 -DFKQIINLMETGKINTAPWLTHKTAFETLPEVFPLwLNPEEDVIKAIV 339
Cdd:cd08263   319 qDLPELVGLAASGKLDPEALVTHKYKLEEINEAYEN-LRKGLIHGRAIV 366
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 26-324 2.74e-37

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


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 137.65  E-value: 2.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  26 DEVLVKIKRIGICGTDYHAFRGRQ------PFFT-YPRILGHELGAEVVEIGsyQNTRTLKIGDKVSIEPYINCRVCQAC 98
Cdd:cd08265    52 DEILIRVKACGICGSDIHLYETDKdgyilyPGLTeFPVVIGHEFSGVVEKTG--KNVKNFEKGDPVTAEEMMWCGMCRAC 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  99 KRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKV--------HPSSKLDFDQLALVETLGIGLHAV-NRA-TITQNDIVLI 168
Cdd:cd08265   130 RSGSPNHCKNLKELGFSADGAFAEYIAVNARYAweinelreIYSEDKAFEAGALVEPTSVAYNGLfIRGgGFRPGAYVVV 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 169 IGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNlADEVI---ELNDRLTSQMLKERLSGNLPTVIFDATGNKK- 243
Cdd:cd08265   210 YGAGPIGLAAIALAKAAGAsKVIAFEISEERRNLAKEMG-ADYVFnptKMRDCLSGEKVMEVTKGWGADIQVEAAGAPPa 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 244 ---SMETSFSLaaqGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSR-NSLPRDFKQIINLMETGKINTAPWLTHKTAFET 319
Cdd:cd08265   289 tipQMEKSIAI---NGKIVYIGRAATTVPLHLEVLQVRRAQIVGAQgHSGHGIFPSVIKLMASGKIDMTKIITARFPLEG 365


                  ....*
gi 1243936875 320 LPEVF 324
Cdd:cd08265   366 IMEAI 370
PRK13771 PRK13771
putative alcohol dehydrogenase; Provisional
 1-324 5.19e-37

putative alcohol dehydrogenase; Provisional


Pssm-ID: 184316 [Multi-domain]  Cd Length: 334  Bit Score: 135.55  E-value: 5.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:PRK13771    1 MKAVILPGFKQGYRIEEVPDPKPGKDEVVIKVNYAGLCYRDLLQLQGFYPRMKYPVILGHEVVGTVEEVGE--NVKGFKP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDK-VHPSSKLDFDQLALVE-TLGIGLHAVNRA 158
Cdd:PRK13771   79 GDRVASLLYAPDGTCEYCRSGEEAYCKNRLGYGEELDGFFAEYAKVKVTSlVKVPPNVSDEGAVIVPcVTGMVYRGLRRA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 159 TITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKnnLADEVIELNDrlTSQMLKeRLSGnlPTVIFD 237
Cdd:PRK13771  159 GVKKGETVLVTGAgGGVGIHAIQVAKALGAKVIAVTSSESKAKIVSK--YADYVIVGSK--FSEEVK-KIGG--ADIVIE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLaAQGAKIIFIGLFQGEVTFEDP--SFHKKEITLMSSRNSLPRDFKQIINLMETGKINtaPWLTHKT 315
Cdd:PRK13771  232 TVGTPTLEESLRSL-NMGGKIIQIGNVDPSPTYSLRlgYIILKDIEIIGHISATKRDVEEALKLVAEGKIK--PVIGAEV 308


                  ....*....
gi 1243936875 316 AFETLPEVF 324
Cdd:PRK13771  309 SLSEIDKAL 317
MDR_like cd08242
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-318 2.14e-36

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: 133.52  E-value: 2.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLsHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFftyPRILGHELGAEVVEIGsyqnTRTLkI 80
Cdd:cd08242     1 MKALVLDGGLDL-RVEDLPKPEPPPGEALVRVLLAGICNTDLEIYKGYYPF---PGVPGHEFVGIVEEGP----EAEL-V 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVH-IDGGMTEYMKLPQDKVHPSSKLDFDQLA-LVETLGIGLHAVNRA 158
Cdd:cd08242    72 GKRVVGEINIACGRCEYCRRGLYTHCPNRTVLGIVdRDGAFAEYLTLPLENLHVVPDLVPDEQAvFAEPLAAALEILEQV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 159 TITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKNNLADEVIElndrltsqmlkERLSGNLP-TVIFD 237
Cdd:cd08242   152 PITPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSEKLALARRLGVETVLPD-----------EAESEGGGfDVVVE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 238 ATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSlprDFKQIINLMETGKINTAPWLT----- 312
Cdd:cd08242   221 ATGSPSGLELALRLVRPRGTVVLKSTYAGPASFDLTKAVVNEITLVGSRCG---PFAPALRLLRKGLVDVDPLITavypl 297


                  ....*...
gi 1243936875 313 --HKTAFE 318
Cdd:cd08242   298 eeALEAFE 305
Zn_ADH9 cd08269
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 19-339 3.95e-36

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: 132.87  E-value: 3.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  19 DIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRI---LGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYincrvc 95
Cdd:cd08269    13 PRPTPGPGQVLVRVEGCGVCGSDLPAFNQGRPWFVYPAEpggPGHEGWGRVVALGP--GVRGLAVGDRVAGLSG------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  96 qackrglsnccenlqvlgvhidGGMTEYMKLPQDKVHPSSKLDFDQLALVETLGIGLHAVNRATITQNDIVLIIGAGPIG 175
Cdd:cd08269    85 ----------------------GAFAEYDLADADHAVPLPSLLDGQAFPGEPLGCALNVFRRGWIRAGKTVAVIGAGFIG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 176 LSTAQFAKLSGAKVLIAdlnAKRLQFSL---KNNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATGNKKSMETSFSLA 252
Cdd:cd08269   143 LLFLQLAAAAGARRVIA---IDRRPARLalaRELGATEVVTDDSEAIVERVRELTGGAGADVVIEAVGHQWPLDLAGELV 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 253 AQGAKIIFIGLFQGE-VTFEDPSFHKKEITLMSS----RNSLPRDFKQIINLMETGKINTAPWLTHKTAFETLPEVFPLW 327
Cdd:cd08269   220 AERGRLVIFGYHQDGpRPVPFQTWNWKGIDLINAverdPRIGLEGMREAVKLIADGRLDLGSLLTHEFPLEELGDAFEAA 299

                         330
                  ....*....|..
gi 1243936875 328 LNPEEDVIKAIV 339
Cdd:cd08269   300 RRRPDGFIKGVI 311
PRK10309 PRK10309
galactitol-1-phosphate 5-dehydrogenase;
1-322 1.61e-35

galactitol-1-phosphate 5-dehydrogenase;


Pssm-ID: 182371 [Multi-domain]  Cd Length: 347  Bit Score: 131.88  E-value: 1.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDY-HAFRGRQPFftYPRILGHELGAEVVEIGSyqNTRTLK 79
Cdd:PRK10309    1 MKSVVNDTDGIVRVAESPIPEIKHQDDVLVKVASSGLCGSDIpRIFKNGAHY--YPITLGHEFSGYVEAVGS--GVDDLH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  80 IGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYM--------KLPQDkvhpsskLDFDQLALVETLGIG 151
Cdd:PRK10309   77 PGDAVACVPLLPCFTCPECLRGFYSLCAKYDFIGSRRDGGNAEYIvvkrknlfALPTD-------MPIEDGAFIEPITVG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 152 LHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAK-VLIADLNAKRLQFSlKNNLADEVieLNDR-LTSQMLKERLSG 229
Cdd:PRK10309  150 LHAFHLAQGCEGKNVIIIGAGTIGLLAIQCAVALGAKsVTAIDINSEKLALA-KSLGAMQT--FNSReMSAPQIQSVLRE 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 230 N-LPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHK---KEITLMSS--RNSLP---RDFKQIINLM 300
Cdd:PRK10309  227 LrFDQLILETAGVPQTVELAIEIAGPRAQLALVGTLHHDLHLTSATFGKilrKELTVIGSwmNYSSPwpgQEWETASRLL 306

                         330       340
                  ....*....|....*....|..
gi 1243936875 301 ETGKINTAPWLTHKTAFETLPE 322
Cdd:PRK10309  307 TERKLSLEPLIAHRGSFESFAQ 328
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 26-320 3.09e-33

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 125.57  E-value: 3.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  26 DEVLVKIKRIGICGTDYHAFR-GRQPFFT--YPRILGHELGAEVVEigsyQNTRTLKIGDKVSIEPYINCRVCQACKRGL 102
Cdd:PRK09880   28 NGTLVQITRGGICGSDLHYYQeGKVGNFVikAPMVLGHEVIGKIVH----SDSSGLKEGQTVAINPSKPCGHCKYCLSHN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 103 SNCCENLQVLGV-----HIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRATITQNDIVLIIGAGPIGL 176
Cdd:PRK09880  104 ENQCTTMRFFGSamyfpHVDGGFTRYKVVDTAQCIPyPEKADEKVMAFAEPLAVAIHAAHQAGDLQGKRVFVSGVGPIGC 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 177 STAQFAKLSGAKVLI-ADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERlsGNLpTVIFDATGNKKSMETSFSLAAQG 255
Cdd:PRK09880  184 LIVAAVKTLGAAEIVcADVSPRSLSLAREMG-ADKLVNPQNDDLDHYKAEK--GYF-DVSFEVSGHPSSINTCLEVTRAK 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1243936875 256 AKIIFIGLFQGEVTFEDPSFHKKEITLMSS-RnsLPRDFKQIINLMETGKINTAPWLTHKTAFETL 320
Cdd:PRK09880  260 GVMVQVGMGGAPPEFPMMTLIVKEISLKGSfR--FTEEFNTAVSWLANGVINPLPLLSAEYPFTDL 323
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 1-339 3.51e-33

formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase (FDH), which is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. This family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Another member is identified as a dihydroxyacetone reductase. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176246 [Multi-domain]  Cd Length: 345  Bit Score: 125.44  E-value: 3.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08286     1 MKALVYHGPGKISWEDRPKPTIQEPTDAIVKMLKTTICGTDLHILKGDVPTVTPGRILGHEGVGVVEEVGS--AVTNFKV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIEPYINCRVCQACKRGLSNCCENLQ-VLGVHIDGGMTEYMKLP---QDKVHPSSKLDFDQ-LALVETLGIGLH-A 154
Cdd:cd08286    79 GDRVLISCISSCGTCGYCRKGLYSHCESGGwILGNLIDGTQAEYVRIPhadNSLYKLPEGVDEEAaVMLSDILPTGYEcG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 155 VNRATITQNDIVLIIGAGPIGLS---TAQFakLSGAKVLIADLNAKRLQFSLK-------NNLADEVIELNDRLTSQMlk 224
Cdd:cd08286   159 VLNGKVKPGDTVAIVGAGPVGLAallTAQL--YSPSKIIMVDLDDNRLEVAKKlgathtvNSAKGDAIEQVLELTDGR-- 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 225 erlsgNLPTVIfDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEdpsFHKKEI------TLMSSRNSLPRdfkqIIN 298
Cdd:cd08286   235 -----GVDVVI-EAVGIPATFELCQELVAPGGHIANVGVHGKPVDLH---LEKLWIknititTGLVDTNTTPM----LLK 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1243936875 299 LMETGKINTAPWLTHKTAFETLPEVFPLWLN-PEEDVIKAIV 339
Cdd:cd08286   302 LVSSGKLDPSKLVTHRFKLSEIEKAYDTFSAaAKHKALKVII 343
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-324 6.22e-33

