P81186 · NAPA_DESDA
- ProteinPeriplasmic nitrate reductase
- GenenapA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids755 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
- 2 Fe(II)-[cytochrome] + 2 H+ + nitrate = 2 Fe(III)-[cytochrome] + H2O + nitrite
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [4Fe-4S] cluster.
Note: Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
Activity regulation
Activated by potassium and sodium ions and inhibited by magnesium and calcium ions.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
12 μM | nitrate | in the presence of NaCl | ||||
20 μM | nitrate | |||||
32 μM | nitrate | in the absence of NaCl |
pH Dependence
Optimum pH is between 8 and 9.5.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 45 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 48 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 52 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 79 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 81 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 143 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 168 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 172 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 208-212 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: NTSEA | ||||||
Binding site | 236-238 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: DPR | ||||||
Binding site | 255-257 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: GTD | ||||||
Binding site | 340 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 344 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 450 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 475-477 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: IEA | ||||||
Binding site | 647-656 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: SMRVIDHWHT | ||||||
Binding site | 648-653 | substrate | ||||
Sequence: MRVIDH | ||||||
Binding site | 721 | substrate | ||||
Sequence: F | ||||||
Binding site | 729 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 746 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | electron transfer activity | |
Molecular Function | iron ion binding | |
Molecular Function | molybdenum ion binding | |
Molecular Function | molybdopterin cofactor binding | |
Molecular Function | nitrate reductase (cytochrome) activity | |
Biological Process | Mo-molybdopterin cofactor biosynthetic process | |
Biological Process | nitrate assimilation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeriplasmic nitrate reductase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfovibrionia > Desulfovibrionales > Desulfovibrionaceae > Desulfovibrio
Accessions
- Primary accessionP81186
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | Tat-type signal | ||||
Sequence: MSTSRRDFLKYFAMSAAVAAASGAGFGSLALA | ||||||
Chain | PRO_0000019169 | 33-755 | Periplasmic nitrate reductase | |||
Sequence: ADNRPEKWVKGVCRYCGTGCGVLVGVKDGKAVAIQGDPNNHNAGLLCLKGSLLIPVLNSKERVTQPLVRRHKGGKLEPVSWDEALDLMASRFRSSIDMYGPNSVAWYGSGQCLTEESYVANKIFKGGFGTNNVDGNPRLCMASAVGGYVTSFGKDEPMGTYADIDQATCFFIIGSNTSEAHPVLFRRIARRKQVEPGVKIIVADPRRTNTSRIADMHVAFRPGTDLAFMHSMAWVIINEELDNPRFWQRYVNFMDAEGKPSDFEGYKAFLENYRPEKVAEICRVPVEQIYGAARAFAESAATMSLWCMGINQRVQGVFANNLIHNLHLITGQICRPGATSFSLTGQPNACGGVRDGGALSHLLPAGRAIPNAKHRAEMEKLWGLPEGRIAPEPGYHTVALFEALGRGDVKCMIICETNPAHTLPNLNKVHKAMSHPESFIVCIEAFPDAVTLEYADLVLPPAFWCERDGVYGCGERRYSLTEKAVDPPGQCRPTVNTLVEFARRAGVDPQLVNFRNAEDVWNEWRMVSKGTTYDFWGMTRERLRKESGLIWPCPSEDHPGTSLRYVRGQDPCVPADHPDRFFFYGKPDGRAVIWMRPAKGAAEEPDAEYPLYLTSMRVIDHWHTATMTGKVPELQKANPIAFVEINEEDAARTGIKHGDSVIVETRRDAMELPARVSDVCRPGLIAVPFFDPKKLVNKLFLDATDPVSREPEYKICAARVRKA |
Post-translational modification
Predicted to be exported by the Tat system (By similarity).
The position of the signal peptide cleavage has been experimentally proven (PubMed:9367852).
The position of the signal peptide cleavage has been experimentally proven (PubMed:9367852).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 38-93 | 4Fe-4S Mo/W bis-MGD-type | ||||
Sequence: EKWVKGVCRYCGTGCGVLVGVKDGKAVAIQGDPNNHNAGLLCLKGSLLIPVLNSKE |
Sequence similarities
Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length755
- Mass (Da)83,497
- Last updated2000-05-30 v2
- ChecksumD54BDB9D1FE21DC2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y18045 EMBL· GenBank· DDBJ | CAA77019.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ920046 EMBL· GenBank· DDBJ | CAI72603.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP001358 EMBL· GenBank· DDBJ | ACL48525.1 EMBL· GenBank· DDBJ | Genomic DNA |