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Conserved domains on  [gi|1123217019|gb|OKW63380|]
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L-sorbose 1-phosphate reductase, partial [Escherichia coli]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MDR super family cl16912
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 9-167 9.17e-87

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


The actual alignment was detected with superfamily member cd08238:

Pssm-ID: 450120 [Multi-domain]  Cd Length: 410  Bit Score: 260.06  E-value: 9.17e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIAINLGCVLPYHGSYFAAASLVEPMCCIIGAYHANYHTTQYVYEHRMGVKPGGNIALLACAGPMGIGAID 88
Cdd:cd08238   115 GLATYHIIPNEVMEQDCLLIYEGDGYAEASLVEPLSCVIGAYTANYHLQPGEYRHRMGIKPGGNTAILGGAGPMGLMAID 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  89 YAINGGIQPSRVVVVDIDDKRLAQVQKLLPVElAASKGIELVYVNTKGMSDPVQMLRALTGDAGFDDIFVYAAVPAVVE 167
Cdd:cd08238   195 YAIHGPIGPSLLVVTDVNDERLARAQRLFPPE-AASRGIELLYVNPATIDDLHATLMELTGGQGFDDVFVFVPVPELVE 272
 
Name Accession Description Interval E-value
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 9-167 9.17e-87

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: 260.06  E-value: 9.17e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIAINLGCVLPYHGSYFAAASLVEPMCCIIGAYHANYHTTQYVYEHRMGVKPGGNIALLACAGPMGIGAID 88
Cdd:cd08238   115 GLATYHIIPNEVMEQDCLLIYEGDGYAEASLVEPLSCVIGAYTANYHLQPGEYRHRMGIKPGGNTAILGGAGPMGLMAID 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  89 YAINGGIQPSRVVVVDIDDKRLAQVQKLLPVElAASKGIELVYVNTKGMSDPVQMLRALTGDAGFDDIFVYAAVPAVVE 167
Cdd:cd08238   195 YAIHGPIGPSLLVVTDVNDERLARAQRLFPPE-AASRGIELLYVNPATIDDLHATLMELTGGQGFDDVFVFVPVPELVE 272
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 34-167 1.76e-10

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: 58.23  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  34 FAAASLVEPMCCiigAYHANyhttqyvyeHRMGVKPGGNIALLACaGPMGIGAIDYAINGGiqPSRVVVVDIDDKRLAQV 113
Cdd:COG1063   138 DEAAALVEPLAV---ALHAV---------ERAGVKPGDTVLVIGA-GPIGLLAALAARLAG--AARVIVVDRNPERLELA 202

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1123217019 114 QKLlpvelaaskGIELVyVNTKGmSDPVQMLRALTGDAGFDDIFVYAAVPAVVE 167
Cdd:COG1063   203 REL---------GADAV-VNPRE-EDLVEAVRELTGGRGADVVIEAVGAPAALE 245
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
81-167 1.88e-07

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 47.60  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  81 PMGIGAIDYAINGGIqpsRVVVVDIDDKRLAQVQKLlpvelaaskGIElVYVNTKGMsDPVQMLRALTGDAGFDDIFVYA 160
Cdd:pfam00107   1 GVGLAAIQLAKAAGA---KVIAVDGSEEKLELAKEL---------GAD-HVINPKET-DLVEEIKELTGGKGVDVVFDCV 66


                  ....*..
gi 1123217019 161 AVPAVVE 167
Cdd:pfam00107  67 GSPATLE 73
 
Name Accession Description Interval E-value
sorbose_phosphate_red cd08238
L-sorbose-1-phosphate reductase; L-sorbose-1-phosphate reductase, a member of the MDR family, ...
 9-167 9.17e-87

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: 260.06  E-value: 9.17e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIAINLGCVLPYHGSYFAAASLVEPMCCIIGAYHANYHTTQYVYEHRMGVKPGGNIALLACAGPMGIGAID 88
Cdd:cd08238   115 GLATYHIIPNEVMEQDCLLIYEGDGYAEASLVEPLSCVIGAYTANYHLQPGEYRHRMGIKPGGNTAILGGAGPMGLMAID 194

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  89 YAINGGIQPSRVVVVDIDDKRLAQVQKLLPVElAASKGIELVYVNTKGMSDPVQMLRALTGDAGFDDIFVYAAVPAVVE 167
Cdd:cd08238   195 YAIHGPIGPSLLVVTDVNDERLARAQRLFPPE-AASRGIELLYVNPATIDDLHATLMELTGGQGFDDVFVFVPVPELVE 272
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 9-167 1.47e-10

