B5FNQ2 · NAPA_SALDC
- ProteinPeriplasmic nitrate reductase
- GenenapA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids828 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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] + nitrate + 2 H+ = 2 Fe(III)-[cytochrome] + nitrite + H2O
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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 49 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 53 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 81 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 83 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 150 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 175 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 179 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 212-219 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: WGSNMAEM | ||||||
Binding site | 243-247 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: STFQH | ||||||
Binding site | 262-264 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: QSD | ||||||
Binding site | 372 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 376 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 482 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 508-509 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: SD | ||||||
Binding site | 531 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 558 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 718-727 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: TGRVLEHWHT | ||||||
Binding site | 794 | substrate | ||||
Sequence: F | ||||||
Binding site | 802 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 819 | Mo-bis(molybdopterin guanine dinucleotide) (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | oxidoreductase complex | |
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 | cellular respiration | |
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 > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionB5FNQ2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | Tat-type signal | ||||
Sequence: MKLSRRSFMKANAVAAAAAAAGLSVPGVARA | ||||||
Chain | PRO_1000186370 | 32-828 | Periplasmic nitrate reductase | |||
Sequence: VVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPMLRMKDGSYHKDGEFTPVSWEQAFDVMEEKFKTSLKEKGPEAIGMFGSGQWTIWEGYAAAKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRITNRRLSDPNVKVAVLSTFQHRSFELADNGIVFTPQSDLVILNYIANYIIQNNAVNQDFFTKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFDEYKAFVAEYTLDKTAEMTGVPKDQLEQLAQLYADPNKRVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFSHRLPADMVVTNEKHRDICEKHWQIPAGTIPAKVGLHAVAQDRALKDGKLNVYWVMCNNNMQAGPNINEDRMPGWRDPRNFIIVSDPYPTVSALSADLILPTAMWVEKEGAYGNAERRTQFWRQQIKAPGEAKSDLWQLVQFSRRFKTEEVWPEALLSQKPELRGKTLYDVLFATPAVSKFPLSELKEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHNARGLRWPVVEGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAESPDNEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVVFIHPLDAKARDLRRGDKVKVSSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNNLTLDATDPLSKETDFKKCAVKLAKV |
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.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 39-95 | 4Fe-4S Mo/W bis-MGD-type | ||||
Sequence: IKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKD |
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.
- Length828
- Mass (Da)92,890
- Last updated2008-10-14 v1
- ChecksumC6F99BC2D2509A82
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001144 EMBL· GenBank· DDBJ | ACH76253.1 EMBL· GenBank· DDBJ | Genomic DNA |