Q8EIJ1 · NAPA_SHEON

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:
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster.
Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | Rhea| CHEBI:60539 )

Note: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site45[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site48[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site52[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site80[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site82Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site149Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site174Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site178Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site211-218Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site261-263Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site371Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site375Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site481Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site507-508Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site530Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site557Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site716-725Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site792substrate
Binding site800Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site817Mo-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
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
    • Ordered locus names
      SO_0848

Organism names

Accessions

  • Primary accession
    Q8EIJ1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-32Tat-type signal
ChainPRO_000004600333-826Periplasmic 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.

Proteomic databases

Interaction

Subunit

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

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain38-944Fe-4S Mo/W bis-MGD-type

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    826
  • Mass (Da)
    92,475
  • Last updated
    2003-03-01 v1
  • Checksum
    33474D23868F6316
MSISRREFLKANAAVAAATAVGVTLPVKMVEAAESDNIKWDKAPCRFCGVGCSVLVGTKAGKVVATKGDPESPVNRGLNCIKGYFLSKIMYGKDRLTTPLLRMKDGKYHKEGEFTPVSWDVAFDTMAAKWKHSIATKGPTSVGMFGSGQWTIWEGYAASKLHKAGFLTNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDLEAADHFVLWGANMAEMHPILWARLSDRRLSSKDCRVHVLSTFENRSFDLADNPMVFHPQSDLVILNYIANYIIQNKAVNTDFVTKHTKFALGVDDIGYGLRPDHPLEKKAKNPGNGKSTPISFDEYAKFVSTYTLEYAAKMSGVEPEKLETLAKAYADPKAKVMSLWTMGINQHVRGVWANNMLYNIHLLTGKIATPGNSPFSLTGQPSACGTAREVGTFAHRLPADMVVDNDKHRAITEKMWQVPEGTIPPKPGYHAVLQSRMLKDGKLNCYWTMCTNNMQAGPNINEEMYPGFRNPENFIVVSDPYPTVTAMAADLILPTAMWVEKEGAYGNAERRTHMWHQQVKAPEGAKSDLWQLVEFSKRFKVAEVWPAELIAKKPEYADKTLYEVLFANGVINKFPTTDCKGDLNDESEHFSFYVQKGIFEEYAAFGRGHGHDLAEFDRYHETRGLRWPVVNDKETLRRFVEGSDPYVKAGEGYNFYGKPDGKAVIFALPYEPAAEEPNSEYDLWMSTGRVLEHWHTGSMTARVPELYRAYPDAQIFMHPEDAKARGLQRGDEVLVASPRGEIKTRVETKGRNKPPRGVVFMPFFDARQLVNKLILDATDPLSKETDFKKCPVKVMKA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014299
EMBL· GenBank· DDBJ
AAN53924.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp