A0A2B7Y3H9 · A0A2B7Y3H9_POLH7
- ProteinSulfate adenylyltransferase
- GeneMET3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids573 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Catalytic activity
- sulfate + ATP + H+ = adenosine 5'-phosphosulfate + diphosphate
Activity regulation
Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS).
Pathway
Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 197 | sulfate (UniProtKB | ChEBI) | |||
Binding site | 197-200 | ATP (UniProtKB | ChEBI) | |||
Active site | 198 | ||||
Active site | 199 | ||||
Binding site | 199 | sulfate (UniProtKB | ChEBI) | |||
Active site | 200 | ||||
Site | 203 | Transition state stabilizer | |||
Site | 206 | Transition state stabilizer | |||
Binding site | 291-294 | ATP (UniProtKB | ChEBI) | |||
Binding site | 295 | sulfate (UniProtKB | ChEBI) | |||
Site | 330 | Induces change in substrate recognition on ATP binding | |||
Binding site | 333 | ATP (UniProtKB | ChEBI) | |||
Binding site | 434-437 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 515 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | adenylylsulfate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | sulfate adenylyltransferase (ATP) activity | |
Biological Process | cysteine biosynthetic process | |
Biological Process | hydrogen sulfide biosynthetic process | |
Biological Process | methionine biosynthetic process | |
Biological Process | sulfate assimilation via adenylyl sulfate reduction | |
Biological Process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSulfate adenylyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenales incertae sedis > Polytolypa
Accessions
- Primary accessionA0A2B7Y3H9
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-169 | N-terminal | |||
Domain | 4-164 | ATP-sulfurylase PUA-like | |||
Domain | 173-387 | Sulphate adenylyltransferase catalytic | |||
Region | 395-573 | Allosteric regulation domain; adenylyl-sulfate kinase-like | |||
Domain
The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme.
Sequence similarities
In the C-terminal section; belongs to the APS kinase family.
In the N-terminal section; belongs to the sulfate adenylyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length573
- Mass (Da)64,035
- Last updated2017-12-20 v1
- ChecksumB327927458FBB133
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
PDNA01000084 EMBL· GenBank· DDBJ | PGH15247.1 EMBL· GenBank· DDBJ | Genomic DNA |