C1D9G3 · NAPA_LARHH

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 site53[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site56[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site60[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site88[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site90Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site157Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site182Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site186Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site219-226Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site250-254Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site269-271Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site379Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site383Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site489Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site515-516Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site538Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site565Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site729-738Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site805substrate
Binding site813Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site830Mo-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
      LHK_02081

Organism names

Accessions

  • Primary accession
    C1D9G3

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-34Tat-type signal
ChainPRO_100018636635-839Periplasmic 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.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain46-1024Fe-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
    839
  • Mass (Da)
    94,304
  • Last updated
    2009-05-26 v1
  • Checksum
    1C02424A6F70B510
MTLTRRDFIKANAAAAAATAAAVNLPLVPSMAQAATTDPATAGADIKWDKAACRFCGTGCSVLVGTKGGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGEDRLTKPLLRMKNGKFDKNGEFTPVTWKQAFDVMEEKFKTAMKAGGPEAVAMFGSGQWTIWEGYAAAKFMKAGLRSNNLDPNARHCMASAVVGFMRTFNMDEPMGCYDDIEKADAFVLWGSNMAEMHPILWSRITDRRLTHPDCQVHVLSTYEHRSFELADNKLVFGPQTDLAILNYIANHIIQTGAVNKDFIQKYCAFMKGDTDIGYGLRPTHPKQKAAKNPDSGKMDPITFEQFAAFVKPYTLEYTARTSCVPAERLKRLAELYADPKKKVVSFWTMGFNQHTRGTWANNLVYNIHLLTGKISTPGCGPFSLTGQPSACGTAREVGTFAHRLPADLVVMNPEHRKIAENIWKLPEGTIPPKMGLHAVAMQRALKDSKLKVYWQQCNNNMQAGPNINEEMYPGWRNPETFIIVSDPYPTVSAMAADLILPTAMWVEKEGAYGNAERRTQFWRQQVNAPGEAKSDLWQVVEFSKRFKVEEVWPAELVAKKPEYRGKTLYDVLFANGQVNKYKLDDMARQHGTAYHNEEARHVGFYLQKGLFEEYAAFGRGHGHDLALFDTYHKARGLRWPVVDGKETLWRYREGFDPYVKKGEGVRFYGQKDGRARIIALPFEPAAEVPDREYNMWLCTGRVLEHWHTGSMTRRVPELYRAVPDAQVFMHPADAELRGLKRGQQVKVISRRGEITLTLETRGRNKPPQGLVFIPFFDEGRLVNKLTLDATCPLSKETDYKKCAVKVVRA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001154
EMBL· GenBank· DDBJ
ACO75065.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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