A0A3L7AZH7 · A0A3L7AZH7_9ACTN
- Proteinassimilatory sulfite reductase (ferredoxin)
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids855 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.
Catalytic activity
- 3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] = 7 H+ + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [4Fe-4S] cluster per subunit.
Note: Binds 1 siroheme per subunit.
Pathway
Nitrogen metabolism; nitrate reduction (assimilation).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 624 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 630 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 664 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 668 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 668 | Fe (UniProtKB | ChEBI) of siroheme (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | heme binding | |
Molecular Function | metal ion binding | |
Molecular Function | NADP binding | |
Molecular Function | sulfite reductase (ferredoxin) activity | |
Biological Process | nitrate assimilation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameassimilatory sulfite reductase (ferredoxin)
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Micromonosporales > Micromonosporaceae > Micromonospora
Accessions
- Primary accessionA0A3L7AZH7
Proteomes
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-278 | FAD/NAD(P)-binding | ||||
Sequence: DLVVIGNGMVGQRFVDALRARDPHGRWRVTVLAEEGRPAYDRVRLSAFFDGVDADALNLHTPHDGVQLRLGEPATAIDRERRVVSTATGEHRYDALVLATGSYPFVPPVPGADLPGVFVYRTLDDLAALRAYARGRRAGAVIGGGLLGLEAANALRLLGLRTDVVEFAPRLMPVQVDPAGGAMLRRYVEELGVRTHLGVATTAIRPGPDGSVAALELSDGHIVEAELVVVAAGIRPRDDLARAAGLPLGPRGGVLVDETCRSADEWIWAVGECA | ||||||
Domain | 315-380 | NADH-rubredoxin oxidoreductase C-terminal | ||||
Sequence: ATKLKLLGVDVASFGDAHGVTPGCLDVTFTDPATRVYAKLVLSDDARTLLGGVLVGDASAYPTLRA | ||||||
Domain | 411-458 | BFD-like [2Fe-2S]-binding | ||||
Sequence: VCSCNAVTRGDVDAAIAGGCADVPALKACTRAGTSCGSCVPMLKQLLD | ||||||
Domain | 543-604 | Nitrite/Sulfite reductase ferredoxin-like | ||||
Sequence: QRDGSYSVVPRIPGGEITPEKLIVIGEVARDFRLYTKITGGQRIDLFGARVEQLPQIWRRLV | ||||||
Domain | 615-751 | Nitrite/sulphite reductase 4Fe-4S | ||||
Sequence: GKALRTVKSCVGETWCRYGVQDSVGLAVALELRYRGLRAPHKIKSAVSGCARECAEARSKDFGVIATETGWNLYVGGNGGFRPRHADLFATDLSTEALISLIDRFLMYYIRTADRLQRTAAWIEAMDGGLDHLRSVI | ||||||
Region | 808-855 | Disordered | ||||
Sequence: LERGQPVPARGAPPPTAPGEERHGREREADDTDQRRQPVALGLPEVRR | ||||||
Compositional bias | 826-842 | Basic and acidic residues | ||||
Sequence: GEERHGREREADDTDQR |
Sequence similarities
Belongs to the nitrite and sulfite reductase 4Fe-4S domain family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length855
- Mass (Da)90,777
- Last updated2019-02-13 v1
- ChecksumA61CA58C99AA9E77
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 826-842 | Basic and acidic residues | ||||
Sequence: GEERHGREREADDTDQR |