A0A2A4NS30 · A0A2A4NS30_9FLAO

Function

function

Catalytic subunit of the 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 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 site150Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site175Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site179Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site261-263Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site363Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site367Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site472Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site497-498Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site520Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site547Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site664-673Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site740substrate
Binding site748Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)
Binding site765Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular region
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 ProcessMo-molybdopterin cofactor biosynthetic process
Biological Processnitrate assimilation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Nitrate reductase
  • EC number

Gene names

    • Name
      napA
    • ORF names
      COB98_09230

Organism names

Accessions

  • Primary accession
    A0A2A4NS30

Proteomes

Subcellular Location

Secreted
Note: Membrane-associated.

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-34
ChainPRO_501231414035-774Nitrate 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 nitrate reductase NapAB complex composed of NapA and NapB.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain46-1024Fe-4S Mo/W bis-MGD-type

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    774
  • Mass (Da)
    86,939
  • Last updated
    2017-12-20 v1
  • MD5 Checksum
    76C8D005BC9918B508EF07876F67EBF6
MVQKKIDRRLFVKKMAAVAAMTAAVNMFPGIVFASEQDQGIPAGNLSWKKGPCRFCGVGCGILVGVENGKAVAVKGDPNSSVNKGLLCVKGYHQIMCIQAKDRLKYALVKKNGKYVKTPLNEALDLVAEKMKSTIKNDGKDAVAMYTSGQSTIPEGYLASKLMKGAIGTNNLDCNARLCMASAVTGFMTTFGIDEPMGCYEDIDHADYFITWGNNMAEMHPVLFSRMLEQKNNRGAKIIDFATRTTRSSMASDKSILFEPQTDLAVANAICYEIINNGWVNRKFVENHTTFLKGKTNIGYGLEDNFTFKEEETKISFEDYTLFLEDYTPVKVAKYSGVSVKNIKYLAAIYGDPNKKVVSYWCMGMNQHTRGTWINNLVYNIHLLTGKISQPGNGPFSLTGQPSACGTAREVGTFTHRLPKGVVTKEKYRRLAAKIWKVPYENIPSKPTYHATEMFRAVDRGDIKFIWIQATNPLASLPKTSRYRPAMEKESCFVVVSDVFPTPTSDVADVILPAKWHIEKGGLYGNSERRTQYWQTMVEGPGETEADAWMTIEVARRMGYGHLFPYSKENHVEEIYEEYRQFHQGNKHGMAPIEVLKKQAGAMWPFVNGKSTKWRFNAAYDPACTNGKEFDFYGKPEGKAVIWQRPYEPAPELPDPEYPFLLSTGRVIEHWHTGSMTRRIPVLHRAMPHSYVEFHPEDAKKMGFINGEKVKVVSRRGSCILPVSINERGVPTRGQVFVPFFDENMLINDVTLDAFCPISKQPDYKKCAVKIVKV

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NVRM01000088
EMBL· GenBank· DDBJ
PCH75259.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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