Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

Q2RQN9 · HCP_RHORT

Function

function

Catalyzes the reduction of hydroxylamine to form NH3 and H2O.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.
hybrid [4Fe-2O-2S] cluster (UniProtKB | Rhea| CHEBI:60519 )

Note: Binds 1 hybrid [4Fe-2O-2S] cluster.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site3[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site6[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site15[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site21[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site248hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site272hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site316hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site403hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI); via persulfide group
Binding site431hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site456hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site490hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site492hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionhydroxylamine reductase activity
Molecular Functionmetal ion binding
Molecular Functionperoxidase activity
Biological Processresponse to hydrogen peroxide

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Hydroxylamine reductase
  • EC number
  • Alternative names
    • Hybrid-cluster protein
      (HCP
      )
    • Prismane protein

Gene names

    • Name
      hcp
    • Ordered locus names
      Rru_A2759

Organism names

Accessions

  • Primary accession
    Q2RQN9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_10000091591-549Hydroxylamine reductase
Modified residue403Cysteine persulfide

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the HCP family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    549
  • Mass (Da)
    57,949
  • Last updated
    2006-01-24 v1
  • MD5 Checksum
    7554FCED7E66AE34ABB1A374765A2836
MYCYQCEQTAQGVACVTVGLCGKTAEVAALQDLLIEAAKGLSQYAYRLRQLGIALPEIDAFVLDALFTTVTNVSFDPARLEEQLREAACLRDQLRARYDAACAARHTSPETLSGPALWQPASTRAGLVGTGEAASIAHRLTAQGADLTGLQDLLLYGVKGMAAYACHARILGQTDESVAAFVHEVLTTLAEVPADAEALLGLVLRCGTVSLTVLDLLDRANTGAYGDPQPTPVLMGHRAGKAILVSGHDLKDLAVLLEQTVGLGVDIYTHGEMLPAHGYPELKKYPHLVGHYGGAWQRQRSEFAAFPGPILMTTNCIQNPTAAYRDRLFTCGLVAHPEATALSGRNFAPLIASALAAPGFAEDGPVRHHLAGFGHKAVLGVAPQIIDAVKAGAIRRFVLIGGCDGHESARSYFDDLAGSLPQDAVVLTLGCGKFRVIDHDMGTIAGLPRLLDMGQCNDAYSAIKVAQALAEAFGVGVNDLPLSLVLSWFEQKAVTVLLALLALGVRNIRLGPNLPAFITPPVLKVLVDRFGIMPVGTVAEDLAAMGLAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000230
EMBL· GenBank· DDBJ
ABC23556.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help