A0A4P6X4H4 · A0A4P6X4H4_HYDPS

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.

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 site139Cu cation Z2 (UniProtKB | ChEBI)
Binding site140Cu cation Z3 (UniProtKB | ChEBI)
Binding site188Cu cation Z2 (UniProtKB | ChEBI)
Binding site270Ca2+ 2 (UniProtKB | ChEBI)
Binding site273Ca2+ 2 (UniProtKB | ChEBI)
Binding site281Ca2+ 2 (UniProtKB | ChEBI)
Binding site287Ca2+ 2 (UniProtKB | ChEBI)
Binding site340Ca2+ 2 (UniProtKB | ChEBI)
Binding site342Cu cation Z1 (UniProtKB | ChEBI)
Binding site398Cu cation Z1 (UniProtKB | ChEBI)
Binding site450Cu cation Z3 (UniProtKB | ChEBI)
Binding site471Ca2+ 1 (UniProtKB | ChEBI)
Binding site486Ca2+ 1 (UniProtKB | ChEBI)
Binding site511Cu cation Z4 (UniProtKB | ChEBI)
Binding site590Cu cation A1 (UniProtKB | ChEBI)
Binding site625Cu cation A1 (UniProtKB | ChEBI)
Binding site625Cu cation A2 (UniProtKB | ChEBI)
Binding site627Cu cation A2 (UniProtKB | ChEBI)
Binding site629Cu cation A2 (UniProtKB | ChEBI)
Binding site629Cu cation A1 (UniProtKB | ChEBI)
Binding site633Cu cation A2 (UniProtKB | ChEBI)
Binding site636Cu 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
      HPF_17320

Organism names

Accessions

  • Primary accession
    A0A4P6X4H4

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
Domain548-644Cytochrome oxidase subunit II copper A binding
Region549-644COX2-like

Sequence similarities

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

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    644
  • Mass (Da)
    70,409
  • Last updated
    2019-07-31 v1
  • Checksum
    526D0F97845016D9
MKDDSISNDQDRAAWGRRKFLNTAALAGLSIGAVACTDKSAGTAATPAAPAAPADAAHAASGAAAGHLKPGELDTYYGLWSGGHTGDMRVLGMPSGRELLRIPCFVPDALVGWGITNESKAIMGTKADGSLRYTVADTHHTHASYKDGNYDGRYAWINDKINSRLARIRLDYFVCDKITQLPNVQGFHGIFPDKADPVDPAINYTTRVFCGAEFSIPLPNTGTEDSSKYRSMFTCVDAESMEVRWQVLIDGNCDLTATSYDGKLAATNQYNIEMGAKYEDMMSAERDACLFFNIARIEEAVKAGKFKTVGTSKVPVVDGTHEANKDPKTALTAYVSVPKNPHGVNASPDGKYFICAGKLSPTATVIELSKVLEWFDGKLEKLDDAIVAEVELGLGPLHTAFDGRGNAYTTLFLDSQVVKWNVDAAIKFHAGDKAAKYVVDRIDVHYQPGHINASQSETKAADGKYLAVGCKFSKDRFLPVGPLHAENEQLIDISGEKMVLMGDHPVRGEPHDFIIFKRDLVKPKQVYSLDDFPNAVKDPKESGVFRNGKKVTVKMTSQAPAFSLREFKVKKGDEVTLILTNLDKIEDLTHGFAIPNYNVNFIVNPQETASVTFIADQPGVFWCYCTHFCHALHLEMRSRMIVEA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP037867
EMBL· GenBank· DDBJ
QBM29458.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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