A0AAN1CYS9 · A0AAN1CYS9_VIBNA

Function

function

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

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 site374Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site378Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site484Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site510-511Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site533Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site560Mo-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 Componentmembrane
Cellular Componentnitrate reductase 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
      BA890_21925

Organism names

Accessions

  • Primary accession
    A0AAN1CYS9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-29
ChainPRO_504297445330-829Periplasmic 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
    829
  • Mass (Da)
    92,981
  • Last updated
    2024-10-02 v1
  • MD5 Checksum
    F4A11A17974CC7F6C4489ED001E2B0C9
MKMTRRAFVKANAAASAAAVAGITLPASAANLIASSDQSKITWDKAPCRFCGTGCSVLVGTQNGKVVATQGDPEAPVNKGLNCIKGYFLSKIMYGQDRLTQPLLRMKDGKYHKDGEFTPVSWDVAFDTMAEKWKASLEKKGPTSVGMFGSGQWTVMEGYAAAKMMKAGFRSNNIDPNARHCMASAVVGFMRAFGIDEPMGCYDDFENADAFVLWGSNMAEMHPVLWTRITDRRLSHPHVRVNVLSTYYHRSFELADHGYIFNPQSDLAIANFIANYIIENDAVNWDFVNKHTNFTQADTDIGYGLRDDDPLQKAAKNPNSGKLTAISFEEYKKSVAPYTVEKASEISGVEKEKLIELAKQYADPNTKVMSLWTMGMNQHTRGVWMNNLVYNIHLLTGKIATPGNSPFSLTGQPSACGTAREVGTFAHRLPADMVVANPKHREIAEKIWKLPEGTIPPKPGFHAVLQDRMLNDGVLNCYWVQCNNNMQAGPNINTERLPGYRNPENFIVVSDPYPTATAQAADLVLPTAMWIEKEGAYGNAERRTQAWYQQVGTVGEAKSDLWQVMEFAKRFKMEEVWPEELLAKAPEYRGKTMYDMLFKNGQVDKFPVEEARELNDDSHHFGYYVQKGLFEEYATFGRGHGHDLAPYDVYHTVRGLRWPVVDGKETQWRFKEGSDPYAKAGSGWDFYGNADGKAKIISAPYEAPPEMPDSEYDLWLCTGRVLEHWHTGTMTRRVPELYKAVPDAVCYMHPEDAKARNVRRGEEILIANKRGEVRARVETRGRNRPPQGLVFVPFFDARILINKLILDATDPLSKQTDFKKCPVKITKIA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP016346
EMBL· GenBank· DDBJ
ANQ15365.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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