C1AUL1 · CYSH_RHOOB
- ProteinAdenosine 5'-phosphosulfate reductase
- GenecysH
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids247 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Catalytic activity
- [thioredoxin]-disulfide + AMP + 2 H+ + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate
RHEA-COMP:10700 CHEBI:50058 Position: n/n+3+ CHEBI:456215 + 2 CHEBI:15378 + CHEBI:17359 = RHEA-COMP:10698 CHEBI:29950 Position: nCHEBI:29950 Position: n+3+ CHEBI:58243
Cofactor
Note: Binds 1 [4Fe-4S] cluster per subunit.
Pathway
Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 133 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 134 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 216 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 219 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 242 | Nucleophile; cysteine thiosulfonate intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | adenylyl-sulfate reductase (thioredoxin) activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoadenylyl-sulfate reductase (thioredoxin) activity | |
Biological Process | cysteine biosynthetic process | |
Biological Process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenosine 5'-phosphosulfate reductase
- EC number
- Short namesAPS reductase
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Nocardiaceae > Rhodococcus
Accessions
- Primary accessionC1AUL1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000117931 | 1-247 | Adenosine 5'-phosphosulfate reductase | |||
Sequence: MSVDLSSATEGDLRELAARGAASLEGASARELLQWTEETFGSGASEGTGYRNSFIVASNMQDGVLVHLAAQVHPGVDVLFLDTGYHFAETIGTRDAVEQVYGVNVINARAEASVAEQDAAEGKDLFAREPNRCCALRKVAPLKKTLAGYKAWVTGIRRVEAPTRANAPLISFDDAFGLVKINPIAAWSDEDMQSYIDEHSILVNPLVDEGYPSIGCAPCTSKPAPGSDPRSGRWAGQAKTECGLHAS |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 222-247 | Disordered | ||||
Sequence: KPAPGSDPRSGRWAGQAKTECGLHAS |
Sequence similarities
Belongs to the PAPS reductase family. CysH subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length247
- Mass (Da)26,281
- Last updated2009-05-26 v1
- ChecksumCE003F53096FA310
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP011115 EMBL· GenBank· DDBJ | BAH49219.1 EMBL· GenBank· DDBJ | Genomic DNA |