A0A6I3SC05 · A0A6I3SC05_9BURK

Function

function

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

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site52[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site55[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site59[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site87[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site89Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site156Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site181Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site185Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site421Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site425Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site531Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site579Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site606Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site810-819Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site886substrate
Binding site894Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site911Mo-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
    • ORF names
      GMD42_07325

Organism names

  • Taxonomic identifier
  • Strain
    • BIOML-A2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Sutterellaceae > Parasutterella

Accessions

  • Primary accession
    A0A6I3SC05

Proteomes

Subcellular Location

Keywords

PTM/Processing

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

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    921
  • Mass (Da)
    103,172
  • Last updated
    2020-08-12 v1
  • Checksum
    DA2B4CAA6F516634
MTINNPQVKRRDLLKAGVAASAAMTVGIPLSEVAKAAVQSSEGAIVWTKGVCRFCGTGCGLQVGVKDGRVVATKGDPDAPVNKGLNCIKGYFNAKILYGKDRLTQPLMRRTNGKFDKNGKFEAVTWDEALTEMANQFKRVYKEKGPTGVAILGSGQYTIPEAYAASKLVKAGWRSNNIDPNARLCMASAVVGFYQVFGIDEPANNYSDIEKCNTMVLWGNNMAEAHPVLWSRVADRKLTHKETKIINLTTYKNMSSNMADETIIFAPNGDLAILNYILREIVHRDAIDHDFVNKHCIFAAGGMDIGYGMRPTDKFVFPKEKDIQAKQNAIILSKEEAIAQSRPELAGKEVKQTQQGGKAGAHWSISFEDFKKGVEPYTLDFTAQIAKGDPDESLEDFKKKLKNLADIYIDKKNDILSFWCMGFNQHQRGVWVNELIYSVHLLLAKHARPGNGAFSLTGQPSACGSAREVGTFCHRLPSDLLVAQKPARVKSEKIWGVPEKTINPKVGRAYMEILRGMEDNSVNFVWTQVVNPFQAAPNSNHWLKAARHPENFVVVADAYPTFSCQYADLILPAAMIFEKWGLYGNAERRTQGWQQMANPPGEARTDLWMMMEFAKRLQVKDCWGEQPVPGLKVDGYTDGKLPSVLDEAEKMGIKPDMTLYDVLFARPDNLKVAWPDPDLVSKINSTTAPGNLNWFPEKALFNEYRKFTLGDGHDLADFTTYMNSETRGLIWPVVNGKETLYRFNQDYDPYVKEGGYAFYGKLFKAIPTGNLFGVTDPKPVPLPNKAKIFFRPYAAPVEQPDKEYDLWLCTGRILEHWHTGSMTMRVPELERAQANSFLYMNPKDAEKRGLKNGDVAVCESRRGQVKAIVQTNQRNFMPRGMTWLAFFDRKVQTNQVVIDATDPISEEPDFKKSAVKVYKAQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WNCL01000018
EMBL· GenBank· DDBJ
MTU43434.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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