A0A3D3FMU7 · A0A3D3FMU7_9SPIR

  • Protein
    Hydroxylamine reductase
  • Gene
    hcp
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the reduction of hydroxylamine to form NH3 and H2O.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site5[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site8[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site17[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site23[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site243hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site267hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site311hybrid [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 site491hybrid [4Fe-2O-2S] cluster (UniProtKB | ChEBI)
Binding site493hybrid [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

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
    • ORF names
      DIC34_08790

Organism names

  • Taxonomic identifier
  • Organism
    Treponema sp
  • Strain
    • UBA12037
  • Taxonomic lineage
    Bacteria > Spirochaetota > Spirochaetia > Spirochaetales > Treponemataceae > Treponema

Accessions

  • Primary accession
    A0A3D3FMU7

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue403Cysteine persulfide

Family & Domains

Sequence similarities

Belongs to the HCP family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    549
  • Mass (Da)
    58,687
  • Last updated
    2019-01-16 v1
  • Checksum
    57086C1915497E3C
MGMYCNQCEEAAKDTACTVRGVCGKDETVSNLQDVLIYALKGLSLVAVTARNAGVVDAAVSRVLVEGLFATITNANFDKAVFVARIREAIAVREELKKKLAARGIKLPANLHDSARFNPNTEIEMLDAWTSASFLAIENADVRALRSLVIFGLKGMAAYVEHAGNLGKRDRGIVEFAERALAATVDDGLDAAALTALVLETGKYGVDAMALLDGANTGAYGNPEPTTVQLGVRSNPGILISGHDLKDLEELLIQTAGSGVDVYTHGEMLPAHYYPGFKKFGNFVGNYGSAWWKQTEEFDAFNGPVLLTTNCLVPPKANYMARIFTTGESGFPGCVHIADREDGGTKDFSALIEMARTCAPPKELERGTITGGFAHAAVDAVAPAVVEAVKNGAIKRFFVMAGCDGRMKGRDYYTEFAEALPKDTVILTAGCAKFRYNKLNLGDICGIPRVLDAGQCNDSYSLALTALKLKDAFGVADVNDLPISFNIAWYEQKAVIVLLALLHLGFRNIHLGPTLPAFLSPNVVTVLVNNFGIAGIGSVEDDVKLFMGA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DPXI01000051
EMBL· GenBank· DDBJ
HCM26624.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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