P49050 · NIA_PICAN
- ProteinNitrate reductase [NADPH]
- GeneYNR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids859 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Catalytic activity
- H2O + NADP+ + nitrite = H+ + NADPH + nitrate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD.
Note: Binds 1 heme group. The heme group is called cytochrome b-557.
Note: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 137 | Mo (UniProtKB | ChEBI) of Mo-molybdopterin (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 538 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 561 | Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 655-658 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RAYT | ||||||
Binding site | 672-676 | FAD (UniProtKB | ChEBI) | ||||
Sequence: LIKVY | ||||||
Binding site | 677 | FAD (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 687-689 | FAD (UniProtKB | ChEBI) | ||||
Sequence: IMT | ||||||
Binding site | 737 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 740 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 829-838 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: MLLVCGPPGM |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | FAD binding | |
Molecular Function | heme binding | |
Molecular Function | molybdenum ion binding | |
Molecular Function | molybdopterin cofactor binding | |
Molecular Function | nitrate reductase (NADPH) activity | |
Molecular Function | sulfite oxidase activity | |
Biological Process | nitrate assimilation | |
Biological Process | nitric oxide biosynthetic process | |
Biological Process | sulfur compound metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNitrate reductase [NADPH]
- EC number
- Short namesNR
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Pichiaceae > Ogataea
Accessions
- Primary accessionP49050
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000166044 | 1-859 | Nitrate reductase [NADPH] | |||
Sequence: MDSIVTEVTYGLEIKKIKDITELPFPVRQDSPLTEVLPTDLKTKDNFVARDPDLLRLTGSHPFNSEPPLTKLYDSGFLTPVSLHFVRNHGPVPYVPDENILDWEVSIEGMVETPYKIKLSDIMEQFDIYSTPVTMVCAGNRRKEQNMVKKGAGFNWGAAGTSTSLWTGCMLGDVIGKARPSKRARFVWMEGADNPANGAYRTCIRLSWCMDPERCIMIAYQQNGEWLHPDHGKPLRVVIPGVIGGRSVKWLKKLVVSDRPSENWYHYFDNRVLPTMVTPEMAKSDDRWWKDERYAIYDLNLQTIICKPENQQVIKISEDEYEIAGFGYNGGGVRIGRIEVSLDKGKSWKLADIDYPEDRYREAGYFRLFGGLVNVCDRMSCLCWCFWKLKVPLSELARSKDILIRGMDERMMVQPRTMYWNVTSMLNNWWYRVAIIREGESLRFEHPVVANKPGGWMDRVKAEGGDILDNNWGEVDDTVKQAERRPHIDEDLEMMCNREKMDVVIKYSEFEAHKDSETEPWFAVKGQVFDGSSYLEDHPGGAQSILMVSGEDATDDFIAIHSSFAKKLLPSMHLGRLEEVSSVTKVKSVEQNVKREVLLDPRKWHKITLAEKEVISSDSRIFKFDLEHSEQLSGLPTGKHLFLRLKDSSGKYVMRAYTPKSSNSLRGRLEILIKVYFPNREYPNGGIMTNLIENLQVGNQIEVKGPVGEFEYVKCGHCSFNNKPYQMKHFVMISGGSGITPTYQVLQAIFSDPEDRTSVQLFFGNKKVDDILLREELDHIQEKYPEQFKVDYSLSDLDHLPENWSGVRGRLTFDILDTYVRGKKMGEYMLLVCGPPGMNGVVENWCNARKLDKQYVVYF | ||||||
Disulfide bond | 383 | Interchain | ||||
Sequence: C |
Keywords
- PTM
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 502-578 | Cytochrome b5 heme-binding | ||||
Sequence: DVVIKYSEFEAHKDSETEPWFAVKGQVFDGSSYLEDHPGGAQSILMVSGEDATDDFIAIHSSFAKKLLPSMHLGRLE | ||||||
Domain | 602-713 | FAD-binding FR-type | ||||
Sequence: RKWHKITLAEKEVISSDSRIFKFDLEHSEQLSGLPTGKHLFLRLKDSSGKYVMRAYTPKSSNSLRGRLEILIKVYFPNREYPNGGIMTNLIENLQVGNQIEVKGPVGEFEYV |
Sequence similarities
Belongs to the nitrate reductase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length859
- Mass (Da)98,534
- Last updated1996-02-01 v1
- Checksum79569977B01E3967
Keywords
- Technical term