A0A847LRY6 · A0A847LRY6_9SPIR
- ProteinHydroxylamine reductase
- Genehcp
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids543 (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 + NH4+ + H2O = hydroxylamine + AH2 + H+
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) | |||
Binding site | 8 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 17 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 23 | [4Fe-4S] cluster (UniProtKB | ChEBI) | |||
Binding site | 237 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 261 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 305 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 397 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI); via persulfide group | |||
Binding site | 425 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 450 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 485 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | |||
Binding site | 487 | hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI) | |||
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 | |
Molecular Function | peroxidase activity | |
Biological Process | response to hydrogen peroxide |
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 > Exilispira
Accessions
- Primary accessionA0A847LRY6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 397 | Cysteine persulfide | |||
Structure
Sequence
- Sequence statusComplete
- Length543
- Mass (Da)60,022
- Last updated2021-09-29 v1
- MD5 Checksum61FF71A6AD0F56E224DE1B3F1572EE58
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAAYUW010000014 EMBL· GenBank· DDBJ | NLJ04223.1 EMBL· GenBank· DDBJ | Genomic DNA |