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: 58.38  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIAINLGCV--LPYHGSyFAAASLVEPM-CCIIGAyhanyhttqyvyeHRMGVKPGGNIALLAcAGPMGI- 84
Cdd:cd08235   116 GFAEYVRVPAWAVKRGGVlkLPDNVS-FEEAALVEPLaCCINAQ-------------RKAGIKPGDTVLVIG-AGPIGLl 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  85 --------GAidyainggiqpSRVVVVDIDDKRLAQvqkllpvelAASKGIELVyVNTKGmSDPVQMLRALTGDAGFDDI 156
Cdd:cd08235   181 hamlakasGA-----------RKVIVSDLNEFRLEF---------AKKLGADYT-IDAAE-EDLVEKVRELTDGRGADVV 238

                         170
                  ....*....|.
gi 1123217019 157 FVYAAVPAVVE 167
Cdd:cd08235   239 IVATGSPEAQA 249
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 34-167 1.76e-10

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: 58.23  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  34 FAAASLVEPMCCiigAYHANyhttqyvyeHRMGVKPGGNIALLACaGPMGIGAIDYAINGGiqPSRVVVVDIDDKRLAQV 113
Cdd:COG1063   138 DEAAALVEPLAV---ALHAV---------ERAGVKPGDTVLVIGA-GPIGLLAALAARLAG--AARVIVVDRNPERLELA 202

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1123217019 114 QKLlpvelaaskGIELVyVNTKGmSDPVQMLRALTGDAGFDDIFVYAAVPAVVE 167
Cdd:COG1063   203 REL---------GADAV-VNPRE-EDLVEAVRELTGGRGADVVIEAVGAPAALE 245
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 9-157 4.10e-10

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


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 56.81  E-value: 4.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEiainlGCVLPYHGSYFAAASLVEPMCciIGAyHANyhttqyvyeHRMGVKPGgNIALLACAGPMGIGAID 88
Cdd:cd08261   116 GFAEYIVVPA-----DALLVPEGLSLDQAALVEPLA--IGA-HAV---------RRAGVTAG-DTVLVVGAGPIGLGVIQ 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  89 YAINGGIqpsRVVVVDIDDKRLAqvqklLPVELAASKGIELvyvntkGMSDPVQMLRALTGDAGFDDIF 157
Cdd:cd08261   178 VAKARGA---RVIVVDIDDERLE-----FARELGADDTINV------GDEDVAARLRELTDGEGADVVI 232
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 9-167 4.84e-09

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: 53.77  E-value: 4.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIaiNLgCVLPYHGSYFAAAsLVEPMCCiigAYHANYHTtqyvyehrmGVKPGGNIALLACaGPMGIGAID 88
Cdd:cd08236   115 AFAEYVSVPAR--NL-IKIPDHVDYEEAA-MIEPAAV---ALHAVRLA---------GITLGDTVVVIGA-GTIGLLAIQ 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  89 YAINGGIqpSRVVVVDIDDKRLaqvqkllpvELAASKGIELVyVNTKGmsDPVQMLRALTGDAGFDDIFVYAAVPAVVE 167
Cdd:cd08236   178 WLKILGA--KRVIAVDIDDEKL---------AVARELGADDT-INPKE--EDVEKVRELTEGRGADLVIEAAGSPATIE 242
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
81-167 1.88e-07

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 47.60  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  81 PMGIGAIDYAINGGIqpsRVVVVDIDDKRLAQVQKLlpvelaaskGIElVYVNTKGMsDPVQMLRALTGDAGFDDIFVYA 160
Cdd:pfam00107   1 GVGLAAIQLAKAAGA---KVIAVDGSEEKLELAKEL---------GAD-HVINPKET-DLVEEIKELTGGKGVDVVFDCV 66


                  ....*..
gi 1123217019 161 AVPAVVE 167
Cdd:pfam00107  67 GSPATLE 73
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 9-167 6.28e-07