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


Pssm-ID: 176257 [Multi-domain]  Cd Length: 341  Bit Score: 124.95  E-value: 6.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKE-DIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFT-YPRILGHElGA-EVVEIGSyqNTRT 77
Cdd:cd08297     1 MKAAVVEEFGEKPYEVKDvPVPEPGPGEVLVKLEASGVCHTDLHAALGDWPVKPkLPLIGGHE-GAgVVVAVGP--GVSG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  78 LKIGDKVSIePYIN--CRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVH--PSSkLDFDQLALVETLGIGLH 153
Cdd:cd08297    78 LKVGDRVGV-KWLYdaCGKCEYCRTGDETLCPNQKNSGYTVDGTFAEYAIADARYVTpiPDG-LSFEQAAPLLCAGVTVY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 154 -AVNRATITQNDIVLIIGA----GPIGLstaQFAKLSGAKVLIADLNAKRLQFSLKnnL-ADEVIELNDRLTSQMLKERL 227
Cdd:cd08297   156 kALKKAGLKPGDWVVISGAggglGHLGV---QYAKAMGLRVIAIDVGDEKLELAKE--LgADAFVDFKKSDDVEAVKELT 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 228 SGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGL-FQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKIN 306
Cdd:cd08297   231 GGGGAHAVVVTAVSAAAYEQALDYLRPGGTLVCVGLpPGGFIPLDPFDLVLRGITIVGSLVGTRQDLQEALEFAARGKVK 310

                         330
                  ....*....|....*...
gi 1243936875 307 TapwLTHKTAFETLPEVF 324
Cdd:cd08297   311 P---HIQVVPLEDLNEVF 325
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 45-339 1.29e-31

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: 119.68  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  45 FRGRQPFFTyPRILGHELGAEVVEIGSyqNTRTLKIGDkvsiepyincRVCqackrglsnccenlqVLGVHidggmTEYM 124
Cdd:cd08255    12 STGTEKLPL-PLPPGYSSVGRVVEVGS--GVTGFKPGD----------RVF---------------CFGPH-----AERV 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 125 KLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFS 202
Cdd:cd08255    59 VVPANLLVPlPDGLPPERAALTALAATALNGVRDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREVVGvDPDAARRELA 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 203 LKNNLADEVielndrltSQMLKERLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITL 282
Cdd:cd08255   139 EALGPADPV--------AADTADEIGGRGADVVIEASGSPSALETALRLLRDRGRVVLVGWYGLKPLLLGEEFHFKRLPI 210

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243936875 283 MSSRNSLP------------RDFKQIINLMETGKIntAPWLTHKTAFETLPEVFPLWLNPEEDVIKAIV 339
Cdd:cd08255   211 RSSQVYGIgrydrprrwteaRNLEEALDLLAEGRL--EALITHRVPFEDAPEAYRLLFEDPPECLKVVL 277
CAD cd08245
Cinnamyl alcohol dehydrogenases (CAD) and related proteins; Cinnamyl alcohol dehydrogenases ...
 24-326 2.24e-31

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


Pssm-ID: 176207 [Multi-domain]  Cd Length: 330  Bit Score: 120.50  E-value: 2.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIePYIN--CRVCQACKRG 101
Cdd:cd08245    23 GPGEVLIKIEACGVCHTDLHAAEGDWGGSKYPLVPGHEIVGEVVEVGA--GVEGRKVGDRVGV-GWLVgsCGRCEYCRRG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 102 LSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSK-LDFDQLALVETLGI-GLHAVNRATITQNDIVLIIGAGPIGLSTA 179
Cdd:cd08245   100 LENLCQKAVNTGYTTQGGYAEYMVADAEYTVLLPDgLPLAQAAPLLCAGItVYSALRDAGPRPGERVAVLGIGGLGHLAV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 180 QFAKLSGAKVLIADLNAKRLQFSLKNNlADEVIelndRLTSQMLKERLSGNLPTVIFDATGNkKSMETSFSLAAQGAKII 259
Cdd:cd08245   180 QYARAMGFETVAITRSPDKRELARKLG-ADEVV----DSGAELDEQAAAGGADVILVTVVSG-AAAEAALGGLRRGGRIV 253

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243936875 260 FIGL-FQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINtaPWLthktafetlpEVFPL 326
Cdd:cd08245   254 LVGLpESPPFSPDIFPLIMKRQSIAGSTHGGRADLQEALDFAAEGKVK--PMI----------ETFPL 309
Zn_ADH_like1 cd08266
Alcohol dehydrogenases of the MDR family; This group contains proteins related to the ...
 22-305 1.05e-30

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


Pssm-ID: 176227 [Multi-domain]  Cd Length: 342  Bit Score: 118.90  E-value: 1.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  22 TIGSDEVLVKIKRIGICGTDYHAFRGrQPF--FTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYINCRVCQACK 99
Cdd:cd08266    24 EPGPDEVLVRVKAAALNHLDLWVRRG-MPGikLPLPHILGSDGAGVVEAVGP--GVTNVKPGQRVVIYPGISCGRCEYCL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 100 RGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSK-LDFDQLALVE-TLGIGLHA-VNRATITQNDIVLIIGAGP-IG 175
Cdd:cd08266   101 AGRENLCAQYGILGEHVDGGYAEYVAVPARNLLPIPDnLSFEEAAAAPlTFLTAWHMlVTRARLRPGETVLVHGAGSgVG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 176 LSTAQFAKLSGAKVLIADLNAKRLQfSLKNNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATGnKKSMETSFSLAAQG 255
Cdd:cd08266   181 SAAIQIAKLFGATVIATAGSEDKLE-RAKELGADYVIDYRKEDFVREVRELTGKRGVDVVVEHVG-AATWEKSLKSLARG 258

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1243936875 256 AKIIFIGLFQG-EVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKI 305
Cdd:cd08266   259 GRLVTCGATTGyEAPIDLRHVFWRQLSILGSTMGTKAELDEALRLVFRGKL 309
FDH_like_ADH3 cd08287
formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol ...
 1-322 2.92e-30

formaldehyde dehydrogenase (FDH)-like; This group contains proteins identified as alcohol dehydrogenases and glutathione-dependant formaldehyde dehydrogenases (FDH) of the zinc-dependent/medium chain alcohol dehydrogenase family. The MDR family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. FDH converts formaldehyde and NAD to formate and NADH. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176247 [Multi-domain]  Cd Length: 345  Bit Score: 117.79  E-value: 2.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFfTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08287     1 MRATVIHGPGDIRVEEVPDPVIEEPTDAVIRVVATCVCGSDLWPYRGVSPT-RAPAPIGHEFVGVVEEVGS--EVTSVKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVsIEPY-INCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQD-----KVHPSSKLDFDQ----LALVETLGI 150
Cdd:cd08287    78 GDFV-IAPFaISDGTCPFCRAGFTTSCVHGGFWGAFVDGGQGEYVRVPLAdgtlvKVPGSPSDDEDLlpslLALSDVMGT 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 151 GLHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-----DLNAKRLQFSlknnlADEVIELNDRLTSQMLKE 225
Cdd:cd08287   157 GHHAAVSAGVRPGSTVVVVGDGAVGLCAVLAAKRLGAERIIAmsrheDRQALAREFG-----ATDIVAERGEEAVARVRE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 226 RLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKI 305
Cdd:cd08287   232 LTGGVGADAVLECVGTQESMEQAIAIARPGGRVGYVGVPHGGVELDVRELFFRNVGLAGGPAPVRRYLPELLDDVLAGRI 311

                         330
                  ....*....|....*..
gi 1243936875 306 NTAPWLTHKTAFETLPE 322
Cdd:cd08287   312 NPGRVFDLTLPLDEVAE 328
PFDH_like cd08282
Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde ...
 1-200 1.96e-28

Pseudomonas putida aldehyde-dismutating formaldehyde dehydrogenase (PFDH); Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. PFDH converts 2 molecules of aldehydes to corresponding carboxylic acid and alcohol. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like the zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these tetrameric FDHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains and a structural zinc in a lobe of the catalytic domain. Unlike ADH, where NAD(P)(H) acts as a cofactor, NADH in FDH is a tightly bound redox cofactor (similar to nicotinamide proteins). The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176242 [Multi-domain]  Cd Length: 375  Bit Score: 113.46  E-value: 1.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLShshKEDI----ITIGSDeVLVKIKRIGICGTDYHAFRGRQPFfTYPRILGHELGAEVVEIGSyqNTR 76
Cdd:cd08282     1 MKAVVYGGPGNVA---VEDVpdpkIEHPTD-AIVRITTTAICGSDLHMYRGRTGA-EPGLVLGHEAMGEVEEVGS--AVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  77 TLKIGDKVSIEPYINCRVCQACKRGLSNCCENLQ----------VLGVHIDGGMTEY----------MKLPQDkvhPSSK 136
Cdd:cd08282    74 SLKVGDRVVVPFNVACGRCRNCKRGLTGVCLTVNpgraggaygyVDMGPYGGGQAEYlrvpyadfnlLKLPDR---DGAK 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243936875 137 LDFDQLALVETLGIGLHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQ 200
Cdd:cd08282   151 EKDDYLMLSDIFPTGWHGLELAGVQPGDTVAVFGAGPVGLMAAYSAILRGAsRVYVVDHVPERLD 215
Zn_ADH_like2 cd08264
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 1-327 3.90e-28

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenases of the medium chain dehydrogenase family. However, this subgroup does not contain the characteristic catalytic zinc site. Also, it contains an atypical structural zinc-binding pattern: DxxCxxCxxxxxxxC. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176225 [Multi-domain]  Cd Length: 325  Bit Score: 111.67  E-value: 3.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGtLSHSHKEDIIT--IGSDEVLVKIKRIGICGTDYHAFRGRqPFFTYPRILGHELGAEVVEIGSYqnTRTL 78
Cdd:cd08264     1 MKALVFEKSG-IENLKVEDVKDpkPGPGEVLIRVKMAGVNPVDYNVINAV-KVKPMPHIPGAEFAGVVEEVGDH--VKGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  79 KIGDKVSIEPYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSKLDFDQLAlvETLGIG----LHA 154
Cdd:cd08264    77 KKGDRVVVYNRVFDGTCDMCLSGNEMLCRNGGIIGVVSNGGYAEYIVVPEKNLFKIPDSISDELA--ASLPVAaltaYHA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 155 VNRATITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVlIAdlnakrlqFSLKNNL----ADEVIELNDRLTSQMLKERLSg 229
Cdd:cd08264   155 LKTAGLGPGETVVVFGAsGNTGIFAVQLAKMMGAEV-IA--------VSRKDWLkefgADEVVDYDEVEEKVKEITKMA- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 230 nlpTVIFDATGNkKSMETSFSLAAQGAKIIFIGLFQG-EVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMETGKINta 308
Cdd:cd08264   225 ---DVVINSLGS-SFWDLSLSVLGRGGRLVTFGTLTGgEVKLDLSDLYSKQISIIGSTGGTRKELLELVKIAKDLKVK-- 298

