Q2RI40 · OORD_MOOTA
- ProteinOxalate oxidoreductase subunit delta
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids315 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Catalyzes the anaerobic oxidation of oxalate using a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. Does not require coenzyme A as cosubstrate. Enables anaerobic growth on oxalate which is used as energy source by the bacteria.
Catalytic activity
- oxalate + oxidized 2[4Fe-4S]-[ferredoxin] = 2 CO2 + reduced 2[4Fe-4S]-[ferredoxin]
CHEBI:30623 + RHEA-COMP:10004 CHEBI:33722 Position: 1CHEBI:33722 Position: 2= 2 CHEBI:16526 + RHEA-COMP:10002 CHEBI:33723 Position: 1CHEBI:33723 Position: 2
Cofactor
Note: Binds 2 [4Fe-4S] clusters per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
58 μM | oxalate |
Kinetic parameters determined with the heterodimer oxalate oxidoreductase complex.
pH Dependence
Optimum pH is 8.7.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 261 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 264 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 267 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 271 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 290 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 293 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 296 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 300 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor | |
Biological Process | oxalate catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOxalate oxidoreductase subunit delta
- EC number
- Short namesOOR delta subunit
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Moorellales > Moorellaceae > Moorella
Accessions
- Primary accessionQ2RI40
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000430799 | 1-315 | Oxalate oxidoreductase subunit delta | |||
Sequence: MSTKDLFAEPNLKQITVWARGVVMNKDARDIVVALTEAAAKEGKYVQAWENYVDLPDRIYVPVRAYARISSDPIESKYIYENETPDIVVLVEESLIKGVPILKGIRPGSTLVVNTKRSIDTILEFLGDTGNLAQIVTVDANSMAEAVMTLSGAEGATDATGIGAGIAAPIAGAVVKATGIVDVENLAAVVKNPAAMRRGYAEAQVRQLPPHEAVEEAAVSATELLRQMPFAGTVPSPVTENEGMVTGNWRIQRPIIDREACTECYTCWIYCPDSCITRTEEGPVFNMKYCKGCGLCTAVCPSGALTNVPELDFKD |
Interaction
Subunit
Dimer of heterotrimer of one alpha, one beta and one delta subunit.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 252-280 | 4Fe-4S ferredoxin-type 1 | ||||
Sequence: QRPIIDREACTECYTCWIYCPDSCITRTE | ||||||
Domain | 281-310 | 4Fe-4S ferredoxin-type 2 | ||||
Sequence: EGPVFNMKYCKGCGLCTAVCPSGALTNVPE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length315
- Mass (Da)33,931
- Last updated2006-01-24 v1
- Checksum488A111A1E1E808C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000232 EMBL· GenBank· DDBJ | ABC19899.1 EMBL· GenBank· DDBJ | Genomic DNA |