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Conserved domains on  [gi|119607312|gb|EAW86906|]
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alcohol dehydrogenase, iron containing, 1, isoform CRA_e [Homo sapiens]

Protein Classification

dehydroquinate synthase/iron-containing alcohol dehydrogenase family protein( domain architecture ID 760)

dehydroquinate synthase (DHQS)/iron-containing alcohol dehydrogenase (FeADH) family protein

CATH:  3.40.50.1970
Gene Ontology:  GO:0046872|GO:0030554
PubMed:  9685163|35751426
SCOP:  3001905

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DHQ_Fe-ADH super family cl02872
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ...
 1-155 3.10e-93

Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


The actual alignment was detected with superfamily member cd08190:

Pssm-ID: 445950 [Multi-domain]  Cd Length: 412  Bit Score: 275.96  E-value: 3.10e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08190  258 MLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGA 337

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:cd08190  338 DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEEIFEDAL 412
 
Name Accession Description Interval E-value
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
 1-155 3.10e-93

Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.


Pssm-ID: 341469 [Multi-domain]  Cd Length: 412  Bit Score: 275.96  E-value: 3.10e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08190  258 MLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGA 337

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:cd08190  338 DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEEIFEDAL 412
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
1-155 2.28e-33

Alcohol dehydrogenase, class IV [Energy production and conversion];


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 120.61  E-value: 2.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:COG1454  242 MALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAILLPHVLRFNAPAAPERYAEIARALGL 308

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTrTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:COG1454  309 DV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRCLANNPRPLTEEDIEAILRAAY 381
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
1-147 7.20e-25

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 97.67  E-value: 7.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312    1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:pfam00465 234 MLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRFNAPAAPEKLAQLARALGE 300

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119607312   81 DTRTARIQDAglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDL 147
Cdd:pfam00465 301 DSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPLTAEDI 362
PRK09860 PRK09860
putative alcohol dehydrogenase; Provisional
 1-155 4.18e-06

putative alcohol dehydrogenase; Provisional


Pssm-ID: 182118 [Multi-domain]  Cd Length: 383  Bit Score: 45.33  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:PRK09860 243 MAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGV 309

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:PRK09860 310 NVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEEIVAIYRAAM 383
 
Name Accession Description Interval E-value
HOT cd08190
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ...
 1-155 3.10e-93

Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.


Pssm-ID: 341469 [Multi-domain]  Cd Length: 412  Bit Score: 275.96  E-value: 3.10e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMYKAKDYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08190  258 MLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFRFTAPACPERHLEAAELLGA 337

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:cd08190  338 DTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRPVTEEDLEEIFEDAL 412
EutG COG1454
Alcohol dehydrogenase, class IV [Energy production and conversion];
1-155 2.28e-33

Alcohol dehydrogenase, class IV [Energy production and conversion];


Pssm-ID: 441063 [Multi-domain]  Cd Length: 381  Bit Score: 120.61  E-value: 2.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:COG1454  242 MALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAILLPHVLRFNAPAAPERYAEIARALGL 308

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTrTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:COG1454  309 DV-GLSDEEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRCLANNPRPLTEEDIEAILRAAY 381
Fe-ADH cd08551
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ...
 1-151 3.89e-28

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.


Pssm-ID: 341481 [Multi-domain]  Cd Length: 372  Bit Score: 106.76  E-value: 3.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKakdynvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08551  235 MLLASLLAGIAFGNAGLGAVHALAYPLGG---RYH----------IPHGVANAILLPYVMEFNLPACPEKYAEIAEALGE 301

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALF 151
Cdd:cd08551  302 DVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPLTEEDIREIY 372
Fe-ADH pfam00465
Iron-containing alcohol dehydrogenase;
1-147 7.20e-25

Iron-containing alcohol dehydrogenase;


Pssm-ID: 425696 [Multi-domain]  Cd Length: 362  Bit Score: 97.67  E-value: 7.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312    1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:pfam00465 234 MLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRFNAPAAPEKLAQLARALGE 300

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119607312   81 DTRTARIQDAglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDL 147
Cdd:pfam00465 301 DSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPLTAEDI 362
Fe-ADH-like cd08185
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 1-152 4.14e-21

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341464 [Multi-domain]  Cd Length: 379  Bit Score: 87.94  E-value: 4.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdynvdHPLVPHGLSVVLTSPAVFTFTAQMFPER--HLEMAEIL 78
Cdd:cd08185  242 MAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGAGLAALYPAYFEFTIEKAPEKfaFVARAEAS 309

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119607312  79 GADTrtariQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpqeRVT----KLAPCPQSEEDLAALFE 152
Cdd:cd08185  310 GLSD-----AKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLAENAM---ETMgglfANNPVELTEEDIVEIYE 379
Fe-ADH-like cd08191
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 1-155 3.26e-19

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.