                         330
                  ....*....|....*....
gi 1243936875 309 pwlTHKTafetlpevFPLW 327
Cdd:cd08264   299 ---VWKT--------FKLE 306
CAD2 cd08298
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 1-204 3.99e-28

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


Pssm-ID: 176258 [Multi-domain]  Cd Length: 329  Bit Score: 111.51  E-value: 3.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSH---SHKE-DIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTR 76
Cdd:cd08298     1 MKAMVLEKPGPIEEnplRLTEvPVPEPGPGEVLIKVEACGVCRTDLHIVEGDLPPPKLPLIPGHEIVGRVEAVGP--GVT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  77 TLKIGDKVSIEP-YINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDKVHPSSKlDFDQLALVETL--G-IGL 152
Cdd:cd08298    79 RFSVGDRVGVPWlGSTCGECRYCRSGRENLCDNARFTGYTVDGGYAEYMVADERFAYPIPE-DYDDEEAAPLLcaGiIGY 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1243936875 153 HAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLK 204
Cdd:cd08298   158 RALKLAGLKPGQRLGLYGFGASAHLALQIARYQGAEVFAFTRSGEHQELARE 209
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 1-341 9.29e-27

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: 107.54  E-value: 9.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDII--TIGSDEVLVKIKRIGICGTDYHAFRGRQPF-FTYPRILGHELGAEVVEIGSyqNTRT 77
Cdd:COG0604     1 MKAIVITEFGGPEVLELEEVPvpEPGPGEVLVRVKAAGVNPADLLIRRGLYPLpPGLPFIPGSDAAGVVVAVGE--GVTG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  78 LKIGDKVsiepyincrvcqackrglsnccenlqvLGVHIDGGMTEYMKLPQDKVH--PSSkLDFDQLA-LVETLGIGLHA 154
Cdd:COG0604    79 FKVGDRV---------------------------AGLGRGGGYAEYVVVPADQLVplPDG-LSFEEAAaLPLAGLTAWQA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 155 VN-RATITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVLIADLNAKRLQFsLKNNLADEVIELND-RLTSQmLKERLSGNL 231
Cdd:COG0604   131 LFdRGRLKPGETVLVHGAaGGVGSAAVQLAKALGARVIATASSPEKAEL-LRALGADHVIDYREeDFAER-VRALTGGRG 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 232 PTVIFDATGnKKSMETSFSLAAQGAKIIFIGLFQGEVT-FEDPSFHKKEITLMSS------RNSLPRDFKQIINLMETGK 304
Cdd:COG0604   209 VDVVLDTVG-GDTLARSLRALAPGGRLVSIGAASGAPPpLDLAPLLLKGLTLTGFtlfardPAERRAALAELARLLAAGK 287

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1243936875 305 INTapwlthktafeTLPEVFPLwlnpeEDVIKAIVYL 341
Cdd:COG0604   288 LRP-----------VIDRVFPL-----EEAAEAHRLL 308
benzyl_alcohol_DH cd08278
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ...
 18-271 3.14e-25

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: 104.12  E-value: 3.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  18 EDII--TIGSDEVLVKIKRIGICGTDYHaFRGRQPFFTYPRILGHElGAEVVE-IGSyqNTRTLKIGDKVsIEPYINCRV 94
Cdd:cd08278    18 EDVEldDPRPDEVLVRIVATGICHTDLV-VRDGGLPTPLPAVLGHE-GAGVVEaVGS--AVTGLKPGDHV-VLSFASCGE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  95 CQACKRGLSNCCENLQVL---GVHIDGGmTEYMKLPQDKVHP-----SS-------------KLDFDQ-LALVETLGIGL 152
Cdd:cd08278    93 CANCLSGHPAYCENFFPLnfsGRRPDGS-TPLSLDDGTPVHGhffgqSSfatyavvhernvvKVDKDVpLELLAPLGCGI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 H----AV-NRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKnnL-ADEVIELNDRLTSQMLKE 225
Cdd:cd08278   172 QtgagAVlNVLKPRPGSSIAVFGAGAVGLAAVMAAKIAGCTTIIAvDIVDSRLELAKE--LgATHVINPKEEDLVAAIRE 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1243936875 226 rLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGL--FQGEVTFE 271
Cdd:cd08278   250 -ITGGGVDYALDTTGVPAVIEQAVDALAPRGTLALVGAppPGAEVTLD 296
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 1-339 7.88e-25

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: 103.09  E-value: 7.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEdIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKI 80
Cdd:cd08285     1 MKAFAMLGIGKVGWIEKP-IPVCGPNDAIVRPTAVAPCTSDVHTVWGGAPGERHGMILGHEAVGVVEEVGS--EVKDFKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  81 GDKVSIePYIN-CRVCQACKRG-LSNCCENLQ--VLGVHIDGGMTEYMKLPQDKVH----PSSKLDFDQLALVETLGIGL 152
Cdd:cd08285    78 GDRVIV-PAITpDWRSVAAQRGyPSQSGGMLGgwKFSNFKDGVFAEYFHVNDADANlaplPDGLTDEQAVMLPDMMSTGF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 HAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNlADEVIEL-NDRLTSQMLkeRLSGN 230
Cdd:cd08285   157 HGAELANIKLGDTVAVFGIGPVGLMAVAGARLRGAGRIIAvGSRPNRVELAKEYG-ATDIVDYkNGDVVEQIL--KLTGG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 231 LPT-VIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSF-------HKKEITLMSSRNSLpRdFKQIINLMET 302
Cdd:cd08285   234 KGVdAVIIAGGGQDTFEQALKVLKPGGTISNVNYYGEDDYLPIPREewgvgmgHKTINGGLCPGGRL-R-MERLASLIEY 311

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1243936875 303 GKINTAPWLTHKT-AFETLPEVFPLWLNPEEDVIKAIV 339
Cdd:cd08285   312 GRVDPSKLLTHHFfGFDDIEEALMLMKDKPDDLIKPVI 349
CAD_like cd08296
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 24-270 7.92e-25

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


Pssm-ID: 176256 [Multi-domain]  Cd Length: 333  Bit Score: 102.71  E-value: 7.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIePYI--NCRVCQACKRG 101
Cdd:cd08296    24 GPGEVLIKVEACGVCHSDAFVKEGAMPGLSYPRVPGHEVVGRIDAVGE--GVSRWKVGDRVGV-GWHggHCGTCDACRRG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 102 LSNCCENLQVLGVHIDGGMTEYMKLPQDK-VHPSSKLDFDQLALVETLGIG-LHAVNRATITQNDIVLIIGAGPIGLSTA 179
Cdd:cd08296   101 DFVHCENGKVTGVTRDGGYAEYMLAPAEAlARIPDDLDAAEAAPLLCAGVTtFNALRNSGAKPGDLVAVQGIGGLGHLAV 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 180 QFAKLSGAKVL-IADLNAKRlQFSLKnnL-ADEVIELNDRLTSQMLKErLSGnlPTVIFDATGNKKSM-ETSFSLAAQGa 256
Cdd:cd08296   181 QYAAKMGFRTVaISRGSDKA-DLARK--LgAHHYIDTSKEDVAEALQE-LGG--AKLILATAPNAKAIsALVGGLAPRG- 253

                         250
                  ....*....|....
gi 1243936875 257 KIIFIGLFQGEVTF 270
Cdd:cd08296   254 KLLILGAAGEPVAV 267
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
173-302 9.97e-23

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 91.90  E-value: 9.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 173 PIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNLPTVIFDATGNKKSMETSFSLA 252
Cdd:pfam00107   1 GVGLAAIQLAKAAGAKVIAVDGSEEKLELAKELG-ADHVINPKETDLVEEIKELTGGKGVDVVFDCVGSPATLEQALKLL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1243936875 253 AQGAKIIFIGLFQGEVTFEDPSFHKKEITLMSSRNSLPRDFKQIINLMET 302
Cdd:pfam00107  80 RPGGRVVVVGLPGGPLPLPLAPLLLKELTILGSFLGSPEEFPEALDLLAS 129
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 24-339 1.71e-22

Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 96.74  E-value: 1.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQPFfTYPRILGHElGAEVVE-IGsyQNTRTLKIGDKV--SIEPYinCRVCQACKR 100
Cdd:cd05279    24 KAGEVRIKVVATGVCHTDLHVIDGKLPT-PLPVILGHE-GAGIVEsIG--PGVTTLKPGDKVipLFGPQ--CGKCKQCLN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 101 GLSNCCENLQVL---GVHIDG------------------GMTEYMKLPQDKVhpsSKLD----FDQLALVE---TLGIGl 152
Cdd:cd05279    98 PRPNLCSKSRGTngrGLMSDGtsrftckgkpihhflgtsTFAEYTVVSEISL---AKIDpdapLEKVCLIGcgfSTGYG- 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 HAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSlKNNLADEVIELNDRLT--SQMLKErLSG 229
Cdd:cd05279   174 AAVNTAKVTPGSTCAVFGLGGVGLSVIMGCKAAGASRIIAvDINKDKFEKA-KQLGATECINPRDQDKpiVEVLTE-MTD 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 230 NLPTVIFDATGNKKSMETSF-SLAAQGAKIIFIGLFQG--EVTFeDPSFHKKEITLMSS---RNSLPRDFKQIINLMETG 303
Cdd:cd05279   252 GGVDYAFEVIGSADTLKQALdATRLGGGTSVVVGVPPSgtEATL-DPNDLLTGRTIKGTvfgGWKSKDSVPKLVALYRQK 330

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1243936875 304 KINTAPWLTHKTAFETLPEVFPLWLNPEedVIKAIV 339
Cdd:cd05279   331 KFPLDELITHVLPFEEINDGFDLMRSGE--SIRTIL 364
liver_ADH_like1 cd08281
Zinc-dependent alcohol dehydrogenases (ADH) and class III ADG (AKA formaldehyde dehydrogenase); ...
 1-324 2.15e-22

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: 96.29  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGtLSHSHKE----DIITI-----GSDEVLVKIKRIGICGTDYHAFRGRQPFFTyPRILGHELGAEVVEIGs 71
Cdd:cd08281     1 MRAAVLRETG-APTPYADsrplVIEEVeldppGPGEVLVKIAAAGLCHSDLSVINGDRPRPL-PMALGHEAAGVVVEVG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  72 yQNTRTLKIGDKVSIEPYINCRVCQACKRGLSNCCE---NLQVLGVHIDGGM------------------TEYMKLPQDK 130
Cdd:cd08281    78 -EGVTDLEVGDHVVLVFVPSCGHCRPCAEGRPALCEpgaAANGAGTLLSGGRrlrlrggeinhhlgvsafAEYAVVSRRS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 131 VHPSSK-LDFDQLAL----VETlGIGlHAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQfsLK 204
Cdd:cd08281   157 VVKIDKdVPLEIAALfgcaVLT-GVG-AVVNTAGVRPGQSVAVVGLGGVGLSALLGAVAAGASQVVAvDLNEDKLA--LA 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 205 NNL-ADEVIELNDRLTSQMLKERLSGNLpTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDP--SFHKKEIT 281
Cdd:cd08281   233 RELgATATVNAGDPNAVEQVRELTGGGV-DYAFEMAGSVPALETAYEITRRGGTTVTAGLPDPEARLSVPalSLVAEERT 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1243936875 282 LMSSR--NSLP-RDFKQIINLMETGKINTAPWLTHKTAFETLPEVF 324
Cdd:cd08281   312 LKGSYmgSCVPrRDIPRYLALYLSGRLPVDKLLTHRLPLDEINEGF 357
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 24-331 1.07e-21

Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 94.33  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRqPFFTYPRILGHElGAEVVE-IGsyQNTRTLKIGDKVsIEPYI-NCRVCQACKRG 101
Cdd:cd08277    26 KANEVRIKMLATSVCHTDILAIEGF-KATLFPVILGHE-GAGIVEsVG--EGVTNLKPGDKV-IPLFIgQCGECSNCRSG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 102 LSNCCENLQVL--GVHIDG------------------GMTEYMKLPQD---KVHPSSKLDfdqlaLVETLGIGLH----- 153
Cdd:cd08277   101 KTNLCQKYRANesGLMPDGtsrftckgkkiyhflgtsTFSQYTVVDENyvaKIDPAAPLE-----HVCLLGCGFStgyga 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 154 AVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNlADEVIELND--RLTSQMLKErLSGN 230
Cdd:cd08277   176 AWNTAKVEPGSTVAVFGLGAVGLSAIMGAKIAGASRIIGvDINEDKFEKAKEFG-ATDFINPKDsdKPVSEVIRE-MTGG 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 231 LPTVIFDATGNKKSMETSFSLAAQG-AKIIFIGLFQGEVTFEDPSFHKKEITL-------MSSRNSLPRdfkqIINLMET 302
Cdd:cd08277   254 GVDYSFECTGNADLMNEALESTKLGwGVSVVVGVPPGAELSIRPFQLILGRTWkgsffggFKSRSDVPK----LVSKYMN 329

                         330       340
                  ....*....|....*....|....*....
gi 1243936875 303 GKINTAPWLTHKTAFETLPEVFPLWLNPE 331
Cdd:cd08277   330 KKFDLDELITHVLPFEEINKGFDLMKSGE 358
enoyl_reductase_like cd08249
enoyl_reductase_like; Member identified as possible enoyl reductase of the MDR family. 2-enoyl ...
 1-322 3.11e-20

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


Pssm-ID: 176211 [Multi-domain]  Cd Length: 339  Bit Score: 89.95  E-value: 3.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKE-DIITIGSDEVLVKIKRIGICGTDY-HAFRGRQPffTYPRILGHELGAEVVEIGSyqNTRTL 78
Cdd:cd08249     1 QKAAVLTGPGGGLLVVVDvPVPKPGPDEVLVKVKAVALNPVDWkHQDYGFIP--SYPAILGCDFAGTVVEVGS--GVTRF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  79 KIGDkvsiepyincRVCQACKRGLSNCCENlqvlgvhidGGMTEYMKLPQD---KVhPSSkLDFDQ------------LA 143
Cdd:cd08249    77 KVGD----------RVAGFVHGGNPNDPRN---------GAFQEYVVADADltaKI-PDN-ISFEEaatlpvglvtaaLA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 144 LVETLGIGLHAVNRATITQNDIVLIIGAG-PIGLSTAQFAKLSGAKVL-IADlnAKRLQFsLKNNLADEVIELNDRLTSQ 221
Cdd:cd08249   136 LFQKLGLPLPPPKPSPASKGKPVLIWGGSsSVGTLAIQLAKLAGYKVItTAS--PKNFDL-VKSLGADAVFDYHDPDVVE 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 222 MLKERLSGNLPTViFDATGNKKSMETSFSLAAQGAKIIFIGL-FQGEVTFEDPSFHKKEITLMSSRNSLPRD-------F 293
Cdd:cd08249   213 DIRAATGGKLRYA-LDCISTPESAQLCAEALGRSGGGKLVSLlPVPEETEPRKGVKVKFVLGYTVFGEIPEDrefgevfW 291

                         330       340
                  ....*....|....*....|....*....
gi 1243936875 294 KQIINLMETGKINTAPWLTHKTAFETLPE 322
Cdd:cd08249   292 KYLPELLEEGKLKPHPVRVVEGGLEGVQE 320
alcohol_DH_plants cd08301
Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 27-326 4.27e-20

Plant alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176261 [Multi-domain]  Cd Length: 369  Bit Score: 90.05  E-value: 4.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  27 EVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHElGAEVVE-IGsyQNTRTLKIGDKVsIEPYI-NCRVCQACKRGLSN 104
Cdd:cd08301    29 EVRIKILHTSLCHTDVYFWEAKGQTPLFPRILGHE-AAGIVEsVG--EGVTDLKPGDHV-LPVFTgECKECRHCKSEKSN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 105 CCENLQV---LGVHIDGGMTEYMKLPQD----------------------KVHPSSKLdfDQLALVE---TLGIGLhAVN 156
Cdd:cd08301   105 MCDLLRIntdRGVMINDGKSRFSINGKPiyhfvgtstfseytvvhvgcvaKINPEAPL--DKVCLLScgvSTGLGA-AWN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 157 RATITQNDIVLIIGAGPIGLSTAQFAKLSGA-KVLIADLNAKRLQFSLKNNLADEV-IELNDRLTSQMLKERLSGNLPTV 234
Cdd:cd08301   182 VAKVKKGSTVAIFGLGAVGLAVAEGARIRGAsRIIGVDLNPSKFEQAKKFGVTEFVnPKDHDKPVQEVIAEMTGGGVDYS 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 235 iFDATGNKKSMETSFSLAAQG-AKIIFIGLFQGEVTFedpSFHKKEI----TLMSS-------RNSLPRDFKQIINlmet 302
Cdd:cd08301   262 -FECTGNIDAMISAFECVHDGwGVTVLLGVPHKDAVF---STHPMNLlngrTLKGTlfggykpKTDLPNLVEKYMK---- 333

                         330       340
                  ....*....|....*....|....
gi 1243936875 303 GKINTAPWLTHKTAFETLPEVFPL 326
Cdd:cd08301   334 KELELEKFITHELPFSEINKAFDL 357
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 27-245 3.09e-19

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 87.28  E-value: 3.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  27 EVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGsyQNTRTLKIGDKVsIEPYI-NCRVCQACKRGLSNC 105
Cdd:cd08300    29 EVRIKILATGVCHTDAYTLSGADPEGLFPVILGHEGAGIVESVG--EGVTSVKPGDHV-IPLYTpECGECKFCKSGKTNL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 106 CENL---QVLGVHIDG------------------GMTEYMKLPQ---DKVHPSSklDFDQLAL----VETlGIGLhAVNR 157
Cdd:cd08300   106 CQKIratQGKGLMPDGtsrfsckgkpiyhfmgtsTFSEYTVVAEisvAKINPEA--PLDKVCLlgcgVTT-GYGA-VLNT 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 158 ATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRlqFSLKNNL-ADEVIELND--RLTSQMLKERLSGNLpT 233
Cdd:cd08300   182 AKVEPGSTVAVFGLGAVGLAVIQGAKAAGASRIIGiDINPDK--FELAKKFgATDCVNPKDhdKPIQQVLVEMTDGGV-D 258

                         250
                  ....*....|..
gi 1243936875 234 VIFDATGNKKSM 245
Cdd:cd08300   259 YTFECIGNVKVM 270
MDR_like_2 cd05289
alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases; ...
 1-341 4.36e-19

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


Pssm-ID: 176191 [Multi-domain]  Cd Length: 309  Bit Score: 86.08  E-value: 4.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDI--ITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTY---PRILGHELGAEVVEIGSyqNT 75
Cdd:cd05289     1 MKAVRIHEYGGPEVLELADVptPEPGPGEVLVKVHAAGVNPVDLKIREGLLKAAFPltlPLIPGHDVAGVVVAVGP--GV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  76 RTLKIGDKVsiepyincrvcqackrglsnccenLQVLGVHIDGGMTEYMKLPQDKVH--PSSkLDFDQLALVETLGI--- 150
Cdd:cd05289    79 TGFKVGDEV------------------------FGMTPFTRGGAYAEYVVVPADELAlkPAN-LSFEEAAALPLAGLtaw 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 151 -GLHAVnrATITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVlIADLNAKRLQFsLKNNLADEVIElndrLTSQMLKERLS 228
Cdd:cd05289   134 qALFEL--GGLKAGQTVLIHGAaGGVGSFAVQLAKARGARV-IATASAANADF-LRSLGADEVID----YTKGDFERAAA 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 229 GNLPTVIFDATGNkKSMETSFSLAAQGAKIIFI-GLFQGEVTFEDPSFHKKEITLMSSRnslpRDFKQIINLMETGKINT 307
Cdd:cd05289   206 PGGVDAVLDTVGG-ETLARSLALVKPGGRLVSIaGPPPAEQAAKRRGVRAGFVFVEPDG----EQLAELAELVEAGKLRP 280

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1243936875 308 apwlthktafeTLPEVFPLwlnpeEDVIKAIVYL 341
Cdd:cd05289   281 -----------VVDRVFPL-----EDAAEAHERL 298
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 23-263 4.75e-19

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


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 86.40  E-value: 4.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  23 IGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYIN-CRVCQACKRG 101
Cdd:cd05283    22 LGPDDVDIKITYCGVCHSDLHTLRNEWGPTKYPLVPGHEIVGIVVAVGS--KVTKFKVGDRVGVGCQVDsCGTCEQCKSG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 102 LSNCCENLQVL--GVHID-----GGMTEYMKLPQDKVHP-SSKLDFDQLA-LvetL--GIGLHA-VNRATITQNDIVLII 169
Cdd:cd05283   100 EEQYCPKGVVTynGKYPDgtitqGGYADHIVVDERFVFKiPEGLDSAAAApL---LcaGITVYSpLKRNGVGPGKRVGVV 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 170 GAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKnNLADEVIELNDrlTSQMLKERLSGNLptvIFDATGNKKSMETSF 249
Cdd:cd05283   177 GIGGLGHLAVKFAKALGAEVTAFSRSPSKKEDALK-LGADEFIATKD--PEAMKKAAGSLDL---IIDTVSASHDLDPYL 250

                         250
                  ....*....|....
gi 1243936875 250 SLAAQGAKIIFIGL 263
Cdd:cd05283   251 SLLKPGGTLVLVGA 264
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 1-339 4.66e-18

