A0A1W9XAF0 · A0A1W9XAF0_9GAMM

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 site44[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site47[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site51[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site79[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site81Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site148Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site173Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site177Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site260-262Mo-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 site806substrate
Binding site814Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site831Mo-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
      B6247_00190

Organism names

Accessions

  • Primary accession
    A0A1W9XAF0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-31
ChainPRO_501268750432-840Periplasmic 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
Domain37-934Fe-4S Mo/W bis-MGD-type

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    840
  • Mass (Da)
    94,284
  • Last updated
    2017-07-05 v1
  • Checksum
    756F5EB5AEDD3230
MKLTRRDFIKANAVAATAAAAGVTLPGTALADSTDDIRWDKAPCRFCGTGCSVMVGTKDNRVVAVKGDLDSPVNKGLLCVKGYFLPKIMYGDDRLTKPLLRMKNGEYDKNGEFTEISWDKAFDIMAEKWKKALKEKGPNGVGMFGSGQWTVWEGYAAVKLMKAGFRSNNIEPNARHCMASAVAAFIRTFGADEPMGCYDDLENADAFVLWGANMAECHPILWARLTDRRLMGENVKVAVLSTFKNRNFDLADLGIVFTPQTDLAILNYIAHYIIENGYVNEAFVSQQVNFRIGNADIGYGLRPEHPKEKAAKNASAAGGSKAATFEEYKEFVSEYSLDKVHELSGVPKEDLEALAQIYADPNIKVVSYWTMGFNQHTRGTWVNQLCYNVHLLTGKIAEPGNSPFSLTGQPTACGTAREVGTFAHRLPADLVAANPEHRAFAEKVWQLPEGAVADTPGYHAVLQNRKLKDGETNAYWVQCNNNLQAAPNLNEEGYPGYRNPDNFIVVSDPYPTLTGIGSDLILPTAMWVEKEGAYGNSERRTQFWRQQIKAPGESKSDVWQVVEFSKRFLAEEVWPEELMTKNPEYKGKTLYDILFANGAVDKYPKQEVKDAEGQVHPNDEMEHFGFYLQKGLYEEYRRFSLEGPKKGHELATFDQYHESRGLRWPVIQQGDGKPPQETLWRYNEKYDTLVEKGAGMQFYGNADGRANIFALPYEPPAEVPDDEYDMWLVTGRVLEHWMAGSMTRRVPELYRAYPDAVVYMHPKDARRRGLRRGMPAKLTSLRGEMIINVETRGRNRPPEGVIFVPFFDAGRLINKLTLDATCPLSKEADFKKCAVKVERA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NBMI01000001
EMBL· GenBank· DDBJ
OQY57410.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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