N1P8M1 · N1P8M1_YEASC
- ProteinSulfate adenylyltransferase
- GeneMET3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids511 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
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 | 195 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 195-198 | ATP (UniProtKB | ChEBI) | ||||
Sequence: QTRN | ||||||
Active site | 196 | |||||
Sequence: T | ||||||
Active site | 197 | |||||
Sequence: R | ||||||
Binding site | 197 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 198 | |||||
Sequence: N | ||||||
Site | 201 | Transition state stabilizer | ||||
Sequence: H | ||||||
Site | 204 | Transition state stabilizer | ||||
Sequence: H | ||||||
Binding site | 289-292 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRDH | ||||||
Binding site | 293 | sulfate (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Site | 328 | Induces change in substrate recognition on ATP binding | ||||
Sequence: F | ||||||
Binding site | 331 | ATP (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionN1P8M1
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homohexamer. Dimer of trimers.
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-167 | N-terminal | ||||
Sequence: MPAPHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNGGFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTRIALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGDYYVGGSLEAIQLPQHY | ||||||
Domain | 3-162 | ATP-sulfurylase PUA-like | ||||
Sequence: APHGGILQDLIARDALKKNELLSEAQSSDILVWNLTPRQLCDIELILNGGFSPLTGFLNENDYSSVVTDSRLADGTLWTIPITLDVDEAFANQIKPDTRIALFQDDEIPIAILTVQDVYKPNKTIEAEKVFRGDPEHPAISYLFNVAGDYYVGGSLEAIQ | ||||||
Region | 168-393 | Catalytic | ||||
Sequence: DYPGLRKTPAQLRLEFQSRQWDRVVAFQTRNPMHRAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPNGIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKGVDFYGPYDAQELVESYKHELDIEVVPFRMVTYLPDEDRYAPIDQIDTTKTRTLNISGTELRRRLRVGGEIPEWFSYPEVVKILRESNPPRPK | ||||||
Domain | 172-386 | Sulphate adenylyltransferase catalytic | ||||
Sequence: LRKTPAQLRLEFQSRQWDRVVAFQTRNPMHRAHRELTVRAAREANAKVLIHPVVGLTKPGDIDHHTRVRVYQEIIKRYPNGIAFLSLLPLAMRMSGDREAVWHAIIRKNYGASHFIVGRDHAGPGKNSKGVDFYGPYDAQELVESYKHELDIEVVPFRMVTYLPDEDRYAPIDQIDTTKTRTLNISGTELRRRLRVGGEIPEWFSYPEVVKILRE | ||||||
Region | 394-511 | Required for oligomerization; adenylyl-sulfate kinase-like | ||||
Sequence: QGFSIVLGNSLTVSREQLSIALLSTFLQFGGGRYYKIFEHNNKTELLSLIQDFIGSGSGLIIPNQWEDDKDSVVGKQNVYLLDTSSSADIQLESADEPISHIVQKVVLFLEDNGFFVF |
Domain
The oligomerization domain is distantly related to APS kinases, but it is not functional and does not bind APS. It is required for oligomerization of the enzyme, although the oligomerization state has no effect on the catalytic activity of the enzyme.
Sequence similarities
Belongs to the sulfate adenylyltransferase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length511
- Mass (Da)57,725
- Last updated2013-06-26 v1
- ChecksumA1E7B994A9C24DFD