A0A6V8SIB4 · A0A6V8SIB4_9CLOT
- ProteinHydroxylamine reductase
- Genehcp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids551 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reduction of hydroxylamine to form NH3 and H2O.
Catalytic activity
- A + H2O + NH4+ = AH2 + H+ + hydroxylamine
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [4Fe-4S] cluster.
Note: Binds 1 hybrid [4Fe-2O-2S] cluster.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 7 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 10 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 19 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 25 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 243 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 267 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 311 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 403 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI); via persulfide group | ||||
Sequence: C | ||||||
Binding site | 431 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 456 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 490 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 492 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | hydroxylamine reductase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHydroxylamine reductase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A6V8SIB4
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 403 | Cysteine persulfide | ||||
Sequence: C |
Structure
Sequence
- Sequence statusComplete
- Length551
- Mass (Da)61,523
- Last updated2020-12-02 v1
- Checksum631EA7EB62A3EEC4
Keywords
- Technical term