aldehyde ferredoxin oxidoreductase (AOR) family protein similar to AOR, formaldehyde ferredoxin oxidoreductase (FOR), and glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR)
Aldehyde ferredoxin oxidoreductase, N-terminal domain; Aldehyde ferredoxin oxidoreductase (AOR) catalyzes the reversible oxidation of aldehydes to their corresponding carboxylic acids with their accompanying reduction of the redox protein ferredoxin. This domain interacts with the tungsten cofactor.
Pssm-ID: 426943 [Multi-domain] Cd Length: 199 Bit Score: 258.87 E-value: 2.12e-83
Aldehyde ferredoxin oxidoreductase, N-terminal domain; Enzymes of the aldehyde ferredoxin ...
5-202
1.54e-78
Aldehyde ferredoxin oxidoreductase, N-terminal domain; Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates. This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic archea. carboxylic acid reductase found in clostridia. and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum. GAPOR may be involved in glycolysis. but the functions of the other proteins are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases.
Pssm-ID: 129026 [Multi-domain] Cd Length: 199 Bit Score: 246.28 E-value: 1.54e-78
Aldehyde ferredoxin oxidoreductase, N-terminal domain; Aldehyde ferredoxin oxidoreductase (AOR) catalyzes the reversible oxidation of aldehydes to their corresponding carboxylic acids with their accompanying reduction of the redox protein ferredoxin. This domain interacts with the tungsten cofactor.
Pssm-ID: 426943 [Multi-domain] Cd Length: 199 Bit Score: 258.87 E-value: 2.12e-83
Aldehyde ferredoxin oxidoreductase, N-terminal domain; Enzymes of the aldehyde ferredoxin ...
5-202
1.54e-78
Aldehyde ferredoxin oxidoreductase, N-terminal domain; Enzymes of the aldehyde ferredoxin oxidoreductase (AOR) family contain a tungsten cofactor and an 4Fe4S cluster and catalyse the interconversion of aldehydes to carboxylates. This family includes AOR, formaldehyde ferredoxin oxidoreductase (FOR), glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR), all isolated from hyperthermophilic archea. carboxylic acid reductase found in clostridia. and hydroxycarboxylate viologen oxidoreductase from Proteus vulgaris, the sole member of the AOR family containing molybdenum. GAPOR may be involved in glycolysis. but the functions of the other proteins are not yet clear. AOR has been proposed to be the primary enzyme responsible for oxidising the aldehydes that are produced by the 2-keto acid oxidoreductases.
Pssm-ID: 129026 [Multi-domain] Cd Length: 199 Bit Score: 246.28 E-value: 1.54e-78
Aldehyde ferredoxin oxidoreductase, domains 2 _ 3; Aldehyde ferredoxin oxidoreductase (AOR) catalyzes the reversible oxidation of aldehydes to their corresponding carboxylic acids with their accompanying reduction of the redox protein ferredoxin. This family is composed of two structural domains that bind the tungsten cofactor via DXXGL(C/D) motifs. In addition to maintaining specific binding interactions with the cofactor, another role for domains 2 and 3 may be to regulate substrate access to AOR.
Pssm-ID: 426196 Cd Length: 388 Bit Score: 214.39 E-value: 7.82e-64
Uncharacterized protein family (UPF0160); This family of proteins contains a large number of ...
178-298
2.09e-03
Uncharacterized protein family (UPF0160); This family of proteins contains a large number of metal binding residues. The patterns are suggestive of a phosphoesterase function. The conserved DHH motif may mean this family is related to pfam01368.
Pssm-ID: 461014 Cd Length: 315 Bit Score: 40.57 E-value: 2.09e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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