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: 83.81  E-value: 4.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGRqpfFTYPR------ILGHELGAEVVEIGSyqn 74
Cdd:cd08230     1 MKAIAVKPGKPGVRVVDIPEPEPTPGEVLVRTLEVGVCGTDREIVAGE---YGTAPpgedflVLGHEALGVVEEVGD--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  75 TRTLKIGDKVSiePYI--NCRVCQACKRGLSNCCENLQVL--GVH-IDGGMTEYMKLPQD---KVHPSSKldfdQLA-LV 145
Cdd:cd08230    75 GSGLSPGDLVV--PTVrrPPGKCLNCRIGRPDFCETGEYTerGIKgLHGFMREYFVDDPEylvKVPPSLA----DVGvLL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 146 ETLGI---GLH---AVNRATITQN-DIVLIIGAGPIGLSTAQFAKLSGAKVLIADlnaKRLQFSLKNNLADE--VIELND 216
Cdd:cd08230   149 EPLSVvekAIEqaeAVQKRLPTWNpRRALVLGAGPIGLLAALLLRLRGFEVYVLN---RRDPPDPKADIVEElgATYVNS 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 217 RLTsqMLKERLSGNLPTVIFDATGNKKSMETSFSLAAQGAKIIFIGLFQGEVTFEDP--SFHK----KEITLMSSRNSLP 290
Cdd:cd08230   226 SKT--PVAEVKLVGEFDLIIEATGVPPLAFEALPALAPNGVVILFGVPGGGREFEVDggELNRdlvlGNKALVGSVNANK 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1243936875 291 RDFKQIINLMETGKINTAPWL----THKTAFETLPEVFplwLNPEEDVIKAIV 339
Cdd:cd08230   304 RHFEQAVEDLAQWKYRWPGVLerliTRRVPLEEFAEAL---TEKPDGEIKVVI 353
PRK09422 PRK09422
ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional
 1-212 5.85e-18

ethanol-active dehydrogenase/acetaldehyde-active reductase; Provisional


Pssm-ID: 181842 [Multi-domain]  Cd Length: 338  Bit Score: 83.54  E-value: 5.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITIGSDEVLVKIKRIGICGTDYHAFRGrqPFFTYP-RILGHELGAEVVEIGSyqNTRTLK 79
Cdd:PRK09422    1 MKAAVVNKDHTGDVVVEKTLRPLKHGEALVKMEYCGVCHTDLHVANG--DFGDKTgRILGHEGIGIVKEVGP--GVTSLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  80 IGDKVSIE-PYINCRVCQACKRGLSNCCENLQVLGVHIDGGMTEY--------MKLPQDkvhpsskLDFDQLALVETLGI 150
Cdd:PRK09422   77 VGDRVSIAwFFEGCGHCEYCTTGRETLCRSVKNAGYTVDGGMAEQcivtadyaVKVPEG-------LDPAQASSITCAGV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243936875 151 GLH-AVNRATITQNDIVLIIGAGPIGLSTAQFAK-LSGAKVLIADLNAKRLQFSlKNNLADEVI 212
Cdd:PRK09422  150 TTYkAIKVSGIKPGQWIAIYGAGGLGNLALQYAKnVFNAKVIAVDINDDKLALA-KEVGADLTI 212
quinone_oxidoreductase_like_1 cd08243
Quinone oxidoreductase (QOR); NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 1-272 5.12e-17

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


Pssm-ID: 176205 [Multi-domain]  Cd Length: 320  Bit Score: 80.35  E-value: 5.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDI--ITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqntRTL 78
Cdd:cd08243     1 MKAIVIEQPGGPEVLKLREIpiPEPKPGWVLIRVKAFGLNRSEIFTRQGHSPSVKFPRVLGIEAVGEVEEAPG----GTF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  79 KIGDKVSiepyincrvcqACKRGLsnccenlqvlGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQL-ALVETLGIGLHAVN 156
Cdd:cd08243    77 TPGQRVA-----------TAMGGM----------GRTFDGSYAEYTLVPNEQVYAiDSDLSWAELaALPETYYTAWGSLF 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 157 RA-TITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVLIADLNAKRlQFSLKNNLADEVIeLNDRLTSQMLKERLSGnlptv 234
Cdd:cd08243   136 RSlGLQPGDTLLIRGGtSSVGLAALKLAKALGATVTATTRSPER-AALLKELGADEVV-IDDGAIAEQLRAAPGG----- 208

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1243936875 235 iFDA----TGNkKSMETSFSLAAQGAKIIFIGLFQGEVTFED 272
Cdd:cd08243   209 -FDKvlelVGT-ATLKDSLRHLRPGGIVCMTGLLGGQWTLED 248
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 22-341 7.35e-17

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


Pssm-ID: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 79.95  E-value: 7.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  22 TIGSDEVLVKIKRIGICGTDYHAFRGRQPFFT---YPRILGHELGAEVVEIGSyqNTRTLKIGDKVsiepyincrvcqac 98
Cdd:cd08267    23 TPKPGEVLVKVHAASVNPVDWKLRRGPPKLLLgrpFPPIPGMDFAGEVVAVGS--GVTRFKVGDEV-------------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  99 krglsnccenLQVLGVHIDGGMTEYMKLPQDKV-HPSSKLDFDQLALVETLGI-GLHAV-NRATITQNDIVLIIGA-GPI 174
Cdd:cd08267    87 ----------FGRLPPKGGGALAEYVVAPESGLaKKPEGVSFEEAAALPVAGLtALQALrDAGKVKPGQRVLINGAsGGV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 175 GLSTAQFAKLSGAKVlIADLNAKRLQF--SLKnnlADEVIelnDRLTSQMLKERLSGNLPTVIFDATGNKK-SMETSFSL 251
Cdd:cd08267   157 GTFAVQIAKALGAHV-TGVCSTRNAELvrSLG---ADEVI---DYTTEDFVALTAGGEKYDVIFDAVGNSPfSLYRASLA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 252 AAQGAKIIFIGL---FQGEVTFEDPSFH---KKEITLMSSRNSlPRDFKQIINLMETGKIntapwlthKTAFEtlpEVFP 325
Cdd:cd08267   230 LKPGGRYVSVGGgpsGLLLVLLLLPLTLgggGRRLKFFLAKPN-AEDLEQLAELVEEGKL--------KPVID---SVYP 297

                         330
                  ....*....|....*.
gi 1243936875 326 LwlnpeEDVIKAIVYL 341
Cdd:cd08267   298 L-----EDAPEAYRRL 308
zeta_crystallin cd08253
Zeta-crystallin with NADP-dependent quinone reductase activity (QOR); Zeta-crystallin is a eye ...
 1-326 8.62e-17

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


Pssm-ID: 176215 [Multi-domain]  Cd Length: 325  Bit Score: 79.94  E-value: 8.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPG---TLSHSHKEDIiTIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVE-IGSyqNTR 76
Cdd:cd08253     1 MRAIRYHEFGapdVLRLGDLPVP-TPGPGEVLVRVHASGVNPVDTYIRAGAYPGLPPLPYVPGSDGAGVVEaVGE--GVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  77 TLKIGDKVsiepyincrvcqackrglsnCCENLQVLGVHidGGMTEYMKLPQDKVHP-SSKLDFDQLAlveTLGI-GLHA 154
Cdd:cd08253    78 GLKVGDRV--------------------WLTNLGWGRRQ--GTAAEYVVVPADQLVPlPDGVSFEQGA---ALGIpALTA 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 155 ----VNRATITQNDIVLIIG-AGPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSG 229
Cdd:cd08253   133 yralFHRAGAKAGETVLVHGgSGAVGHAAVQLARWAGARVIATASSAEGAELVRQAG-ADAVFNYRAEDLADRILAATAG 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 230 NLPTVIFDATGNkKSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSFHKKEITLM------SSRNSLPRDFKQIINLMETG 303
Cdd:cd08253   212 QGVDVIIEVLAN-VNLAKDLDVLAPGGRIVVYGSGGLRGTIPINPLMAKEASIRgvllytATPEERAAAAEAIAAGLADG 290

                         330       340
                  ....*....|....*....|...
gi 1243936875 304 kintapWLTHKTAfetlpEVFPL 326
Cdd:cd08253   291 ------ALRPVIA-----REYPL 302
QOR1 cd08241
Quinone oxidoreductase (QOR); QOR catalyzes the conversion of a quinone + NAD(P)H to a ...
 1-262 1.03e-15

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


Pssm-ID: 176203 [Multi-domain]  Cd Length: 323  Bit Score: 76.77  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDIITI--GSDEVLVKIKRIGICGTDYHAFRGR-Q-----PFftyprILGHELGAEVVEIGSy 72
Cdd:cd08241     1 MKAVVCKELGGPEDLVLEEVPPEpgAPGEVRIRVEAAGVNFPDLLMIQGKyQvkpplPF-----VPGSEVAGVVEAVGE- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  73 qNTRTLKIGDKVsiepyincrvcqackrglsnccenlqvLGVHIDGGMTEYMKLPQDKVHPS-SKLDFDQ-LALVETLGI 150
Cdd:cd08241    75 -GVTGFKVGDRV---------------------------VALTGQGGFAEEVVVPAAAVFPLpDGLSFEEaAALPVTYGT 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 151 GLHA-VNRATITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVLIADLNAKRLQFsLKNNLADEVIELNDRLTSQMLKERLS 228
Cdd:cd08241   127 AYHAlVRRARLQPGETVLVLGAaGGVGLAAVQLAKALGARVIAAASSEEKLAL-ARALGADHVIDYRDPDLRERVKALTG 205

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1243936875 229 GNLPTVIFDATGNKKSmETSFSLAAQGAKIIFIG 262
Cdd:cd08241   206 GRGVDVVYDPVGGDVF-EASLRSLAWGGRLLVIG 238
MDR7 cd08276
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-191 2.79e-14

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


Pssm-ID: 176237 [Multi-domain]  Cd Length: 336  Bit Score: 72.57  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSH--SHKEDIITIGSDEVLVKIK------RigicgtDYHAFRGRQPF-FTYPRILGHELGAEVVEIGS 71
Cdd:cd08276     1 MKAWRLSGGGGLDNlkLVEEPVPEPGPGEVLVRVHavslnyR------DLLILNGRYPPpVKDPLIPLSDGAGEVVAVGE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  72 yQNTRtLKIGDKVSiePYINcrvcQACKRGLSNCCENLQVLGVHIDGGMTEYMKLPQDK-VHPSSKLDFDQLAlveTLGI 150
Cdd:cd08276    75 -GVTR-FKVGDRVV--PTFF----PNWLDGPPTAEDEASALGGPIDGVLAEYVVLPEEGlVRAPDHLSFEEAA---TLPC 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1243936875 151 -GLHA----VNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLI 191
Cdd:cd08276   144 aGLTAwnalFGLGPLKPGDTVLVQGTGGVSLFALQFAKAAGARVIA 189
PLN02740 PLN02740
Alcohol dehydrogenase-like
 27-326 4.95e-14

Alcohol dehydrogenase-like


Pssm-ID: 178341 [Multi-domain]  Cd Length: 381  Bit Score: 72.14  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  27 EVLVKIKRIGICGTDYHAFRGR-QPFFTYPRILGHELGAEVVEIGsyQNTRTLKIGDKVSiePYIN--CRVCQACKRGLS 103
Cdd:PLN02740   37 EVRIKILYTSICHTDLSAWKGEnEAQRAYPRILGHEAAGIVESVG--EGVEDLKAGDHVI--PIFNgeCGDCRYCKRDKT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 104 NCCENLQV-----LGVHiDGG--------------------MTEYMKLPQD---KVHPSSKLdfDQLALVE---TLGIGL 152
Cdd:PLN02740  113 NLCETYRVdpfksVMVN-DGKtrfstkgdgqpiyhflntstFTEYTVLDSAcvvKIDPNAPL--KKMSLLScgvSTGVGA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 hAVNRATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRLQFSLKNNLADEVIELN-DRLTSQMLKERLSGN 230
Cdd:PLN02740  190 -AWNTANVQAGSSVAIFGLGAVGLAVAEGARARGASKIIGvDINPEKFEKGKEMGITDFINPKDsDKPVHERIREMTGGG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 231 LpTVIFDATGNKKSMETSFSLAAQG-AKIIFIGLFQgevTFEDPSFHKKEitLMSSRN---SLPRDFK---QIINLME-- 301
Cdd:PLN02740  269 V-DYSFECAGNVEVLREAFLSTHDGwGLTVLLGIHP---TPKMLPLHPME--LFDGRSitgSVFGDFKgksQLPNLAKqc 342

