A0A366XBF5 · A0A366XBF5_9RHOB

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

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 site129Cu cation Z2 (UniProtKB | ChEBI)
Binding site130Cu cation Z3 (UniProtKB | ChEBI)
Binding site178Cu cation Z2 (UniProtKB | ChEBI)
Binding site255Ca2+ 2 (UniProtKB | ChEBI)
Binding site258Ca2+ 2 (UniProtKB | ChEBI)
Binding site266Ca2+ 2 (UniProtKB | ChEBI)
Binding site272Ca2+ 2 (UniProtKB | ChEBI)
Binding site319Ca2+ 2 (UniProtKB | ChEBI)
Binding site321Cu cation Z1 (UniProtKB | ChEBI)
Binding site376Cu cation Z1 (UniProtKB | ChEBI)
Binding site427Cu cation Z3 (UniProtKB | ChEBI)
Binding site448Ca2+ 1 (UniProtKB | ChEBI)
Binding site463Ca2+ 1 (UniProtKB | ChEBI)
Binding site488Cu cation Z4 (UniProtKB | ChEBI)
Binding site578Cu cation A1 (UniProtKB | ChEBI)
Binding site613Cu cation A1 (UniProtKB | ChEBI)
Binding site613Cu cation A2 (UniProtKB | ChEBI)
Binding site615Cu cation A2 (UniProtKB | ChEBI)
Binding site617Cu cation A2 (UniProtKB | ChEBI)
Binding site617Cu cation A1 (UniProtKB | ChEBI)
Binding site621Cu cation A2 (UniProtKB | ChEBI)
Binding site624Cu 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
      DS909_03565

Organism names

  • Taxonomic identifier
  • Strain
    • C3M10
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Roseobacteraceae > Phaeobacter

Accessions

  • Primary accession
    A0A366XBF5

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
Domain534-635Cytochrome oxidase subunit II copper A binding
Region537-635COX2-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
    635
  • Mass (Da)
    70,074
  • Last updated
    2018-11-07 v1
  • Checksum
    0F65A009FEF4942A
MSDHENKLNVTRRGLLGATATGAVAAAAGVGSTLMSAKEASAAAKVALEPGELDDYYGFWSSGQTGELRILGVPSMREFMRVPVFNRCSATGWGQTNESRKILTEGLLPETKEFLAANGKEMYDNGDLHHPHMSFTDGVYDGRFIFMNDKANTRVARVRCDVMKCDKIIEIPNAMDIHGMRPQKYPRTGYVFANGEHEAPLVNDGKILDEPAEYVNIFTAIDGDEMEVAWQVIVSGNLDNTDCDYQGKYAFSTSYNSEMGMNLGEMTENEMDHVVVFNIKAIEAAVAAGKYEELNGVKVVDGRKNAGTNLTRYIPIPNSPHGVNAAPDKKHIMINGKLSPTVSVIDVTKVDALFESDADPRSAIVAEPQLGLGPLHTAFDNKGNAYTTLFLDSQVVKWDIAKAIESFAGSDVDPILDKVDVQYQPGHNSTSMGETADADGKWLISMNKFSKDRFLNVGPLKPENEQLIDISGDKMKVVHDGPTFAEPHDSIIVRRDIVNPVNVWDRNDPMWEEARKQAEADGVDLEDTPEEPIRDGNKVRVYMTSQAPTFSMEKFTVKQGDEVTVYVTNLDDVDDVTHGFCMANFGVAMEVGPMATASVTFIAERPGVHWFYCQWFCHALHMEMRGRMLVEPRAS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QOCE01000011
EMBL· GenBank· DDBJ
RBW60515.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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