A0A1Q5RDI8 · A0A1Q5RDI8_9BRAD

Function

function

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

Caution

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 site51[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site54[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site58[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site86[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site88Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site155Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site180Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site184Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site217-224Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site248-252Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site267-269Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site378Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site382Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site488Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site514-515Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site537Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site564Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site724-733Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site800substrate
Binding site808Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site825Mo-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
      AC629_36280

Organism names

  • Taxonomic identifier
  • Strain
    • NAS80.1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Nitrobacteraceae > Bradyrhizobium

Accessions

  • Primary accession
    A0A1Q5RDI8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-32
ChainPRO_501250231833-834Periplasmic 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
Domain44-1004Fe-4S Mo/W bis-MGD-type

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    834
  • Mass (Da)
    93,827
  • Last updated
    2017-04-12 v1
  • MD5 Checksum
    AF83AA21CB714B0003AC9B29CDE5B464
MTSPKLDRRQMLKLEAAAIAAAAAGMPAPALAANLVSERDNSELKWDKAACRFCGTGCSVMVATKDNRVVATHGDIKAEVNRGLNCVKGYFLSKIMYGHDRLTQPMLRKTNGKYDKNGDFTPVSWTEAFDIMEAKWKEAMKKRGPNGVAMFGSGQWTIWEGYAASKLFKAGFRTNNIDPNARHCMASAVAGMMRTFGIDEPAGCYDDIEATDAFVLWGSNMAEMHPILWTRVADRRLSAPHVRVAVLSTFEHRSFDLADIGMVFVPQTDLYILNAIANHIIKTGRVNKDFVNAHTIFRRGQTDIGYGLRPEHPLQKKATGAAKANDSTDMSYDEYVKFVSDYTLEKAAKMSGVPLNRLEALAELYADPKTKVVSFWTMGFNQHTRGVWCNNLVYNIHLLTGKISAPGNSPFSLTGQPSACGTAREVGTFSHRLPADMVVTNKAHRDHAEHLWLLPEGTIPDKPGAHAVLQSRMLKDGLINAYWVQVNNNLQAGPNANEETYPGFRNPDNFIVVSDAYPSVTALAADLILPTAMWVEKEGAYGNAERRTQFWHQLVNAPGEAKSDLWQLMEFSKRFKIEEVWPEELIAKKPDVRGKTLFDVLFKNGQVDKFPTSEIEEGYANEESKAFGFYVQKGLFEEYASFGRGHGHDLAPFDTYHRERGLRWPVVNGQETKWRFREGSDPYVKQGTDVQFYGYPDGKARIFALPYEPAAESPDNEYPFWLSTGRVLEHWHSGTMTRRVPELYKAFPEAVCFMHPDDAQEAKLRRGDEVKVVSRRGYIRARVETRGRDRPPRGLVFVPWFDESKLINKVTLDATDPISLQTDYKKCAVRIERV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LGHL01000214
EMBL· GenBank· DDBJ
OKO73807.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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