Q6MSC7 · PURA_MYCMS
- ProteinAdenylosuccinate synthetase
- GenepurA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids432 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Catalytic activity
- GTP + IMP + L-aspartate = GDP + 2 H+ + N6-(1,2-dicarboxyethyl)-AMP + phosphate
Cofactor
Note: Binds 1 Mg2+ ion per subunit.
Pathway
Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 16-22 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GDEGKGK | ||||||
Active site | 17 | Proton acceptor | ||||
Sequence: D | ||||||
Binding site | 17 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 17-20 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: DEGK | ||||||
Binding site | 42-45 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: NAGH | ||||||
Binding site | 44 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 44-46 | GTP (UniProtKB | ChEBI) | ||||
Sequence: GHM | ||||||
Active site | 45 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 132 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 146 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners | ||||
Sequence: R | ||||||
Binding site | 226 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: Q | ||||||
Binding site | 241 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: T | ||||||
Binding site | 301-307 | substrate | ||||
Sequence: LNTGRPR | ||||||
Binding site | 305 | IMP (UniProtKB | ChEBI); ligand shared between dimeric partners; in other chain | ||||
Sequence: R | ||||||
Binding site | 307 | GTP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 333-335 | GTP (UniProtKB | ChEBI) | ||||
Sequence: LFD | ||||||
Binding site | 415-417 | GTP (UniProtKB | ChEBI) | ||||
Sequence: SVG |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | adenylosuccinate synthase activity | |
Molecular Function | GTP binding | |
Molecular Function | magnesium ion binding | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | IMP metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate synthetase
- EC number
- Short namesAMPSase ; AdSS
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Mycoplasmatota > Mollicutes > Mycoplasmataceae > Mycoplasma
Accessions
- Primary accessionQ6MSC7
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000224295 | 1-432 | Adenylosuccinate synthetase | |||
Sequence: MKNNYKSLVIVGSQWGDEGKGKITDYFSQKADVVVRFAGGDNAGHMIEFNNKRHKVTIIPSGVFNPKVKNIIGNGTVINLKSLVNEIKRLNESNISTDNVFVSDRAHLIFDWHALIDQLQEENRKENKIGTTKRGIGPTYADKAARYGIRICDFQNPNFKEILKENLDYHNQIITKVYNHEPLDFDVIYNESMTNYQFIKNNIIDSGYEVSNLINENKFVLFEGAQGVLLDIDHGTYPFVTSSNCSANNASIGTGIHNKQINKVLGIVKAYNTRVGSGAMVSEIKTELAHKLRERGREYGLNTGRPRRIGWLDLVALKYAIRVGGIDQLFLTLFDVLDTETKIKICTHYKLDGKIIDWFPASDYELKRCEPVYEELDGWNQDITKVTSFEELPINAQKYIKRIEEIVKVPFLGFSVGSDRKQTILIKGEFDD |
Interaction
Structure
Sequence
- Sequence statusComplete
- Length432
- Mass (Da)49,098
- Last updated2004-07-05 v1
- Checksum3DCC6894937C5A01
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX293980 EMBL· GenBank· DDBJ | CAE77463.1 EMBL· GenBank· DDBJ | Genomic DNA |