B5FNQ2 · NAPA_SALDC

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 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 (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
    • Ordered locus names
      SeD_A2602

Organism names

Accessions

  • Primary accession
    B5FNQ2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-31Tat-type signal
ChainPRO_100018637032-828Periplasmic 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.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain39-954Fe-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
    828
  • Mass (Da)
    92,890
  • Last updated
    2008-10-14 v1
  • Checksum
    C6F99BC2D2509A82
MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPMLRMKDGSYHKDGEFTPVSWEQAFDVMEEKFKTSLKEKGPEAIGMFGSGQWTIWEGYAAAKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRITNRRLSDPNVKVAVLSTFQHRSFELADNGIVFTPQSDLVILNYIANYIIQNNAVNQDFFTKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFDEYKAFVAEYTLDKTAEMTGVPKDQLEQLAQLYADPNKRVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFSHRLPADMVVTNEKHRDICEKHWQIPAGTIPAKVGLHAVAQDRALKDGKLNVYWVMCNNNMQAGPNINEDRMPGWRDPRNFIIVSDPYPTVSALSADLILPTAMWVEKEGAYGNAERRTQFWRQQIKAPGEAKSDLWQLVQFSRRFKTEEVWPEALLSQKPELRGKTLYDVLFATPAVSKFPLSELKEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHNARGLRWPVVEGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAESPDNEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVVFIHPLDAKARDLRRGDKVKVSSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNNLTLDATDPLSKETDFKKCAVKLAKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001144
EMBL· GenBank· DDBJ
ACH76253.1
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