A0A9X9HVP9 · A0A9X9HVP9_NEISU
- ProteinSulfite reductase [NADPH] flavoprotein alpha-component
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids596 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
function
Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component.
Catalytic activity
- 3 H2O + hydrogen sulfide + 3 NADP+ = 4 H+ + 3 NADPH + sulfite
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Note: Binds 1 FMN per subunit.
Pathway
Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen sulfide from sulfite (NADPH route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 64-69 | FMN (UniProtKB | ChEBI) | ||||
Sequence: SQTGNA | ||||||
Binding site | 111-114 | FMN (UniProtKB | ChEBI) | ||||
Sequence: STQG | ||||||
Binding site | 147-156 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LGDSSYPNFC | ||||||
Binding site | 319 | FAD (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 353 | FAD (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 383-386 | FAD (UniProtKB | ChEBI) | ||||
Sequence: RLYS | ||||||
Binding site | 401-403 | FAD (UniProtKB | ChEBI) | ||||
Sequence: TVG | ||||||
Binding site | 416-419 | FAD (UniProtKB | ChEBI) | ||||
Sequence: GVAS | ||||||
Binding site | 516-517 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: SR | ||||||
Binding site | 522-526 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: KVYVQ | ||||||
Binding site | 558 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 596 | FAD (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | sulfite reductase (NADPH) activity | |
Biological Process | cysteine biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSulfite reductase [NADPH] flavoprotein alpha-component
- EC number
- Short namesSiR-FP
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Neisseriales > Neisseriaceae > Neisseria
Accessions
- Primary accessionA0A9X9HVP9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Subunit
Alpha8-beta8. The alpha component is a flavoprotein, the beta component is a hemoprotein.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 58-196 | Flavodoxin-like | ||||
Sequence: VLVLSASQTGNARSVAESLHAKLQAAGVEARLSSASDFKSKTLPDGDIVLLVTSTQGEGEPPEEALPLYKFIYGKKKPDLSKLTFAVLGLGDSSYPNFCQAGKDFDAKFAELGAGRLNDLGICDLEFQTDADAWIAAVV | ||||||
Domain | 230-445 | FAD-binding FR-type | ||||
Sequence: EKPYTAILSVRQKITSRDAEKDVEHIEIDLSGSGLHYQAGDALGVWPLNAGDLVQEILDLNQLSGNETVQLSDGRETDIRTALTESADITQNTPAFVQQYAELTNNEELKTIAADKAQLDAYLAATPPVGVFAAHLHPLDAQTLYSLFRPQTPRLYSIASAQDEVGEEVHLTVGVVRFNHHDHTYTGVASGYLGERLEEGSEIRVFVEPNPNFRLP |
Family and domain databases
Sequence
- Sequence statusComplete
- Length596
- Mass (Da)65,029
- Last updated2023-11-08 v1
- Checksum559CF7B49E76047A