A0A1C7LTY9 · A0A1C7LTY9_GRIFR
- ProteinSulfate adenylyltransferase
- GeneMET3_1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids578 (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 | 215 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 215-218 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QTRN | ||||||
Active site | 216 | |||||
Sequence: T | ||||||
Active site | 217 | |||||
Sequence: R | ||||||
Binding site | 217 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 218 | |||||
Sequence: N | ||||||
Site | 221 | Transition state stabilizer | ||||
Sequence: H | ||||||
Site | 224 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 309-312 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRDH | ||||||
Binding site | 313 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Site | 348 | Induces change in substrate recognition on ATP binding | ||||
Sequence: F | ||||||
Binding site | 351 | ATP (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 438-441 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: DTIR | ||||||
Binding site | 523 | 3'-phosphoadenylyl sulfate (UniProtKB | ChEBI); allosteric inhibitor | ||||
Sequence: K |
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 > Basidiomycota > Agaricomycotina > Agaricomycetes > Polyporales > Grifolaceae > Grifola
Accessions
- Primary accessionA0A1C7LTY9
Proteomes
Subcellular Location
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-187 | N-terminal | ||||
Sequence: MANTPHGGILKDLVARDEPLRNNLKAEAATLPEILLTERQLCDLELIINGGFSPLEGFMNEADYKSVVDTLRLADGSLFPMPITLDVSREDIDALSIASGSRIVLRDPRDDEALAIITVDDIYQPDQVKEAIQVFGADDPAHPSVAYLRSKVKDFYVGGKVQAIQPQHTSTTLRSDVSSFAGLFETL | ||||||
Domain | 4-165 | ATP-sulfurylase PUA-like | ||||
Sequence: TPHGGILKDLVARDEPLRNNLKAEAATLPEILLTERQLCDLELIINGGFSPLEGFMNEADYKSVVDTLRLADGSLFPMPITLDVSREDIDALSIASGSRIVLRDPRDDEALAIITVDDIYQPDQVKEAIQVFGADDPAHPSVAYLRSKVKDFYVGGKVQAIQ | ||||||
Domain | 194-400 | Sulphate adenylyltransferase catalytic | ||||
Sequence: DTPSELRAHFKKVAWRKVVAFQTRNPMHRAHRELTVRAARQRQANVLIHPVVGLTKPGDVDHYTRVRVYEAIMAKYPNGMGHLALLPLAMRMAGPREAVWHAIIRKNFGATHFIVGRDHAGPGKNSQGKDFYGPYDAQDLVMKYHEELQIEMVPFQQMTYLPSSDEYQPIDEVPKGVQTLDISGTELRRRLKTGAPIPDWFSYDAVG | ||||||
Region | 400-578 | Allosteric regulation domain; adenylyl-sulfate kinase-like | ||||
Sequence: GFVIFLTGLHNSGKDTIAKALQVTLNQQGGRSVSLLLGDTIRPDLDIPFTNGPEERSKDLQRLGFVAAELARAGAAVIVAPVAPKQASRDTIKSTVNHSAGAGANLFTIHVATPLEHCEATDRKNVYVRARKGEINGVAGVDEVFETPERPELTVDVTSQSVPEIVHSIVLLLETNSLL |
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
- Length578
- Mass (Da)63,611
- Last updated2016-11-30 v1
- ChecksumE31B450C9B8C1CBD
Keywords
- Technical term