Pssm-ID: 341470 [Multi-domain]  Cd Length: 392  Bit Score: 82.66  E-value: 3.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdHplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08191  252 MALAALLAGLAFGTAGTAAAHALQYPIGALT-----------H--TSHGVGNGLLLPYVMRFNRPARAAELAEIARALGV 318

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTrTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:cd08191  319 TT-AGTSEEAADRAIERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPRPPTEEDLLRILRAAF 392
Fe-ADH-like cd14863
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 1-153 3.73e-19

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341485 [Multi-domain]  Cd Length: 380  Bit Score: 82.20  E-value: 3.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNVdhplvPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd14863  240 MLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YHI-----PHGLACALALPVVLEFNAEAYPEKVKKIAKALGV 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEA 153
Cdd:cd14863  307 SFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNPRPITEEEVAEILEA 378
LPO cd08176
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ...
 1-126 4.56e-15

Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.


Pssm-ID: 341455 [Multi-domain]  Cd Length: 378  Bit Score: 71.04  E-value: 4.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08176  241 MALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAPATGEKYRDIARAMGV 307

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVK 126
Cdd:cd08176  308 DTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAE 353
Fe-ADH-like cd17814
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 1-151 7.59e-15

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341489 [Multi-domain]  Cd Length: 374  Bit Score: 70.26  E-value: 7.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKMykakdynvdhplvPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd17814  238 MMLASLQAGLAFSNASLGAVHAMAHSLGGLLDL-------------PHGECNALLLPHVIRFNFPAAPERYRKIAEAMGL 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpqeR----VTKlaPCPQSEEDLAALF 151
Cdd:cd17814  305 DVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM---KdpclVTN--PRRPTREDIEEIY 374
Fe-ADH-like cd08186
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ...
 4-155 1.99e-14

Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.


Pssm-ID: 341465 [Multi-domain]  Cd Length: 380  Bit Score: 69.22  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   4 ASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdhPLVPHGLSVVLTSPAVFTFTAQMFPErhlEMAEILgadtr 83
Cdd:cd08186  240 ASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVKYIYKAVPE---TLADIL----- 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312  84 taRIQDAGLV--------LADTLRKFLFDLDVDDGLAAVGYSKADIPALVK---GTLPQERVTKLAPCPQSEEDLAALFE 152
Cdd:cd08186  300 --RPIVPGLKgtpdeaekAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPSLDLLLSLAPVEVTEEVVREIYE 377


                 ...
gi 119607312 153 ASM 155
Cdd:cd08186  378 ESL 380
HVD cd08193
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ...
 1-153 6.94e-13

5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.


Pssm-ID: 341472 [Multi-domain]  Cd Length: 379  Bit Score: 64.84  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKakdynvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08193  238 MLLGSMLAGQAFANAPVAAVHALAYPLGG---HFH----------VPHGLSNALVLPHVLRFNLPAAEALYAELARALLP 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVTKLAPCPQSEEDLAALFEA 153
Cdd:cd08193  305 GLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPREVTEEDALAIYQA 377
Fe-ADH-like cd14862
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 1-151 1.10e-12

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341484 [Multi-domain]  Cd Length: 375  Bit Score: 64.17  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQmFPERHLEMAEILGA 80
Cdd:cd14862  238 MHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAK-VTDERYDLLKLLGI 303

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTAriQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKAD----IPALVKGTLpQERVTKLAPCPQSEEDLAALF 151
Cdd:cd14862  304 EARDE--EEALKKLVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAM-EDSCTITSPRPPSEEDLKKLF 375
Fe-ADH-like cd08194
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 1-125 3.32e-12

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.


Pssm-ID: 341473 [Multi-domain]  Cd Length: 378  Bit Score: 62.93  E-value: 3.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVkmykakdynvdHplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08194  235 MMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLPAVTEFSLPGAPERYAEIARAMGI 301

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVdDGLAAVGYSKADIPALV 125
Cdd:cd08194  302 ATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEFEAAL 345
Fe-ADH-like cd08196
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 1-151 1.14e-11

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341475 [Multi-domain]  Cd Length: 367  Bit Score: 61.06  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08196  239 MALASLLAGLAFSQTRTTASHACSYPLTSH--------FG-----IPHGEACALTLPSFIRLNAEALPGRLDELAKQLGF 305

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119607312  81 DTrtarIQDaglvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVtKLAPCPQSEEDLAALF 151
Cdd:cd08196  306 KD----AEE----LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA-NNNPVEVTKEDLEKLL 367
PDDH cd08188
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ...
 1-152 1.58e-11

1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.


