A0A7U9QCG0 · A0A7U9QCG0_ECOLX

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 site46[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site49[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site53[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site81[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site83Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site150Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site175Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site179Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site212-219Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site243-247Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site262-264Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site372Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site376Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site482Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site508-509Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site531Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site558Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site718-727Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site794substrate
Binding site802Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site819Mo-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 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
      ECKIH15140_02733

Organism names

  • Taxonomic identifier
  • Strain
    • KIH15-140
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A7U9QCG0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-31
ChainPRO_503137735432-828Periplasmic 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
Domain39-954Fe-4S Mo/W bis-MGD-type

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    828
  • Mass (Da)
    93,027
  • Last updated
    2021-06-02 v1
  • Checksum
    FE94297F7E822758
MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITWDQAFDVMEEKFKTALKEKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGANMAEMHPILWSRITNRRLSNQDVTVAVLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFFSKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEYTLVKTAEMTGVPKDQLEQLAQLYADPNKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNEKHRDICEKKWNIPSGTIPAKIGLHAVAQDRALKDGKLNVYWTMCTNNMQAGPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEELLAKKPELRGKTLYEVLYATPEVSKFPVSELAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPVVNGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BJSI01000104
EMBL· GenBank· DDBJ
GEG55346.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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