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HAMAP rule MF_03126

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General rule information [?]

Accession MF_03126
Dates 13-AUG-2010 (Created)
1-JUN-2023 (Last updated, Version 10)
Name Adenylosucc_synth_vert_basic
Scope
Eukaryota; Vertebrata
Templates P28650 (PURA1_MOUSE); P0A7D4 (PURA_ECOLI): [Recover all]
case <OC:Eukaryota>
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
PURA1
Protein name
RecName: Full=Adenylosuccinate synthetase isozyme 1;
Short=AMPSase 1;
Short=AdSS 1;
EC 6.3.4.4;
AltName: Full=Adenylosuccinate synthetase, basic isozyme;
AltName: Full=Adenylosuccinate synthetase, muscle isozyme;
Short=M-type adenylosuccinate synthetase;
AltName: Full=IMP--aspartate ligase 1;
Gene name
ADSSL1, ADSS1

Comments [?]

Function Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
Catalytic activity RHEA:15753: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
EC 6.3.4.4
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
Pathway Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subunit Homodimer.
Subcellular location Cytoplasm.
Similarity Belongs to the adenylosuccinate synthetase family.

Keywords [?]


Gene Ontology [?]

GO:0004019; Molecular function: adenylosuccinate synthase activity.
GO:0005525; Molecular function: GTP binding.
GO:0000287; Molecular function: magnesium ion binding.
GO:0006164; Biological process: purine nucleotide biosynthetic process.
GO:0005737; Cellular component: cytoplasm.

Cross-references [?]

PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1;
PS00513; ADENYLOSUCCIN_SYN_2; 1;
Pfam PF00709; Adenylsucc_synt; 1;
NCBIfam TIGR00184; PurA; 1;

Features [?]

From: PURA1_MOUSE (P28650)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     42     48       /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565     G-D-E-G-K-G-K  
BINDING     70     72       /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565     G-H-T  
BINDING     363     365       /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565     K-L-D  
BINDING     445     448       /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565     G-V-G-K  
BINDING     43     46       /ligand="IMP" /ligand_id="ChEBI:CHEBI:58053     D-E-G-K  
BINDING     68     71       /ligand="IMP" /ligand_id="ChEBI:CHEBI:58053     N-A-G-H  
BINDING     331     337       /ligand="substrate     x-x-T-x-[KR]-x-R  
ACT_SITE     43     43       Proton acceptor     D  
ACT_SITE     71     71       Proton donor     H  
BINDING     43     43       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     D  
BINDING     70     70       /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420     G  
BINDING     43     43       /ligand="substrate     D  
BINDING     163     163       /ligand="IMP" /ligand_id="ChEBI:CHEBI:58053     T  
BINDING     177     177       /ligand="IMP" /ligand_id="ChEBI:CHEBI:58053" /ligand_note="ligand shared between dimeric partners     R  
BINDING     256     256       /ligand="IMP" /ligand_id="ChEBI:CHEBI:58053     N  
BINDING     271     271       /ligand="IMP" /ligand_id="ChEBI:CHEBI:58053     T  
BINDING     335     335       /ligand="IMP" /ligand_id="ChEBI:CHEBI:58053     R  
BINDING     337     337       /ligand="GTP" /ligand_id="ChEBI:CHEBI:37565     R  

Additional information [?]

Size range 449-459 amino acids
Related rules MF_03125 (PURA); MF_03127 (PURA2)
Fusion None