Pssm-ID: 341467 [Multi-domain]  Cd Length: 377  Bit Score: 60.99  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLEMAEIL 78
Cdd:cd08188  240 MAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLPACPERFADIARAL 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119607312  79 GADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFE 152
Cdd:cd08188  305 GENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKEDVIAIYR 377
HEPD cd08182
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ...
 1-152 3.43e-10

Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.


Pssm-ID: 341461 [Multi-domain]  Cd Length: 370  Bit Score: 56.85  E-value: 3.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISglvkmykaKDYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHlemaeilgA 80
Cdd:cd08182  236 MAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----VPHGHACALTLPAVLRYNAGADDECD--------D 294

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119607312  81 DTRTARIQDAGLV-----LADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLPQERVtKLAPCPQSEEDLAALFE 152
Cdd:cd08182  295 DPRGREILLALGAsdpaeAAERLRALLESLGLPTRLSEYGVTAEDLEALAASVNTPERL-KNNPVRLSEEDLLRLLE 370
4HBD_NAD cd14860
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ...
 3-158 4.00e-10

4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.


Pssm-ID: 341482  Cd Length: 371  Bit Score: 56.84  E-value: 4.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   3 LASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKakdynvdhplVPHGLS--VVLTspAVFTFTAQMFPERHLE-----MA 75
Cdd:cd14860  235 IASNYAGIAFGNAGCAAVHALSYPLGG---KYH----------VPHGEAnyAVFT--GVLKNYQEKNPDGEIKklnefLA 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312  76 EILGADTRTAriqdaglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLP-QERVTKLAPCPQSEEDLAALFeas 154
Cdd:cd14860  300 KILGCDEEDV---------YDELEELLNKILPKKPLHEYGMKEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY--- 367


                 ....
gi 119607312 155 MKLY 158
Cdd:cd14860  368 KELY 371
NADPH_BDH cd08179
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ...
 1-153 1.66e-09

NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.


Pssm-ID: 341458 [Multi-domain]  Cd Length: 379  Bit Score: 54.89  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLEMAEIL 78
Cdd:cd08179  239 MHNASCLAGMAFSNSGLGIVHSMAHKGGAFFG-------------IPHGLanAILL--PYVIEFNSKDPEARARYAALLI 303

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119607312  79 GADTRTArIQDaglvLADTLRKFLFDLDVDDGLAAVGYS----KADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEA 153
Cdd:cd08179  304 GLTDEEL-VED----LIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMAENAM-NDACTGTNPRKPTVEEMKELLKA 376
Fe-ADH-like cd14865
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 1-155 5.42e-08

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341487 [Multi-domain]  Cd Length: 383  Bit Score: 50.62  E-value: 5.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLEMAEIL 78
Cdd:cd14865  241 LAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHVMRYNLDAAAERYAELALAL 305

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119607312  79 --GADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:cd14865  306 ayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILFNPREVDPEDILAILEAAY 383
Fe-ADH-like cd08183
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 1-152 1.90e-07

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341462 [Multi-domain]  Cd Length: 377  Bit Score: 49.04  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGlvkMYKAkdynvdhplvPHGL--SVVLtsPAVFTFTAQ---------MFPE 69
Cdd:cd08183  237 MALASLLGGLALANAGLGAVHGLAGPLGG---MFGA----------PHGAicAALL--PPVLEANLRalrerepdsPALA 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312  70 RHLEMAEILgADTRTARIQDaglvLADTLRKFLFDLDVdDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAA 149
Cdd:cd08183  302 RYRELAGIL-TGDPDAAAED----GVEWLEELCEELGI-PRLSEYGLTEEDFPEIVEKAR-GSSSMKGNPIELSDEELLE 374


                 ...
gi 119607312 150 LFE 152
Cdd:cd08183  375 ILE 377
Fe-ADH-like cd14861
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ...
 1-155 2.11e-07

Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.


Pssm-ID: 341483 [Multi-domain]  Cd Length: 374  Bit Score: 49.05  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNaGVHLCHGMSYPISGLVKMykakdynvdhplvPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd14861  241 MMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYVLRFNRPAVEDKLARLARALGL 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTAriqDAglvLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:cd14861  307 GLGGF---DD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNPRPVTAEDYRALLREAL 374
PRK09860 PRK09860
putative alcohol dehydrogenase; Provisional
 1-155 4.18e-06

putative alcohol dehydrogenase; Provisional


Pssm-ID: 182118 [Multi-domain]  Cd Length: 383  Bit Score: 45.33  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:PRK09860 243 MAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKVAAARLRDCAAAMGV 309

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  81 DTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEASM 155
Cdd:PRK09860 310 NVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEEIVAIYRAAM 383
PRK13805 PRK13805
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
 1-120 6.69e-06

bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional


Pssm-ID: 237515 [Multi-domain]  Cd Length: 862  Bit Score: 44.79  E-value: 6.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQ------MFP------ 68
Cdd:PRK13805 706 MHNASTIAGMAFANAFLGICHSMAHKLGAEFH-------------IPHGRANAILLPHVIRYNATdppkqaAFPqyeypr 772

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 119607312  69 --ERHLEMAEILG--ADTRTARIQdaglVLADTLRKFLFDLDVDDGLAAVGYSKAD 120
Cdd:PRK13805 773 adERYAEIARHLGlpGSTTEEKVE----SLIKAIEELKAELGIPMSIKEAGVDEAD 824
AAD_C cd08178
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ...
 1-120 1.06e-05

C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.


