A0A6I0JJS2 · A0A6I0JJS2_BACUN

Function

function

Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process.

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:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 1 Ca2+ ion per monomer.
heme c (UniProtKB | Rhea| CHEBI:61717 )

Note: Binds 5 heme c groups covalently per monomer.

Pathway

Nitrogen metabolism; nitrate reduction (assimilation).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site116Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue
Binding site144heme c 1 (UniProtKB | ChEBI); covalent
Binding site147heme c 1 (UniProtKB | ChEBI); covalent
Binding site148Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue
Binding site182heme c 2 (UniProtKB | ChEBI); covalent
Binding site185heme c 2 (UniProtKB | ChEBI); covalent
Binding site186Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue
Binding site224heme c 3 (UniProtKB | ChEBI); covalent
Binding site227heme c 3 (UniProtKB | ChEBI); covalent
Binding site228Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue
Binding site230Ca2+ (UniProtKB | ChEBI)
Binding site231Ca2+ (UniProtKB | ChEBI)
Binding site231substrate
Binding site276Ca2+ (UniProtKB | ChEBI)
Binding site278Ca2+ (UniProtKB | ChEBI)
Binding site279substrate
Binding site290Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue
Binding site297heme c 4 (UniProtKB | ChEBI); covalent
Binding site300heme c 4 (UniProtKB | ChEBI); covalent
Binding site301Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue
Binding site315Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue
Binding site328heme c 5 (UniProtKB | ChEBI); covalent
Binding site331heme c 5 (UniProtKB | ChEBI); covalent
Binding site332Fe (UniProtKB | ChEBI) of heme c 5 (UniProtKB | ChEBI); axial binding residue
Binding site407Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentperiplasmic space
Molecular Functioncalcium ion binding
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionnitrite reductase (cytochrome, ammonia-forming) activity
Biological Processnitrate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome c-552
  • EC number
  • Alternative names
    • Ammonia-forming cytochrome c nitrite reductase
      (Cytochrome c nitrite reductase
      )

Gene names

    • Name
      nrfA
    • ORF names
      GAQ72_13765

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BIOML-A38
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides

Accessions

  • Primary accession
    A0A6I0JJS2

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-32Helical

Keywords

Family & Domains

Features

Showing features for coiled coil.

TypeIDPosition(s)Description
Coiled coil340-367

Sequence similarities

Belongs to the cytochrome c-552 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    494
  • Mass (Da)
    56,158
  • Last updated
    2020-08-12 v1
  • Checksum
    3A4FB03BC07320B3
MEKRLKSWQGWLLFGGSMVVVFVLGLCVSALMERRAELASVFNNRKTVIEGIEARNEVFKSDFPREYQTWTETAKTDFQSEFNGNVAVDVLEQRPEMVILWAGYAFSKDYSTPRGHMHAIEDITATLRTGAPATDADGPQPSTCWTCKSPDVPRMMEAIGVDAFYNNKWGALGGEIVNPIGCADCHEPENMNLHISRPALIEAFERQGKDITEATPQEMRSLVCAQCHVEYYFKGDGKYLTFPWDKGFTVEDMEAYYDEAGFYDYIHKLSRTPILKAQHPDFEIARMGIHGQRGVSCADCHMPYKSEGGVKFSDHHIQSPLAMIDRTCQTCHRESEETLCNNVYERQRKANEIRNRLEQELAKAHIEAKFAWDKGATEEQMKEVLALIRQAQWRWDFGVASHGGAFHAPQEIQRVLSHGLDRAMQARLAVSKVLAKHGYTDNVPMPDISTKAKAQQYIGLDMEAEQQAKQKFLETVIPQWQEEARANKRFIEGN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WCUR01000049
EMBL· GenBank· DDBJ
KAB4114747.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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