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: 47.70  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIAINlgcVLPYHGSYFAAASLVEPMCCiigAYHAnyhttqyVYEHRmGVKPGGNIALLAcAGPMGIGAID 88
Cdd:cd05188    88 GFAEYVVVPADNLV---PLPDGLSLEEAALLPEPLAT---AYHA-------LRRAG-VLKPGDTVLVLG-AGGVGLLAAQ 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  89 YAINGGiqpSRVVVVDIDDKRLaqvqkllpvELAASKGIELVYVNTKGmsDPVQMLRaLTGDAGFDDIFVYAAVPAVVE 167
Cdd:cd05188   153 LAKAAG---ARVIVTDRSDEKL---------ELAKELGADHVIDYKEE--DLEEELR-LTGGGGADVVIDAVGGPETLA 216
THR_DH_like cd08239
L-threonine dehydrogenase (TDH)-like; MDR/AHD-like proteins, including a protein annotated as ...
 9-154 1.83e-06

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: 46.54  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEiainlGCVLPYHGSY-FAAASLVepmCCIIG-AYHAnyhttqyvyEHRMGVKPGGNIALLAcAGPMGIGA 86
Cdd:cd08239   118 GHAEYMLVPE-----KTLIPLPDDLsFADGALL---LCGIGtAYHA---------LRRVGVSGRDTVLVVG-AGPVGLGA 179

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123217019  87 IDYAINGGIQPsrVVVVDIDDKRLaqvqkllpvELAASKGIELVYvntKGMSDPVQMLRALTGDAGFD 154
Cdd:cd08239   180 LMLARALGAED--VIGVDPSPERL---------ELAKALGADFVI---NSGQDDVQEIRELTSGAGAD 233
FDH_like_ADH2 cd08286
formaldehyde dehydrogenase (FDH)-like; This group is related to formaldehyde dehydrogenase ...
 66-154 2.25e-06

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: 46.09  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  66 GVKPGGNIALlACAGPMGIGAIDYAINggIQPSRVVVVDIDDKRLAQVQKllpveLAASKGielvyVNTKGmSDPVQMLR 145
Cdd:cd08286   163 KVKPGDTVAI-VGAGPVGLAALLTAQL--YSPSKIIMVDLDDNRLEVAKK-----LGATHT-----VNSAK-GDAIEQVL 228


                  ....*....
gi 1123217019 146 ALTGDAGFD 154
Cdd:cd08286   229 ELTDGRGVD 237
Zn_ADH2 cd08256
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ...
 9-154 2.65e-06

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: 45.86  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIAINLGcvLPYHGSYFAAAsLVEPMCCIIgayhanyHTTQyvyehRMGVKpGGNIALLACAGPMGIGAID 88
Cdd:cd08256   129 GMAEYMRFPKEAIVHK--VPDDIPPEDAI-LIEPLACAL-------HAVD-----RANIK-FDDVVVLAGAGPLGLGMIG 192

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123217019  89 YAINGGiqPSRVVVVDIDDKRLaqvqkllpvELAASKGIELVYVNTKgmSDPVQMLRALTGDAGFD 154
Cdd:cd08256   193 AARLKN--PKKLIVLDLKDERL---------ALARKFGADVVLNPPE--VDVVEKIKELTGGYGCD 245
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 34-161 2.67e-06

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: 45.97  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  34 FAAASLVEPMCCiigAYHAnyhttqyVYEHRMGVKPGGNIALLAcAGPMGIGAIDYAINGGiqPSRVVVVDIDDKRlaqv 113
Cdd:cd08265   178 FEAGALVEPTSV---AYNG-------LFIRGGGFRPGAYVVVYG-AGPIGLAAIALAKAAG--ASKVIAFEISEER---- 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1123217019 114 qkllpVELAASKGIELVYvNTKGMSD--PVQMLRALTGDAGfDDIFVYAA 161
Cdd:cd08265   241 -----RNLAKEMGADYVF-NPTKMRDclSGEKVMEVTKGWG-ADIQVEAA 283
butanediol_DH_like cd08233
(2R,3R)-2,3-butanediol dehydrogenase; (2R,3R)-2,3-butanediol dehydrogenase, a zinc-dependent ...
 34-167 1.88e-05

(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: 43.30  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  34 FAAASLVEPMCCiigAYHAnyhttqyVyeHRMGVKPGGNIALLAcAGPMGIGAIDYAINGGIqpSRVVVVDIDDKRLAQV 113
Cdd:cd08233   149 LEEAALVEPLAV---AWHA-------V--RRSGFKPGDTALVLG-AGPIGLLTILALKAAGA--SKIIVSEPSEARRELA 213

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1123217019 114 QKLLPVELaaskgielvyVNTKGMsDPVQMLRALTGDAGFDDIFVYAAVPAVVE 167
Cdd:cd08233   214 EELGATIV----------LDPTEV-DVVAEVRKLTGGGGVDVSFDCAGVQATLD 256
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 9-167 6.72e-05

