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HAMAP rule MF_03126

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_03126
Accession MF_03126
Dates 13-AUG-2010 (Created)
3-SEP-2024 (Last updated, Version 12)
Name Adenylosucc_synth_vert_basic
Scope(s) Eukaryota
Vertebrata
Template(s) P28650 (PURA1_MOUSE); P0A7D4 (PURA_ECOLI); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_03126 (Get profile general information and statistics)
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 Name=ADSSL1; Synonyms=ADSS1;

Comments [?]

FUNCTIONComponent 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 Reaction=IMP + L-aspartate + GTP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H(+); Xref=Rhea:RHEA:15753, ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053, ChEBI:CHEBI:58189; EC=6.3.4.4;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
PATHWAYPurine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the adenylosuccinate synthetase family.

Keywords [?]

Cytoplasm
GTP-binding
Ligase
Magnesium
Metal-binding
Nucleotide-binding
Purine biosynthesis

Gene Ontology [?]

GO:0004019; Molecular function:adenylosuccinate synthase activity
GO:0005525; Molecular function:GTP binding
GO:0000287; Molecular function:magnesium ion binding
GO:0044208; Biological process:'de novo' AMP biosynthetic process
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1;
PROSITE 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 /note="Proton acceptor" D
ACT_SITE 71 71 /note="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
MF_03127
Fusion Nter: None Cter: None



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