Pssm-ID: 341457 [Multi-domain]  Cd Length: 400  Bit Score: 44.10  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFTAQ-------MFP----- 68
Cdd:cd08178  246 MHNAATIAGMAFANAFLGICHSLAHKLGAAFH-------------IPHGRANAILLPHVIRYNATdpptkqaAFPqykyy 312

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119607312  69 ---ERHLEMAEILGADTRTariqDAGLV--LADTLRKFLFDLDVDDGLAAVGYSKAD 120
Cdd:cd08178  313 vakERYAEIADLLGLGGKT----PEEKVesLIKAIEDLKKDLGIPTSIREAGIDEAD 365
PDD cd08180
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ...
 1-152 1.94e-05

1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.


Pssm-ID: 341459 [Multi-domain]  Cd Length: 333  Bit Score: 43.25  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLVKmykakdynvdhplVPHGLSVVLTSPAVFTFtaqmfperhlemaeilga 80
Cdd:cd08180  223 MHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF------------------ 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119607312  81 dtrtariqdaglvLADTLRKFLFDLDVDDGLAAVGYSKAD----IPALVKGTLpQERVTKLAPCPQSEEDLAALFE 152
Cdd:cd08180  272 -------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAAL-ADRCTATNPRKPTAEDLIELLR 333
Fe-ADH-like cd14864
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ...
 3-153 7.41e-05

iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.


Pssm-ID: 341486 [Multi-domain]  Cd Length: 376  Bit Score: 41.52  E-value: 7.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   3 LASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNVDHPLVphgLSVVLtsPAVFTFTAQMFPERHLEMAEILGADT 82
Cdd:cd14864  239 QAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL--PHVIEYAATSAPDKYAKIARALGEDV 305

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119607312  83 RTARIQDAGLVLADTLRKFLFDLDVDDGLAAVGyskadipalVKGTLPQ-------ERVTKLAPCPQSEEDLAALFEA 153
Cdd:cd14864  306 EGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLD---------LASSLEQlaaiaedAPKLNGLPRSMSSDDIFDILKA 374
Fe-ADH-like cd08189
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ...
 1-153 2.03e-04

Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.


Pssm-ID: 341468 [Multi-domain]  Cd Length: 378  Bit Score: 40.14  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISGLvkmykakdYNvdhplVPHGL--SVVLtsPAVFTFTAQMFPERHLEMAEIL 78
Cdd:cd08189  240 MLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYGPAAEKRLAELADAA 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119607312  79 GADTRTARIQDAGLVLADTLRKFLFDLDVDDGLAAVgySKADIPALVKGTLpQErVTKLAPCPQ--SEEDLAALFEA 153
Cdd:cd08189  305 GLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAKRAL-KE-ANPLYPVPRimDRKDCEELLRK 377
PPD-like cd08181
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ...
 1-82 2.54e-04

1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.


Pssm-ID: 341460 [Multi-domain]  Cd Length: 358  Bit Score: 39.88  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSYPISglvkmykakdYNVDhplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILGA 80
Cdd:cd08181  237 LMYASTLAGMVIAQTGTTLPHGLGYPLT----------YFKG---IPHGRANGILLPAYLKLCEKQEPEKVDKILKLLGF 303


                 ..
gi 119607312  81 DT 82
Cdd:cd08181  304 GS 305
PRK15454 PRK15454
ethanolamine utilization ethanol dehydrogenase EutG;
1-154 3.91e-04

ethanolamine utilization ethanol dehydrogenase EutG;


Pssm-ID: 185351 [Multi-domain]  Cd Length: 395  Bit Score: 39.63  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119607312   1 MHLASAFAGIGFGNAGVHLCHGMSY-PISGLvkmykakdynvdHplVPHGLSVVLTSPAVFTFTAQMFPERHLEMAEILg 79
Cdd:PRK15454 261 MLLASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMVCRERFSQIGRAL- 325

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119607312  80 aDTRTARIQDAglvlADTLRKFLFDLDVDDGLAAVGYSKADIPALVKGTLpQERVTKLAPCPQSEEDLAALFEAS 154
Cdd:PRK15454 326 -RTKKSDDRDA----INAVSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQIVGLYAAA 394
 
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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