O05927 · CYSH_PSEAE
- ProteinAdenosine 5'-phosphosulfate reductase
- GenecysH
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids267 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.75 μM | 5'-adenylyl sulfate | 8.5 | 30 | |||
19.6 μM | thioredoxin | 8.5 | 30 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
5.8 μmol/min/mg | 8.5 | 30 | with thioredoxin as electron donor and 5'-adenylyl sulfate as substrate |
pH Dependence
Optimum pH is 8.5.
Pathway
Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 60 | adenosine 5'-phosphosulfate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 85 | adenosine 5'-phosphosulfate (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 139 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 140 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 144 | adenosine 5'-phosphosulfate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 161 | adenosine 5'-phosphosulfate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 228 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 231 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 242-245 | adenosine 5'-phosphosulfate (UniProtKB | ChEBI) | ||||
Sequence: REGR | ||||||
Active site | 256 | 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 | |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionO05927
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Cysteine auxotrophy.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 139 | Loss of activity. Contains essentially no iron. | ||||
Sequence: C → S | ||||||
Mutagenesis | 140 | Retains 3% of wild-type activity. Contains less iron and sulfide than the wild-type. Decreases stability of the iron-sulfur cluster. | ||||
Sequence: C → S | ||||||
Mutagenesis | 228 | Loss of activity. Contains essentially no iron. | ||||
Sequence: C → S | ||||||
Mutagenesis | 231 | Loss of activity. Contains essentially no iron. | ||||
Sequence: C → S | ||||||
Mutagenesis | 256 | Loss of activity. Has iron and sulfide contents very similar to those of the wild-type. Does not affect the stability of the iron-sulfur cluster. | ||||
Sequence: C → S |
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000100638 | 1-267 | Adenosine 5'-phosphosulfate reductase | |||
Sequence: MLPFATIPATERNSAAQHQDPSPMSQPFDLPALASSLADKSPQDILKAAFEHFGDELWISFSGAEDVVLVDMAWKLNRNVKVFSLDTGRLHPETYRFIDQVREHYGIAIDVLSPDPRLLEPLVKEKGLFSFYRDGHGECCGIRKIEPLKRKLAGVRAWATGQRRDQSPGTRSQVAVLEIDGAFSTPEKPLYKFNPLSSMTSEEVWGYIRMLELPYNSLHERGYISIGCEPCTRPVLPNQHEREGRWWWEEATHKECGLHAGNLISKA | ||||||
Disulfide bond | 140↔256 | Redox-active | ||||
Sequence: CGIRKIEPLKRKLAGVRAWATGQRRDQSPGTRSQVAVLEIDGAFSTPEKPLYKFNPLSSMTSEEVWGYIRMLELPYNSLHERGYISIGCEPCTRPVLPNQHEREGRWWWEEATHKEC |
Keywords
- PTM
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MLPFATIPATERNSAAQHQDPSPMS | ||||||
Compositional bias | 10-24 | Polar residues | ||||
Sequence: TERNSAAQHQDPSPM |
Domain
The two chemically discrete steps of the overall reaction take place at distinct sites on the enzyme, mediated via conformational flexibility of the C-terminal 18 residues.
Sequence similarities
Belongs to the PAPS reductase family. CysH subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length267
- Mass (Da)30,215
- Last updated2000-12-08 v2
- ChecksumE9557E1970F21049
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 1; AAB53743 | ||||
Sequence: L → P | ||||||
Compositional bias | 10-24 | Polar residues | ||||
Sequence: TERNSAAQHQDPSPM |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U95379 EMBL· GenBank· DDBJ | AAB53743.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE004091 EMBL· GenBank· DDBJ | AAG05145.1 EMBL· GenBank· DDBJ | Genomic DNA |