Q9URY5 · FHP_SCHPO
- ProteinFlavohemoprotein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids427 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O2 and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress (By similarity).
In the presence of oxygen and NADH, it has NADH oxidase activity, which leads to the generation of superoxide and H2O2. Under anaerobic conditions, it also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity (By similarity).
Catalytic activity
- NADPH + 2 nitric oxide + 2 O2 = H+ + NADP+ + 2 nitrate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Note: Binds 1 heme b group per subunit.
Features
Showing features for site, binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 58 | Involved in heme-bound ligand stabilization and O-O bond activation | ||||
Sequence: Y | ||||||
Site | 113 | Influences the redox potential of the prosthetic heme and FAD groups | ||||
Sequence: K | ||||||
Binding site | 114 | Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue | ||||
Sequence: H | ||||||
Active site | 124 | Charge relay system | ||||
Sequence: Y | ||||||
Active site | 167 | Charge relay system | ||||
Sequence: E | ||||||
Binding site | 216 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 232-235 | FAD (UniProtKB | ChEBI) | ||||
Sequence: REYS | ||||||
Binding site | 301-306 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: GIGITP | ||||||
Site | 420 | Influences the redox potential of the prosthetic heme and FAD groups | ||||
Sequence: E | ||||||
Binding site | 421-424 | FAD (UniProtKB | ChEBI) | ||||
Sequence: FFGP |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | FAD binding | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | nitric oxide dioxygenase NAD(P)H activity | |
Molecular Function | oxygen binding | |
Biological Process | cellular detoxification of nitrogen compound | |
Biological Process | cellular response to nitrosative stress | |
Biological Process | nitric oxide catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFlavohemoprotein
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionQ9URY5
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000280219 | 1-427 | Flavohemoprotein | |||
Sequence: MSSVEVNRENADVANTNRQANLAEGYEIKELNESQKQYIRSSIPILESSGVNLTKAFYQKMLGNYPEVLPYFNKAHQISLSQPRILAFALLNYAKNIDDLTSLSAFMDQIVVKHVGLQIKAEHYPIVGHCLLSTMQELLPSDVATPAFLEAWTTAYGNLAKILIDSEKKVYQSQPWNGFVEFKVTELINESSDVKSVYLGPKDPAFRISHAHPGQYVSVLWEIPGLSHKTLREYSLSNRVDTCRNQFRISVRRVAGGVVSNFVHDNLKVGDIVGVSPPAGNFVYKRSEENVNRPLLCFAGGIGITPLIPIIETALLDGRKVNFCYSSRNYVSRPFKQWLEQLKLKYKENLKLKEFFSEESSVTKEQIVDEVMTRIINEEDLEKLDLSECDIYMLGPNNYMRFVKQELVKLGVEPNKVQSEFFGPYIP |
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-168 | Globin | ||||
Sequence: ELNESQKQYIRSSIPILESSGVNLTKAFYQKMLGNYPEVLPYFNKAHQISLSQPRILAFALLNYAKNIDDLTSLSAFMDQIVVKHVGLQIKAEHYPIVGHCLLSTMQELLPSDVATPAFLEAWTTAYGNLAKILIDSEK | ||||||
Region | 176-427 | Reductase | ||||
Sequence: WNGFVEFKVTELINESSDVKSVYLGPKDPAFRISHAHPGQYVSVLWEIPGLSHKTLREYSLSNRVDTCRNQFRISVRRVAGGVVSNFVHDNLKVGDIVGVSPPAGNFVYKRSEENVNRPLLCFAGGIGITPLIPIIETALLDGRKVNFCYSSRNYVSRPFKQWLEQLKLKYKENLKLKEFFSEESSVTKEQIVDEVMTRIINEEDLEKLDLSECDIYMLGPNNYMRFVKQELVKLGVEPNKVQSEFFGPYIP | ||||||
Domain | 177-285 | FAD-binding FR-type | ||||
Sequence: NGFVEFKVTELINESSDVKSVYLGPKDPAFRISHAHPGQYVSVLWEIPGLSHKTLREYSLSNRVDTCRNQFRISVRRVAGGVVSNFVHDNLKVGDIVGVSPPAGNFVYK |
Domain
Consists of two distinct domains; a N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H.
Sequence similarities
Belongs to the globin family. Two-domain flavohemoproteins subfamily.
In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length427
- Mass (Da)48,459
- Last updated2000-05-01 v1
- Checksum869E5D4578F309D6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329670 EMBL· GenBank· DDBJ | CAB60012.1 EMBL· GenBank· DDBJ | Genomic DNA |