                         330       340
                  ....*....|....*....|....*.
gi 1243936875 302 -TGKINTAPWLTHKTAFETLPEVFPL 326
Cdd:PLN02740  343 mQGVVNLDGFITHELPFEKINEAFQL 368
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 24-269 7.97e-14

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


Pssm-ID: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 71.09  E-value: 7.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQP-FFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPyincrvcqackrgl 102
Cdd:cd08268    26 GAGEVLIRVEAIGLNRADAMFRRGAYIePPPLPARLGYEAAGVVEAVGA--GVTGFAVGDRVSVIP-------------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 103 snccenlqVLGVHIDGGMTEYMKLPQDKV--HPSSkLDFDQLALV----ETLGIGLhaVNRATITQNDIVLIIGA-GPIG 175
Cdd:cd08268    90 --------AADLGQYGTYAEYALVPAAAVvkLPDG-LSFVEAAALwmqyLTAYGAL--VELAGLRPGDSVLITAAsSSVG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 176 LSTAQFAKLSGAKVLIADLNAKRLQFsLKNNLADEVIELNDRLTSQMLKERLSGNLPTVIFDATGNkKSMETSFSLAAQG 255
Cdd:cd08268   159 LAAIQIANAAGATVIATTRTSEKRDA-LLALGAAHVIVTDEEDLVAEVLRITGGKGVDVVFDPVGG-PQFAKLADALAPG 236

                         250
                  ....*....|....
gi 1243936875 256 AKIIFIGLFQGEVT 269
Cdd:cd08268   237 GTLVVYGALSGEPT 250
alcohol_DH_class_I_II_IV cd08299
class I, II, IV alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major ...
 27-326 1.08e-13

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


Pssm-ID: 176259 [Multi-domain]  Cd Length: 373  Bit Score: 71.19  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  27 EVLVKIKRIGICGTDYHAFRGRQPFFtYPRILGHElGAEVVE-IGsyQNTRTLKIGDKVsIEPYI-NCRVCQACKRGLSN 104
Cdd:cd08299    34 EVRIKIVATGICRSDDHVVSGKLVTP-FPVILGHE-AAGIVEsVG--EGVTTVKPGDKV-IPLFVpQCGKCRACLNPESN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 105 CCENLQVL---GVHIDG------------------GMTEYMKLPQDKVhpsSKLDFDQ-LALVETLGIGLH-----AVNR 157
Cdd:cd08299   109 LCLKNDLGkpqGLMQDGtsrftckgkpihhflgtsTFSEYTVVDEIAV---AKIDAAApLEKVCLIGCGFStgygaAVNT 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 158 ATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRlqFSLKNNL-ADEVIELND--RLTSQMLKErLSGNLPT 233
Cdd:cd08299   186 AKVTPGSTCAVFGLGGVGLSAIMGCKAAGASRIIAvDINKDK--FAKAKELgATECINPQDykKPIQEVLTE-MTDGGVD 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 234 VIFDATGNKKSMETSFSLAAQG-AKIIFIGLfqgevtfeDPSFHKKEITLMS----------------SRNSLPR---DF 293
Cdd:cd08299   263 FSFEVIGRLDTMKAALASCHEGyGVSVIVGV--------PPSSQNLSINPMLlltgrtwkgavfggwkSKDSVPKlvaDY 334

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1243936875 294 KQiinlmetGKINTAPWLTHKTAFETLPEVFPL 326
Cdd:cd08299   335 MA-------KKFNLDPLITHTLPFEKINEGFDL 360
MDR9 cd08274
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-189 2.06e-13

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


Pssm-ID: 176235 [Multi-domain]  Cd Length: 350  Bit Score: 70.02  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLS-HSHKED--IITIGSDEVLVKIKRIGICGTD--------------------YHAFRGRQPFFTYPRI 57
Cdd:cd08274     1 MRAVLLTGHGGLDkLVYRDDvpVPTPAPGEVLIRVGACGVNNTDintregwystevdgatdstgAGEAGWWGGTLSFPRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  58 LGHELGAEVVEIGsyQNTRTLKIGDKVSIEPYINCRVcqackRGLSNCCenlQVLGVHIDGGMTEYMKLPQDKVHP-SSK 136
Cdd:cd08274    81 QGADIVGRVVAVG--EGVDTARIGERVLVDPSIRDPP-----EDDPADI---DYIGSERDGGFAEYTVVPAENAYPvNSP 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1243936875 137 LDFDQLALVET-LGIGLHAVNRATITQNDIVLIIGA-GPIGLSTAQFAKLSGAKV 189
Cdd:cd08274   151 LSDVELATFPCsYSTAENMLERAGVGAGETVLVTGAsGGVGSALVQLAKRRGAIV 205
PLN02586 PLN02586
probable cinnamyl alcohol dehydrogenase
 10-106 3.36e-12

probable cinnamyl alcohol dehydrogenase


Pssm-ID: 166227 [Multi-domain]  Cd Length: 360  Bit Score: 66.83  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  10 GTLSHSH---KEDiitiGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSI 86
Cdd:PLN02586   23 GVLSPFHfsrREN----GDEDVTVKILYCGVCHSDLHTIKNEWGFTRYPIVPGHEIVGIVTKLGK--NVKKFKEGDRVGV 96

                          90       100
                  ....*....|....*....|.
gi 1243936875  87 EPYIN-CRVCQACKRGLSNCC 106
Cdd:PLN02586   97 GVIVGsCKSCESCDQDLENYC 117
PLN02514 PLN02514
cinnamyl-alcohol dehydrogenase
 24-281 4.50e-12

cinnamyl-alcohol dehydrogenase


Pssm-ID: 166155 [Multi-domain]  Cd Length: 357  Bit Score: 66.36  E-value: 4.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYIN-CRVCQACKRGL 102
Cdd:PLN02514   33 GPEDVVIKVIYCGICHTDLHQIKNDLGMSNYPMVPGHEVVGEVVEVGS--DVSKFTVGDIVGVGVIVGcCGECSPCKSDL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 103 SNCCEN--LQVLGVHID-----GGMTEYMKLPQD-KVHPSSKLDFDQLALVETLGIGLHAVNRATITQNDIVL--IIGAG 172
Cdd:PLN02514  111 EQYCNKriWSYNDVYTDgkptqGGFASAMVVDQKfVVKIPEGMAPEQAAPLLCAGVTVYSPLSHFGLKQSGLRggILGLG 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 173 PIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKNNLADEVIELNDRLTSQMLKERLSgnlptVIFDATGNKKSMETSFSLA 252
Cdd:PLN02514  191 GVGHMGVKIAKAMGHHVTVISSSDKKREEALEHLGADDYLVSSDAAEMQEAADSLD-----YIIDTVPVFHPLEPYLSLL 265

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1243936875 253 AQGAKIIFIGLFQGEVTFEDPS--FHKKEIT 281
Cdd:PLN02514  266 KLDGKLILMGVINTPLQFVTPMlmLGRKVIT 296
PLN02827 PLN02827
Alcohol dehydrogenase-like
 27-219 2.05e-11

Alcohol dehydrogenase-like


Pssm-ID: 215442 [Multi-domain]  Cd Length: 378  Bit Score: 64.54  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  27 EVLVKIKRIGICGTDYHAFRgRQPFFtyPRILGHELGAEVVEIGsyQNTRTLKIGDKVSIEPYINCRVCQACKRGLSNCC 106
Cdd:PLN02827   39 EIRIKVVSTSLCRSDLSAWE-SQALF--PRIFGHEASGIVESIG--EGVTEFEKGDHVLTVFTGECGSCRHCISGKSNMC 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 107 enlQVLGVHIDGGM------------------------TEYMKLPQD---KVHPSSKLdfDQLALVET-LGIGLHAV-NR 157
Cdd:PLN02827  114 ---QVLGLERKGVMhsdqktrfsikgkpvyhycavssfSEYTVVHSGcavKVDPLAPL--HKICLLSCgVAAGLGAAwNV 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1243936875 158 ATITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIA-DLNAKRL---------QFSLKNNLADEVIELNDRLT 219
Cdd:PLN02827  189 ADVSKGSSVVIFGLGTVGLSVAQGAKLRGASQIIGvDINPEKAekaktfgvtDFINPNDLSEPIQQVIKRMT 260
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 23-323 4.80e-11

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


Pssm-ID: 176200 [Multi-domain]  Cd Length: 410  Bit Score: 63.23  E-value: 4.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  23 IGSDEVLVKIKRIGICGTDYHAFR--GRQP-----FFTYPRILGHELGAEVVEIGS-YQNtrTLKIGDKVSIEPYINcrv 94
Cdd:cd08238    24 IADDEILVRVISDSLCFSTWKLALqgSDHKkvpndLAKEPVILGHEFAGTILKVGKkWQG--KYKPGQRFVIQPALI--- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  95 cqaCKRGLSNCCENLQVLgvhidGGMTEYMKLP-----QDKVHPSSKLDFDQLALVETLG--IGLHAVNRATI------- 160
Cdd:cd08238    99 ---LPDGPSCPGYSYTYP-----GGLATYHIIPnevmeQDCLLIYEGDGYAEASLVEPLScvIGAYTANYHLQpgeyrhr 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 161 ----TQNDIVLIIGAGPIGLSTAQFAkLSGAK----VLIADLNAKRLQFS---LKNNLADEVIEL-------NDRLTsQM 222
Cdd:cd08238   171 mgikPGGNTAILGGAGPMGLMAIDYA-IHGPIgpslLVVTDVNDERLARAqrlFPPEAASRGIELlyvnpatIDDLH-AT 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 223 LKERLSGNLPTVIFDATGNKKSMETSFSL-AAQGAKIIFIGL----FQGEVTFEDPSFHKKEITLMSSRNSlpRDFKQII 297
Cdd:cd08238   249 LMELTGGQGFDDVFVFVPVPELVEEADTLlAPDGCLNFFAGPvdknFSAPLNFYNVHYNNTHYVGTSGGNT--DDMKEAI 326

                         330       340
                  ....*....|....*....|....*.
gi 1243936875 298 NLMETGKINTAPWLTHKTAFETLPEV 323
Cdd:cd08238   327 DLMAAGKLNPARMVTHIGGLNAAAET 352
MDR6 cd08272
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-261 7.82e-11

