A0A4R9X2G4 · A0A4R9X2G4_9HYPH

Function

function

Nitrous-oxide reductase is part of a bacterial respiratory system which is activated under anaerobic conditions in the presence of nitrate or nitrous oxide.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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 2 calcium ions per subunit.
Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds 6 Cu cations per subunit. Each subunit contains 2 copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site of nitrous oxide reduction.

Pathway

Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 4/4.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site138Cu cation Z2 (UniProtKB | ChEBI)
Binding site139Cu cation Z3 (UniProtKB | ChEBI)
Binding site187Cu cation Z2 (UniProtKB | ChEBI)
Binding site328Cu cation Z1 (UniProtKB | ChEBI)
Binding site383Cu cation Z1 (UniProtKB | ChEBI)
Binding site434Cu cation Z3 (UniProtKB | ChEBI)
Binding site495Cu cation Z4 (UniProtKB | ChEBI)
Binding site584Cu cation A1 (UniProtKB | ChEBI)
Binding site619Cu cation A1 (UniProtKB | ChEBI)
Binding site619Cu cation A2 (UniProtKB | ChEBI)
Binding site621Cu cation A2 (UniProtKB | ChEBI)
Binding site623Cu cation A2 (UniProtKB | ChEBI)
Binding site623Cu cation A1 (UniProtKB | ChEBI)
Binding site627Cu cation A2 (UniProtKB | ChEBI)
Binding site630Cu cation A1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmembrane
Cellular Componentperiplasmic space
Molecular Functioncalcium ion binding
Molecular Functioncopper ion binding
Molecular Functioncytochrome-c oxidase activity
Molecular Functionnitrous-oxide reductase activity
Biological Processdenitrification pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nitrous-oxide reductase
  • EC number
  • Alternative names
    • N(2)OR
    • N2O reductase

Gene names

    • Name
      nosZ
    • ORF names
      EN859_030060

Organism names

Accessions

  • Primary accession
    A0A4R9X2G4

Proteomes

Subcellular Location

Keywords

PTM/Processing

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Interaction

Subunit

Homodimer.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain540-641Cytochrome oxidase subunit II copper A binding
Region543-641COX2-like

Sequence similarities

Belongs to the NosZ family.
In the C-terminal section; belongs to the cytochrome c oxidase subunit 2 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    641
  • Mass (Da)
    70,601
  • Last updated
    2019-07-31 v1
  • Checksum
    F34703EA3D4611F8
MSEEEHKTTLSRRQLLGTSAIVAAAGATGIGGTLTLGGSMVSPAAAQSAASGGQKFEIMPGELDEYYVFFSSGQTGEIRIVGAPSMRELMRIPVFNRCSATGWGLTNESRKVLTEGLLPETKEFLKDKGGIYLNGDLHHPHLSFTDGTYDGRYLFANDKANTRVARIRLDVMKCDKIIQLPNQHTVHGLRVQKYPKTGYVFCNGEDRVPIPNDGKVLDDKTKYHAIFTAVDGETMNVAWQVMVDGNLDNVDADYQGKYCYATSYNSEEGVNLAETMAKEQDWVVIFNLKRIEQAVARGDFKEIGGVPVIDGRHGSPYTRYVPVPNSPHGINTAPDGIHVVANGKLSPTCTVFDVRKFDDLFDDKIKPRDTVVAEPQLGLGPLHTAFDGRGNAYTTLFIDSQICKWNIDDAKRSFAGESVDPIRQKLDVHYQPGHNHASMGQTKEADGKWLISLNKFSKDRFLNVGPLKPENDQLIDISGDTMALVHDGPSFAEPHDATLVHRSKINPVSAWDRADPFFADAVKQATADGIDLLSDSQVIRDGNKVRVYMTSAAPAFGLESFTVKQGDEVTVYVTNIDEVEDLTHGFAIVNYGINMEVASQATASVTFTANRAGVYWYYCSWFCHAMHMEMQGRMFVEPQAA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SADR02000031
EMBL· GenBank· DDBJ
TGQ31468.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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