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A0A9X5PLP5 · A0A9X5PLP5_9NEIS

Function

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:
Cu+ (UniProtKB | Rhea| CHEBI:49552 )

Note: Binds 1 Cu+ ion.
Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 1 Cu+ ion.
FAD (UniProtKB | Rhea| CHEBI:57692 )

Pathway

Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 2/4.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site135Cu cation 1 (UniProtKB | ChEBI); type 1 copper site
Binding site140Cu cation 1 (UniProtKB | ChEBI); type 1 copper site
Binding site175Cu cation 1 (UniProtKB | ChEBI); type 1 copper site
Binding site176Cu cation 1 (UniProtKB | ChEBI); type 1 copper site
Binding site184Cu cation 1 (UniProtKB | ChEBI); type 1 copper site
Binding site189Cu cation 1 (UniProtKB | ChEBI); type 1 copper site
Binding site330Cu cation 1 (UniProtKB | ChEBI); type 1 copper site

GO annotations

AspectTerm
Cellular Componentcell outer membrane
Cellular Componentperiplasmic space
Molecular Functioncopper ion binding
Molecular Functionnitrite reductase (NO-forming) activity
Biological Processnitrate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Copper-containing nitrite reductase
  • EC number

Gene names

    • ORF names
      HMPREF3052_05580

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HMSC056A03
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Neisseriaceae > Neisseria

Accessions

  • Primary accession
    A0A9X5PLP5

Proteomes

Subcellular Location

Cell outer membrane
; Lipid-anchor
Periplasm

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-17
ChainPRO_504101795018-385Copper-containing nitrite reductase

Interaction

Subunit

Homotrimer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region30-53Disordered
Compositional bias36-50Polar residues
Domain88-199Plastocyanin-like
Domain207-335Plastocyanin-like

Sequence similarities

Belongs to the multicopper oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    385
  • Mass (Da)
    40,501
  • Last updated
    2023-11-08 v1
  • MD5 Checksum
    9EC7FC802397ACCBE78BFBAC8CA6D01E
MKRQTLAALIASVFALAACGEQAAKPAETPAATASAEAPAASNPQAAAETPSSELPVIDAIVTHAPEVPPPTDRDHPAKVRVKMETVEKTMTMEDGVEYHYWTFNGDVPGQMIRVREGDTVEVEFSNHPSSTVPHNVDFHAATGPGGGAEASFTAPGHTSTFSFKALQAGLYIYHCAVAPVGMHIANGMYGLILVEPKEGLPKVDKEFYIVQGDFYTKGKKGAQGLQPFDMDKAIAEQPEYVVFNGHVGSIAGDNALKAKTGETVRLYVGNGGPNLVSSFHVIGEIFDKVYVEGGKLINENVQSTVIPAGGAAMIEFKVDVPGSYTLVDHSIFRAFNKGALGQLKVEGDENPEIMTKKLSDTVYQPAGAATSAPAAASGASEAAK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias36-50Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LTSK01000061
EMBL· GenBank· DDBJ
OFO28634.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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