A0A087FA63 · A0A087FA63_9PSED

  • Protein
    Periplasmic nitrate reductase
  • Gene
    napA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite.

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:
Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | Rhea| CHEBI:60539 )

Note: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site48[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site51[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site55[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site83[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site85Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site152Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site177Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site181Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site214-221Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site245-249Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site264-266Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site375Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site379Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site485Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site511-512Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site534Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site561Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site721-730Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site797substrate
Binding site805Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site822Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentoxidoreductase complex
Cellular Componentperiplasmic space
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionelectron transfer activity
Molecular Functioniron ion binding
Molecular Functionmolybdenum ion binding
Molecular Functionmolybdopterin cofactor binding
Molecular Functionnitrate reductase (cytochrome) activity
Biological Processcellular respiration
Biological ProcessMo-molybdopterin cofactor biosynthetic process
Biological Processnitrate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Periplasmic nitrate reductase
  • EC number

Gene names

    • Name
      napA
    • ORF names
      JF55_14325

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 1-7
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    A0A087FA63

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-29
ChainPRO_500882102230-834Periplasmic nitrate reductase

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

Component of the periplasmic nitrate reductase NapAB complex composed of NapA and NapB.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain41-974Fe-4S Mo/W bis-MGD-type

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    834
  • Mass (Da)
    93,686
  • Last updated
    2014-10-29 v1
  • Checksum
    52049AF725BE9792
MKLTRREFAKANAAAIAAAAAGLPLVTTASNLITEADMTRLDWNKAPCRFCGTGCSVMVATRDNRVVATHGDVKAEVNRGLNCVKGYFLSKIMYGVDRLNQPLLRMKNGVYDKQGEFQPVSWEQAFDIMEQKTKEALREHGPEAVGMFGSGQWTVWEGYAANKLMKAGFRSNNIDPNARHCMASAVMGFMRTFGMDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSHPNTKVAVLSTFEHRSFDLADIPLVFKPQTDLLILNYIANHIIESGAVNKDFVGKHTKFARGADDIGYGLRADNPLEMQAKNAAKANTWEDMSFEQFAAFVKPYTLERTARESGVAAERLKALAELYADPKRKVMSFWTMGFNQHTRGVWANNLIYNLHLLTSKISEPGNSPFSLTGQPSACGTAREVGTFSHRLPADMLVANPKHRATAEKIWKLPAGTIQEKPGFHAVEQSRKLKDGVLKVYWTQVSNNMQAGPNIMQEVLPGWRNPQAFVIVSDVYPTVSAQAADLILPSAMWVEKEGAYGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRFTTDEVWPAELLAKAPEYKGKTLYQVLFANGQVDQFPREQIEAGYANDEAEAFGFYLQKGLFEEYAQFGRGHAHDLAPFDSYHAERGLRWPVVDGKETRWRYREGLDPYVEKGSGVQFYGYPDKRALIFALPYEPPAESPDDDFPFWLSTGRVLEHWHTGSMTQRVEELHGAVPDALVYMHPDDARALKARRGSEVKVISRRGEIRARIETRGRNKPPRGLVFVPFFDANKLINKVTLDATDPISKQTDYKKCAVKIELVSLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JPRQ01000022
EMBL· GenBank· DDBJ
KFJ91228.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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