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


Pssm-ID: 176233 [Multi-domain]  Cd Length: 326  Bit Score: 62.19  E-value: 7.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKEDII--TIGSDEVLVKIKRIGICGTDYHAFRG----RQPFftyPRILGHELGAEVVEIGSyqN 74
Cdd:cd08272     1 MKALVLESFGGPEVFELREVPrpQPGPGQVLVRVHASGVNPLDTKIRRGgaaaRPPL---PAILGCDVAGVVEAVGE--G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  75 TRTLKIGDKVsiepYincrvcqACKRGLSNccenlqvlgvhIDGGMTEYMKLPQDKVHPSSK-LDFDQLALVETLGI--- 150
Cdd:cd08272    76 VTRFRVGDEV----Y-------GCAGGLGG-----------LQGSLAEYAVVDARLLALKPAnLSMREAAALPLVGItaw 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 151 -GLhaVNRATITQNDIVLI-IGAGPIGLSTAQFAKLSGAKVLIADLNAKRlqfSLKNNL-ADEVIELNDRLTSQMLkERL 227
Cdd:cd08272   134 eGL--VDRAAVQAGQTVLIhGGAGGVGHVAVQLAKAAGARVYATASSEKA---AFARSLgADPIIYYRETVVEYVA-EHT 207

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1243936875 228 SGNLPTVIFDATGNkKSMETSFSLAAQGAKIIFI 261
Cdd:cd08272   208 GGRGFDVVFDTVGG-ETLDASFEAVALYGRVVSI 240
MDR5 cd08271
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 1-240 8.47e-10

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


Pssm-ID: 176232 [Multi-domain]  Cd Length: 325  Bit Score: 59.21  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHKE--DIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHElGAEVVEigsyqntrtl 78
Cdd:cd08271     1 MKAWVLPKPGAALQLTLEeiEIPGPGAGEVLVKVHAAGLNPVDWKVIAWGPPAWSYPHVPGVD-GAGVVV---------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  79 KIGDKVSiEPYINCRVCQAckRGLSNccenlqvlgvhiDGGMTEYMKLPQDKVHPSSK-LDFDQLALVETLG----IGLH 153
Cdd:cd08271    70 AVGAKVT-GWKVGDRVAYH--ASLAR------------GGSFAEYTVVDARAVLPLPDsLSFEEAAALPCAGltayQALF 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 154 AVNRaTITQNDIVLIIGAGPIGLSTAQFAKLSGAKVLI--ADLNAKRLQfSLKnnlADEVIELNDRLTSQMLKERLSGNL 231
Cdd:cd08271   135 KKLR-IEAGRTILITGGAGGVGSFAVQLAKRAGLRVITtcSKRNFEYVK-SLG---ADHVIDYNDEDVCERIKEITGGRG 209


                  ....*....
gi 1243936875 232 PTVIFDATG 240
Cdd:cd08271   210 VDAVLDTVG 218
p53_inducible_oxidoreductase cd05276
PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium ...
 1-342 1.72e-09

PIG3 p53-inducible quinone oxidoreductase; PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176180 [Multi-domain]  Cd Length: 323  Bit Score: 58.22  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPG---TLSHSHKEDIiTIGSDEVLVKIKRIGICGTDYHAFRGRqpfftYP------RILGHELGAEVVEIGS 71
Cdd:cd05276     1 MKAIVIKEPGgpeVLELGEVPKP-APGPGEVLIRVAAAGVNRADLLQRQGL-----YPpppgasDILGLEVAGVVVAVGP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  72 yqNTRTLKIGDkvsiepyincRVCqackrGLsnccenlqVLGvhidGGMTEYMKLPQDKVHP-SSKLDFDQLA-LVETLG 149
Cdd:cd05276    75 --GVTGWKVGD----------RVC-----AL--------LAG----GGYAEYVVVPAGQLLPvPEGLSLVEAAaLPEVFF 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 150 IGLHAV-NRATITQNDIVLI-IGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFsLKNNLADEVIELNDRLTSQMLKERL 227
Cdd:cd05276   126 TAWQNLfQLGGLKAGETVLIhGGASGVGTAAIQLAKALGARVIATAGSEEKLEA-CRALGADVAINYRTEDFAEEVKEAT 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 228 SGNLPTVIFDATGnKKSMETSFSLAAQGAKIIFIGLFQG-EVTFEDPSFHKKEITLMSS--RnSLPRDFK---------Q 295
Cdd:cd05276   205 GGRGVDVILDMVG-GDYLARNLRALAPDGRLVLIGLLGGaKAELDLAPLLRKRLTLTGStlR-SRSLEEKaalaaafreH 282

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1243936875 296 IINLMETGKINTapwLTHKtafetlpeVFPLwlnpeEDVIKAIVYLD 342
Cdd:cd05276   283 VWPLFASGRIRP---VIDK--------VFPL-----EEAAEAHRRME 313
MDR_enoyl_red cd08244
Possible enoyl reductase; Member identified as possible enoyl reductase of the MDR family. ...
 1-273 7.46e-09

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


Pssm-ID: 176206 [Multi-domain]  Cd Length: 324  Bit Score: 56.22  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNE---PGTLSHSHKEDIITiGSDEVLVKIKRIGICGTDYHAFRGRQPFF---TYPRILGHELGAEVVEIGSyqN 74
Cdd:cd08244     1 MRAIRLHEfgpPEVLVPEDVPDPVP-GPGQVRIAVAAAGVHFVDTQLRSGWGPGPfppELPYVPGGEVAGVVDAVGP--G 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  75 TRTLKIGDKVsiepyincrVCQACKRGlsnccenlqvlgvhidGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLG-IGL 152
Cdd:cd08244    78 VDPAWLGRRV---------VAHTGRAG----------------GGYAELAVADVDSLHPvPDGLDLEAAVAVVHDGrTAL 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 153 HAVNRATITQNDIVLIIGA-GPIGLSTAQFAKLSGAKVLIADLNAKRLQFSLKNNlADEVIELNDRLTSQMLKERLSGNL 231
Cdd:cd08244   133 GLLDLATLTPGDVVLVTAAaGGLGSLLVQLAKAAGATVVGAAGGPAKTALVRALG-ADVAVDYTRPDWPDQVREALGGGG 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1243936875 232 PTVIFDATGNKKSMETsFSLAAQGAKIIFIGLFQGEVTFEDP 273
Cdd:cd08244   212 VTVVLDGVGGAIGRAA-LALLAPGGRFLTYGWASGEWTALDE 252
ribitol-5-phosphate_DH cd08237
ribitol-5-phosphate dehydrogenase; NAD-linked ribitol-5-phosphate dehydrogenase, a member of ...
 6-301 5.93e-08

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: 53.52  E-value: 5.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   6 LNEPGTLSHSHKEDIITigSDEVLVKIKRIGICGTDYHAFRG-RQPFF---TYPRILGHELGAEVVeigsYQNTRTLKIG 81
Cdd:cd08237     8 LVRPKFFEVTYEEENLR--EDWVIVRPTYLSICHADQRYYQGnRSPEAlkkKLPMALIHEGIGVVV----SDPTGTYKVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  82 DKVSIEPYINCRVCQACKrglSNCCENLQVLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHAVNR--- 157
Cdd:cd08237    82 TKVVMVPNTPVEKDEIIP---ENYLPSSRFRSSGYDGFMQDYVFLPPDRLVKlPDNVDPEVAAFTELVSVGVHAISRfeq 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 158 ATITQNDIVLIIGAGPIGLSTAQFAK--LSGAKVLIADLNAKRLQfslKNNLADEVIELNDRLtsqmlkERLSGNlptVI 235
Cdd:cd08237   159 IAHKDRNVIGVWGDGNLGYITALLLKqiYPESKLVVFGKHQEKLD---LFSFADETYLIDDIP------EDLAVD---HA 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1243936875 236 FDATGNKksmetsFSLAA--QGAKII----FIGLFQgeVTfEDP------SFHKKEITLMSSRNSLPRDFKQIINLME 301
Cdd:cd08237   227 FECVGGR------GSQSAinQIIDYIrpqgTIGLMG--VS-EYPvpintrMVLEKGLTLVGSSRSTREDFERAVELLS 295
MDR8 cd08273
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 18-305 7.55e-08

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


Pssm-ID: 176234 [Multi-domain]  Cd Length: 331  Bit Score: 53.42  E-value: 7.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  18 EDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTY-PRILGHELGAEVVEIGSyqNTRTLKIGDKVsiepyincrvcq 96
Cdd:cd08273    20 ADLPEPAAGEVVVKVEASGVSFADVQMRRGLYPDQPPlPFTPGYDLVGRVDALGS--GVTGFEVGDRV------------ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  97 ackrglsnccenlqvLGVHIDGGMTEYMKLPQDKVHPSSK-LDFDQL-ALVETLGIGLHAVNR-ATITQNDIVLIIGA-G 172
Cdd:cd08273    86 ---------------AALTRVGGNAEYINLDAKYLVPVPEgVDAAEAvCLVLNYVTAYQMLHRaAKVLTGQRVLIHGAsG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 173 PIGLSTAQFAKLSGAKV----------LIADLNAKRLqfslknnladevielnDRLTSQMLKERLSGNLPTVIFDATGNk 242
Cdd:cd08273   151 GVGQALLELALLAGAEVygtasernhaALRELGATPI----------------DYRTKDWLPAMLTPGGVDVVFDGVGG- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 243 KSMETSFSLAAQGAKIIFIGlFQGEVTFEDPSFHKKEITL--------------------MSSRNSLPRDFKQ----IIN 298
Cdd:cd08273   214 ESYEESYAALAPGGTLVCYG-GNSSLLQGRRSLAALGSLLarlaklkllptgrratfyyvWRDRAEDPKLFRQdlteLLD 292


                  ....*..
gi 1243936875 299 LMETGKI 305
Cdd:cd08273   293 LLAKGKI 299
PLN02178 PLN02178
cinnamyl-alcohol dehydrogenase
 7-106 7.89e-08

cinnamyl-alcohol dehydrogenase


Pssm-ID: 177834 [Multi-domain]  Cd Length: 375  Bit Score: 53.49  E-value: 7.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   7 NEPGTLSHSH---KEDiitiGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGsyQNTRTLKIGDK 83
Cdd:PLN02178   14 DESGVLSPFHfsrREN----GENDVTVKILFCGVCHSDLHTIKNHWGFSRYPIIPGHEIVGIATKVG--KNVTKFKEGDR 87

                          90       100
                  ....*....|....*....|....
gi 1243936875  84 VSIEPYI-NCRVCQACKRGLSNCC 106
Cdd:PLN02178   88 VGVGVIIgSCQSCESCNQDLENYC 111
ETR_like cd05282
2-enoyl thioester reductase-like; 2-enoyl thioester reductase (ETR) catalyzes the ...
 18-308 1.34e-07

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


Pssm-ID: 176645 [Multi-domain]  Cd Length: 323  Bit Score: 52.28  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  18 EDIITIGSDEVLVKIKRIGICGTDYHAFRGRQPFFT-YPRILGHELGAEVVEIGSyqNTRTLKIGDKVsiepyincrvcq 96
Cdd:cd05282    19 LPIPPPGPGEVLVRMLAAPINPSDLITISGAYGSRPpLPAVPGNEGVGVVVEVGS--GVSGLLVGQRV------------ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  97 ackrglsnccenLQVLGVhidGGMTEYMKLPQDKVHP-SSKLDFDQLAlveTLGIglhavNRAT----------ITQNDI 165
Cdd:cd05282    85 ------------LPLGGE---GTWQEYVVAPADDLIPvPDSISDEQAA---MLYI-----NPLTawlmlteylkLPPGDW 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 166 VLIIGAGP-IGLSTAQFAKLSGAKV--------LIADLNAKRlqfslknnlADEVIELNDRLTSQMLKERLSGNLPTVIF 236
Cdd:cd05282   142 VIQNAANSaVGRMLIQLAKLLGFKTinvvrrdeQVEELKALG---------ADEVIDSSPEDLAQRVKEATGGAGARLAL 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 237 DATGNKKSMETSFSLAAQGaKIIFIGLFQGE-VTFEDPSFHKKEITL----------MSSRNSLPRDFKQIINLMETGKI 305
Cdd:cd05282   213 DAVGGESATRLARSLRPGG-TLVNYGLLSGEpVPFPRSVFIFKDITVrgfwlrqwlhSATKEAKQETFAEVIKLVEAGVL 291


