A0A2J8BT29 · A0A2J8BT29_VERDA
- ProteinSulfate adenylyltransferase
- GeneMET3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids575 (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
- ATP + H+ + sulfate = 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 | 199 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 199-202 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QTRN | ||||||
Active site | 200 | |||||
Sequence: T | ||||||
Active site | 201 | |||||
Sequence: R | ||||||
Binding site | 201 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 202 | |||||
Sequence: N | ||||||
Site | 205 | Transition state stabilizer | ||||
Sequence: H | ||||||
Site | 208 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 293-296 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRDH | ||||||
Binding site | 297 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Site | 332 | Induces change in substrate recognition on ATP binding | ||||
Sequence: F | ||||||
Binding site | 335 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 436-439 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: ETVR | ||||||
Binding site | 517 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: R |
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 |
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
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Glomerellales > Plectosphaerellaceae > Verticillium
Accessions
- Primary accessionA0A2J8BT29
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer. Dimer of trimers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-171 | N-terminal | ||||
Sequence: MANTPHGGVLKDLFVRDAPRQAELLEESDKLPSLTLTERHLCDLELILNGGFSPLEGFLNEKDYNGVVKENRLADGSLFSMPINLDVSQQTIDEVGIKPGARITLRDLRDDRALAILTVEEVYKPNKNLEAQEVFGSPDDVTHPGIKHLLQVAQEFYVGGKLEAVQRLAHY | ||||||
Domain | 4-167 | ATP-sulfurylase PUA-like | ||||
Sequence: TPHGGVLKDLFVRDAPRQAELLEESDKLPSLTLTERHLCDLELILNGGFSPLEGFLNEKDYNGVVKENRLADGSLFSMPINLDVSQQTIDEVGIKPGARITLRDLRDDRALAILTVEEVYKPNKNLEAQEVFGSPDDVTHPGIKHLLQVAQEFYVGGKLEAVQR | ||||||
Domain | 175-389 | Sulphate adenylyltransferase catalytic | ||||
Sequence: DLRYTPAELRQHFEKLGWNKVVAFQTRNPMHRAHRELTVRASRSQQANVLIHPVVGLTKPGDIDHFTRVRVYKALLPRYPNGMAALALLPLAMRMGGPREAIWHAIIRKNHGATHFIVGRDHAGPGKNKDGKDWYGAYDAQIAVQKYQEELGIKMVEFQEMIYIPDRDEYQPANEIAPGTHTANISGTELRNRLKTGKEIPAWFSYPEVVKVLRE | ||||||
Region | 397-575 | Allosteric regulation domain; adenylyl-sulfate kinase-like | ||||
Sequence: KGFTIFLTGFQNSGKDQIARALQLILNQGGGRSVSLLLGETVRHELSAELGFSREDRSKNVARIAFVASELTRAGAAVIAAPIAPYEDARSQARELIEKAGPFFLVHVATSLEYSEKTDRRGVYQKARAGEIKGFTGVDDPYEVPAKADLTVDIEKQSVRSAVHQIILLLESQGLLDRI |
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
- Length575
- Mass (Da)64,127
- Last updated2018-03-28 v1
- ChecksumEE5C61BFB4088134
Keywords
- Technical term