A0A6A5U1C1 · A0A6A5U1C1_9PLEO
- ProteinSulfate adenylyltransferase
- GeneMET3
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids592 (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 | 216 | sulfate (UniProtKB | ChEBI) | |||
Binding site | 216-219 | ATP (UniProtKB | ChEBI) | |||
Active site | 217 | ||||
Active site | 218 | ||||
Binding site | 218 | sulfate (UniProtKB | ChEBI) | |||
Active site | 219 | ||||
Site | 222 | Transition state stabilizer | |||
Site | 225 | Transition state stabilizer | |||
Binding site | 310-313 | ATP (UniProtKB | ChEBI) | |||
Binding site | 314 | sulfate (UniProtKB | ChEBI) | |||
Site | 349 | Induces change in substrate recognition on ATP binding | |||
Binding site | 352 | ATP (UniProtKB | ChEBI) | |||
Binding site | 453-456 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | |||
Binding site | 534 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Pleosporomycetidae > Pleosporales > Massarineae > Massarinaceae > Byssothecium
Accessions
- Primary accessionA0A6A5U1C1
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer. Dimer of trimers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-188 | N-terminal | |||
Domain | 4-57 | ATP-sulfurylase PUA-like | |||
Domain | 71-183 | ATP-sulfurylase PUA-like | |||
Domain | 194-406 | Sulphate adenylyltransferase catalytic | |||
Region | 414-592 | 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.
Family and domain databases
Sequence
- Sequence statusComplete
- Length592
- Mass (Da)66,152
- Last updated2020-06-17 v1
- ChecksumF878A1C950B80015
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ML976986 EMBL· GenBank· DDBJ | KAF1958635.1 EMBL· GenBank· DDBJ | Genomic DNA |