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 41.64  E-value: 6.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   9 GNATYMIIPEIAInlgCVLPYHGSYFAAASLvepMCCIIGAYHANYHTtqyvyehrmGVKPGGNIALLACaGPMGIGAID 88
Cdd:COG1064   117 GYAEYVVVPARFL---VKLPDGLDPAEAAPL---LCAGITAYRALRRA---------GVGPGDRVAVIGA-GGLGHLAVQ 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  89 YAInggIQPSRVVVVDIDDKRLAQVQKLlpvelaaskGIELVyVNTKGmSDPVQMLRALTgdaGFDDIFVYAAVPAVVE 167
Cdd:COG1064   181 IAK---ALGAEVIAVDRSPEKLELAREL---------GADHV-VNSSD-EDPVEAVRELT---GADVVIDTVGAPATVN 242
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 5-154 7.73e-05

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: 41.71  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019   5 AASPGN----ATYMIIPEIAinlgCV-LPYHGSyFAAASLVEPMCCiigAYHANyhttqyvyeHRMGVKPGGNIALLAcA 79
Cdd:cd05285   110 AATPPVdgtlCRYVNHPADF----CHkLPDNVS-LEEGALVEPLSV---GVHAC---------RRAGVRPGDTVLVFG-A 171

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123217019  80 GPmgIGAIDYAINGGIQPSRVVVVDIDDKRLaqvqkllpvELAASKGIELVYVNTKGMSDPV-QMLRALTGDAGFD 154
Cdd:cd05285   172 GP--IGLLTAAVAKAFGATKVVVTDIDPSRL---------EFAKELGATHTVNVRTEDTPESaEKIAELLGGKGPD 236
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 66-154 3.63e-04

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: 39.83  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  66 GVKPGGNIALLACaGPMGIGAIDYAINGGiqPSRVVVVDIDDKRLAQVQKLLPVELaaskgielvyVNTKGMSDPVQMLR 145
Cdd:cd08283   181 EVKPGDTVAVWGC-GPVGLFAARSAKLLG--AERVIAIDRVPERLEMARSHLGAET----------INFEEVDDVVEALR 247


                  ....*....
gi 1123217019 146 ALTGDAGFD 154
Cdd:cd08283   248 ELTGGRGPD 256
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 11-149 4.11e-04

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: 39.51  E-value: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  11 ATYMIIPEIAINLgCVLPYHGSYFAAASLvepMCCIIGAYHAnyhttqyvYEHRMGVKPGGNIALLACAGpMGIGAIDYA 90
Cdd:cd08260   119 AEYVAVPRADVNL-VRLPDDVDFVTAAGL---GCRFATAFRA--------LVHQARVKPGEWVAVHGCGG-VGLSAVMIA 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1123217019  91 INGGiqpSRVVVVDIDDKRLAQVQKLLPVELaaskgielvyVNTKGMSDPVQMLRALTG 149
Cdd:cd08260   186 SALG---ARVIAVDIDDDKLELARELGAVAT----------VNASEVEDVAAAVRDLTG 231
CAD3 cd08297
Cinnamyl alcohol dehydrogenases (CAD); These alcohol dehydrogenases are related to the ...
 66-167 8.45e-04

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: 38.67  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  66 GVKPGGNIALLACAGPMGIGAIDYAINGGIqpsRVVVVDIDDKRLaqvqkllpvELAASKGIElVYVNTKGmSDPVQMLR 145
Cdd:cd08297   162 GLKPGDWVVISGAGGGLGHLGVQYAKAMGL---RVIAIDVGDEKL---------ELAKELGAD-AFVDFKK-SDDVEAVK 227

                          90       100
                  ....*....|....*....|..
gi 1123217019 146 ALTGDAGFDDIFVYAAVPAVVE 167
Cdd:cd08297   228 ELTGGGGAHAVVVTAVSAAAYE 249
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 66-154 1.21e-03

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: 38.02  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123217019  66 GVKPGGNIALLACaGPMGIGAIDYAINGGiqPSRVVVVDIDDKRLAQVQKLLPVELAASKGielvyvntkgmSDPVQMLR 145
Cdd:cd05278   164 GIKPGSTVAVIGA-GPVGLCAVAGARLLG--AARIIAVDSNPERLDLAKEAGATDIINPKN-----------GDIVEQIL 229


                  ....*....
gi 1123217019 146 ALTGDAGFD 154
Cdd:cd05278   230 ELTGGRGVD 238
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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