A0A3D3FMU7 · A0A3D3FMU7_9SPIR
- ProteinHydroxylamine reductase
- Genehcp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids549 (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 | 5 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 8 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 17 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 23 | [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 | 491 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 493 | 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 > Spirochaetota > Spirochaetia > Spirochaetales > Treponemataceae > Treponema
Accessions
- Primary accessionA0A3D3FMU7
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
- Length549
- Mass (Da)58,687
- Last updated2019-01-16 v1
- Checksum57086C1915497E3C