A0A9P5T5L0 · A0A9P5T5L0_9FUNG
- ProteinSulfate adenylyltransferase
- GeneMET3
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids574 (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 | 198 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 198-201 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QTRN | ||||||
Active site | 199 | |||||
Sequence: T | ||||||
Active site | 200 | |||||
Sequence: R | ||||||
Binding site | 200 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 201 | |||||
Sequence: N | ||||||
Site | 204 | Transition state stabilizer | ||||
Sequence: H | ||||||
Site | 207 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 292-295 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRDH | ||||||
Binding site | 296 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Site | 331 | Induces change in substrate recognition on ATP binding | ||||
Sequence: F | ||||||
Binding site | 334 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 435-438 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: ETIR |
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 | 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 > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Mortierella
Accessions
- Primary accessionA0A9P5T5L0
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer. Dimer of trimers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-170 | N-terminal | ||||
Sequence: MANTPHGGILKDLVARDLPIRDQLLKEAETVPSIVLTERQLCDLELIISGGFSPLEGFLNQKDYNNVVENLRLANGTLWSIPINLDVAQEDIDTLSLKPAQRVALRDPRNDSPIAILTIEDIYKPDKVKEAKLVFGDDDLAHPSVKYIHQNVKDFYVGGSVQAIQPPTHY | ||||||
Domain | 4-165 | ATP-sulfurylase PUA-like | ||||
Sequence: TPHGGILKDLVARDLPIRDQLLKEAETVPSIVLTERQLCDLELIISGGFSPLEGFLNQKDYNNVVENLRLANGTLWSIPINLDVAQEDIDTLSLKPAQRVALRDPRNDSPIAILTIEDIYKPDKVKEAKLVFGDDDLAHPSVKYIHQNVKDFYVGGSVQAIQ | ||||||
Domain | 174-388 | Sulphate adenylyltransferase catalytic | ||||
Sequence: AYRNTPAEIRAYFQKLNWTRVVAFQTRNPMHRAHRELTVRAARSRQANVLINPVVGLTKPGDIDHFTRVRVYEAIIRRYPTGMAALSLLPLAMRMAGPREALWHAIIRKNHGCSHFIIGRDHAGPGKNSAGKDFYGPYDAQYLVEKYKDEIDIEVVPFQQVTYLPDSDEYVPSNEVPAGAKTLDISGTELRRRLRTGAHIPEWFSYPEVVALLRQ | ||||||
Region | 396-574 | Allosteric regulation domain; adenylyl-sulfate kinase-like | ||||
Sequence: QGFTVFLTGYHASKKEHIARALQVSLNQQGGRSISLLLGETIRGKLSSELGFSKRERDININRLGFVSAELTKAGAGVIVAPIAPYEDARQQARQEIEKVGGFFLIHVATPLEQCIAWDRDGIYERAKKGEITGFTGIDDPYETPKNADLVVDPSTESVAQIVRRIVLLLDKQGYFGDA |
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
- Length574
- Mass (Da)64,265
- Last updated2023-09-13 v1
- Checksum10673F4E10620D2A
Keywords
- Technical term