Q87WW1 · Q87WW1_PSESM
- ProteinSulfate adenylyltransferase subunit 1
- GenecysN
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids632 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
APS kinase catalyzes the synthesis of activated sulfate.
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
Catalytic activity
- sulfate + ATP + H+ = adenosine 5'-phosphosulfate + diphosphate
Pathway
Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3.
Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 31-38 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GNVDDGKS | ||||||
Binding site | 34 | GDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 36 | GDP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 37 | GDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 38 | GDP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 39 | GDP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 83 | GDP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 110-114 | GTP (UniProtKB | ChEBI) | ||||
Sequence: DTPGH | ||||||
Binding site | 165 | GDP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 165-168 | GTP (UniProtKB | ChEBI) | ||||
Sequence: NKMD | ||||||
Binding site | 166 | GDP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 168 | GDP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 205 | GDP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 206 | GDP (UniProtKB | ChEBI) | ||||
Sequence: L |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | adenylylsulfate kinase activity | |
Molecular Function | ATP binding | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | guanosine tetraphosphate binding | |
Molecular Function | sulfate adenylyltransferase (ATP) activity | |
Biological Process | hydrogen sulfide biosynthetic process | |
Biological Process | phosphorylation | |
Biological Process | sulfate assimilation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSulfate adenylyltransferase subunit 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ87WW1
Proteomes
Interaction
Subunit
Heterodimer composed of CysD, the smaller subunit, and CysN.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-241 | Tr-type G | ||||
Sequence: KEMLRFLTCGNVDDGKSTLIGRLLHDSKMIYEDHLEAITRDSKKSGTTGDDVDLALLVDGLQAEREQGITIDVAYRYFSTAKRKFIIADTPGHEQYTRNMATGASTCDLAIILVDARYGVQTQTRRHSYIASLLGIKHIVVAINKMDLNGFDERVFESIKADYLKFAEGIAFKPTTMAFVPMSALKGDNVVNKSERSPWYAGQSLMEILETVEIASDRNY |
Sequence similarities
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
In the C-terminal section; belongs to the APS kinase family.
In the N-terminal section; belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length632
- Mass (Da)69,053
- Last updated2003-06-01 v1
- Checksum4EE729FBD73B23E4
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE016853 EMBL· GenBank· DDBJ | AAO57881.1 EMBL· GenBank· DDBJ | Genomic DNA |