                  ...
gi 1243936875 306 NTA 308
Cdd:cd05282   292 TTP 294
enoyl_red cd05195
enoyl reductase of polyketide synthase; Putative enoyl reductase of polyketide synthase. ...
 26-312 5.66e-07

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


Pssm-ID: 176179 [Multi-domain]  Cd Length: 293  Bit Score: 50.26  E-value: 5.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  26 DEVLVKIKRIGICGTDYHAFRGRQPffTYPRILGHELGAEVVEIGSyqNTRTLKIGDkvsiepyincRVCqackrGLSNc 105
Cdd:cd05195     1 DEVEVEVKAAGLNFRDVLVALGLLP--GDETPLGLECSGIVTRVGS--GVTGLKVGD----------RVM-----GLAP- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 106 cenlqvlgvhidGGMTEYMKLPQDKVHP-SSKLDFDQLAlveTLGI----GLHA-VNRATITQNDIVLII-GAGPIGLST 178
Cdd:cd05195    61 ------------GAFATHVRVDARLVVKiPDSLSFEEAA---TLPVayltAYYAlVDLARLQKGESVLIHaAAGGVGQAA 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 179 AQFAKLSGAKVL-IADLNAKRlQFsLKNNLADEVIELNDRLTS--QMLKERLSGNLPTVIFDATGNKKsMETSFSLAAQG 255
Cdd:cd05195   126 IQLAQHLGAEVFaTVGSEEKR-EF-LRELGGPVDHIFSSRDLSfaDGILRATGGRGVDVVLNSLSGEL-LRASWRCLAPF 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243936875 256 AKIIFIG-------------LFQGEVTFE--DPSfhkkeiTLMSSRNSLPRD-FKQIINLMETGKINTAPWLT 312
Cdd:cd05195   203 GRFVEIGkrdilsnsklgmrPFLRNVSFSsvDLD------QLARERPELLRElLREVLELLEAGVLKPLPPTV 269
QOR2 cd05286
Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR ...
 2-189 2.32e-05

Quinone oxidoreductase (QOR); Quinone oxidoreductase (QOR) and 2-haloacrylate reductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. 2-haloacrylate reductase, a member of this subgroup, catalyzes the NADPH-dependent reduction of a carbon-carbon double bond in organohalogen compounds. Although similar to QOR, Burkholderia 2-haloacrylate reductase does not act on the quinones 1,4-benzoquinone and 1,4-naphthoquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176189 [Multi-domain]  Cd Length: 320  Bit Score: 45.51  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   2 KSIILNEPGTLSHSHKEDI--ITIGSDEVLVKIKRIGICGTD-YHaFRGRQPFfTYPRILGHELGAEVVEIGSyqNTRTL 78
Cdd:cd05286     1 KAVRIHKTGGPEVLEYEDVpvPEPGPGEVLVRNTAIGVNFIDtYF-RSGLYPL-PLPFVLGVEGAGVVEAVGP--GVTGF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  79 KIGDKVSiepYINCRvcqackrglsnccenlqvlgvhidGGMTEYMKLPQDKVHP-SSKLDFDQLALVETLGIGLHA-VN 156
Cdd:cd05286    77 KVGDRVA---YAGPP------------------------GAYAEYRVVPASRLVKlPDGISDETAAALLLQGLTAHYlLR 129

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1243936875 157 RA-TITQNDIVLI-IGAGPIGLSTAQFAKLSGAKV 189
Cdd:cd05286   130 ETyPVKPGDTVLVhAAAGGVGLLLTQWAKALGATV 164
ADH_zinc_N_2 pfam13602
Zinc-binding dehydrogenase;
208-341 8.48e-05

Zinc-binding dehydrogenase;


Pssm-ID: 433341 [Multi-domain]  Cd Length: 131  Bit Score: 41.93  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 208 ADEVIelNDRLTSqmLKERLSGNLPTVIFDATGNKkSMETSFSLAAQGAKIIFIGLFQGEVTFEDPSF----HKKEITLM 283
Cdd:pfam13602   3 ADEVI--DYRTTD--FVQATGGEGVDVVLDTVGGE-AFEASLRVLPGGGRLVTIGGPPLSAGLLLPARkrggRGVKYLFL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1243936875 284 SSRNSLPRD-FKQIINLMETGKINTapwlthktafeTLPEVFPLwlnpeEDVIKAIVYL 341
Cdd:pfam13602  78 FVRPNLGADiLQELADLIEEGKLRP-----------VIDRVFPL-----EEAAEAHRYL 120
Mgc45594_like cd08250
Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of ...
 24-323 5.03e-04

Mgc45594 gene product and other MDR family members; Includes Human Mgc45594 gene product of undetermined function. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES.


Pssm-ID: 176212 [Multi-domain]  Cd Length: 329  Bit Score: 41.47  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875  24 GSDEVLVKIKRIGICGTDYHAFRGR-QPFFTYPRILGHELGAEVVEIGSyqNTRTLKIGDKVSIEPYincrvcqackrgl 102
Cdd:cd08250    29 GPGEVLVKNRFVGINASDINFTAGRyDPGVKPPFDCGFEGVGEVVAVGE--GVTDFKVGDAVATMSF------------- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 103 snccenlqvlgvhidGGMTEYMKLPQDKVHPSSKLDFDQLALVE---TLGIGLHAVNRatITQNDIVLIIGA-GPIGLST 178
Cdd:cd08250    94 ---------------GAFAEYQVVPARHAVPVPELKPEVLPLLVsglTASIALEEVGE--MKSGETVLVTAAaGGTGQFA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 179 AQFAKLSGAKVLIADLNAKRLQFsLKNNLADEVIelNDRltSQMLKERLSGNLP---TVIFDATGnKKSMETSF-SLAAQ 254
Cdd:cd08250   157 VQLAKLAGCHVIGTCSSDEKAEF-LKSLGCDRPI--NYK--TEDLGEVLKKEYPkgvDVVYESVG-GEMFDTCVdNLALK 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 255 GAKII--FIGLFQGEVTFEDPSFHKKEITLMSSRNSL------------PRDFKQIINLMETGKINTAPWLTHKTAFETL 320
Cdd:cd08250   231 GRLIVigFISGYQSGTGPSPVKGATLPPKLLAKSASVrgfflphyakliPQHLDRLLQLYQRGKLVCEVDPTRFRGLESV 310


                  ...
gi 1243936875 321 PEV 323
Cdd:cd08250   311 ADA 313
PRK07190 PRK07190
FAD-binding protein;
161-214 5.64e-04

FAD-binding protein;


Pssm-ID: 235955 [Multi-domain]  Cd Length: 487  Bit Score: 41.72  E-value: 5.64e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243936875 161 TQNDIVLIIGAGPIGLSTAQFAKLSGAKVLIAD-------------LNAKRLQFSLKNNLADEVIEL 214
Cdd:PRK07190    3 TQVTDVVIIGAGPVGLMCAYLGQLCGLNTVIVDksdgplevgradaLNARTLQLLELVDLFDELYPL 69
AL_MDR cd08252
Arginate lyase and other MDR family members; This group contains a structure identified as an ...
 1-84 1.37e-03

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


Pssm-ID: 176214 [Multi-domain]  Cd Length: 336  Bit Score: 40.20  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875   1 MKSIILNEPGTLSHSHK-EDII----TIGSDEVLVKIKRIGICGTDYHAFRGRQPFFTYPRILGHELGAEVVEIGSyqNT 75
Cdd:cd08252     1 MKAIGFTQPLPITDPDSlIDIElpkpVPGGRDLLVRVEAVSVNPVDTKVRAGGAPVPGQPKILGWDASGVVEAVGS--EV 78


                  ....*....
gi 1243936875  76 RTLKIGDKV 84
Cdd:cd08252    79 TLFKVGDEV 87
MDR4 cd08270
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 111-320 1.50e-03

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


Pssm-ID: 176231 [Multi-domain]  Cd Length: 305  Bit Score: 40.05  E-value: 1.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 111 VLGVHIDGGMTEYMKLPQDKVHP-SSKLDFDQLAlveTLGI-GLHAVnRATITQNDI----VLIIGA-GPIGLSTAQFAK 183
Cdd:cd08270    79 VVGLGAMGAWAELVAVPTGWLAVlPDGVSFAQAA---TLPVaGVTAL-RALRRGGPLlgrrVLVTGAsGGVGRFAVQLAA 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243936875 184 LSGAKVLIADLNAKRLQFSLKNNLADEVIELNDrltsqmlkerLSGNLPTVIFDATGNkKSMETSFSLAAQGAKIIFIGL 263
Cdd:cd08270   155 LAGAHVVAVVGSPARAEGLRELGAAEVVVGGSE----------LSGAPVDLVVDSVGG-PQLARALELLAPGGTVVSVGS 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243936875 264 FQGE-VTFEDPSF----HKKEIT--LMSSRNSLPRDFKQIINLMETGKIN-----TAPWLTHKTAFETL 320
Cdd:cd08270   224 SSGEpAVFNPAAFvgggGGRRLYtfFLYDGEPLAADLARLLGLVAAGRLDprigwRGSWTEIDEAAEAL 292
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 166-200 2.86e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 38.63  E-value: 2.86e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1243936875 166 VLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQ 200
Cdd:pfam01262  31 VLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLE 65
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
166-193 4.10e-03

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 38.56  E-value: 4.10e-03
                          10        20
                  ....*....|....*....|....*...
gi 1243936875 166 VLIIGAGPIGLSTAQFAKLSGAKVLIAD 193
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIE 30
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
166-193 4.19e-03

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 38.73  E-value: 4.19e-03
                          10        20
                  ....*....|....*....|....*...
gi 1243936875 166 VLIIGAGPIGLSTAQFAKLSGAKVLIAD 193
Cdd:COG0665     5 VVVIGGGIAGLSTAYHLARRGLDVTVLE 32
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 166-193 5.61e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 38.15  E-value: 5.61e-03
                          10        20
                  ....*....|....*....|....*...
gi 1243936875 166 VLIIGAGPIGLSTAQFAKLSGAKVLIAD 193
Cdd:pfam01266   2 VVVIGGGIVGLSTAYELARRGLSVTLLE 29
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 166-202 7.09e-03

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 38.08  E-value: 7.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1243936875 166 VLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQFS 202
Cdd:pfam01494   4 VLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLP 40
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 166-200 8.25e-03

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


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 36.33  E-value: 8.25e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1243936875  166 VLIIGAGPIGLSTAQFAKLSGAKVLIADLNAKRLQ 200
Cdd:smart01002  23 VVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLR 57
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH