J2UFR1 · J2UFR1_9PSED

  • Protein
    Nitrous-oxide reductase
  • Gene
    nosZ
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site130Cu cation Z2 (UniProtKB | ChEBI)
Binding site131Cu cation Z3 (UniProtKB | ChEBI)
Binding site179Cu cation Z2 (UniProtKB | ChEBI)
Binding site257Ca2+ 2 (UniProtKB | ChEBI)
Binding site260Ca2+ 2 (UniProtKB | ChEBI)
Binding site268Ca2+ 2 (UniProtKB | ChEBI)
Binding site274Ca2+ 2 (UniProtKB | ChEBI)
Binding site325Ca2+ 2 (UniProtKB | ChEBI)
Binding site327Cu cation Z1 (UniProtKB | ChEBI)
Binding site383Cu cation Z1 (UniProtKB | ChEBI)
Binding site434Cu cation Z3 (UniProtKB | ChEBI)
Binding site455Ca2+ 1 (UniProtKB | ChEBI)
Binding site470Ca2+ 1 (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 A1 (UniProtKB | ChEBI)
Binding site623Cu cation A2 (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
      PMI33_01042

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • GM67
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    J2UFR1

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 compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-19Basic and acidic residues
Region1-21Disordered
Domain540-639Cytochrome oxidase subunit II copper A binding
Region543-639COX2-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
    639
  • Mass (Da)
    71,248
  • Last updated
    2012-10-03 v1
  • Checksum
    9DC185E2DD0619E8
MTDTESTKPVQEEEHTGLSRRGFLGSSAVTGAVLAGATTLGGAVFSRESWAAAVKDAQAKTHVGPGELDEYYGFWSGGHQGEVRVLGVPSMRELMRIPVFNVDSATGWGLTNESKRIMGDSAKFQNGDCHHPHISMTDGKYDGKYLFINDKANSRIARIRLDIMKCDKMLTVPNVQAIHGLRLQKVPYTKYVFANAEFVIPHPNDGHTFDLQDKNSFTMFNAVDAEKMEMAFQVIVDGNLDNADMDYTGKYAASTCYNSEKAYDLGGMMRNERDWVVVFNIPRIEAAIKAGKFITLENSKVPVVDGRKTDGKDSEFTRYIPVPKNPHGLNTSSDGKYFIANGKLSPTVSMIAIDRLDDLFADKFKDPREVIAAEPELGLGPLHTTFDGRGNAYTTLFIDSQVVKWNMADAVRAYKGEKVNYIKQKLDVHYQPGHNHASLTETSEADGKWLVVLCKFSKDRFLPTGPLHPENDQLIDISGEEMKLVHDGPAFAEPHDCILARRDQIKTQKIWNRNDPFFAATVELAKKDGINLETDNKVIRDGNHVRVYMTSMAPAYGLTEFTVKQGNEVTVTITNIDQIEDVSHGFVMTNHGASMEISPQQTSSITFTADKAGLHWYYCSWFCHALHMEMVGRMKVERA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-19Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AKJH01000023
EMBL· GenBank· DDBJ
EJM91426.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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