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HAMAP rule MF_03127

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General rule information [?]

Accession MF_03127
Dates 13-AUG-2010 (Created)
1-JUN-2023 (Last updated, Version 11)
Name Adenylosucc_synth_vert_acid
Scope(s) Eukaryota
Vertebrata
Template(s) P30520 (PURA2_HUMAN); P0A7D4 (PURA_ECOLI); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_03127 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PURA2
Protein name RecName: Full=Adenylosuccinate synthetase isozyme 2;
                 Short=AMPSase 2;
                 Short=AdSS 2;
                 EC=6.3.4.4;
AltName: Full=Adenylosuccinate synthetase, acidic isozyme;
AltName: Full=Adenylosuccinate synthetase, liver isozyme;
                 Short=L-type adenylosuccinate synthetase;
AltName: Full=IMP--aspartate ligase 2;
Gene name Name=ADSS; Synonyms=ADSS2;

Comments [?]

FUNCTIONPlays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
CATALYTIC ACTIVITY Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2- dicarboxyethyl)-AMP + phosphate; 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
case <FTGroup:1>
Acetylation
end case

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

Features [?]

From: PURA2_HUMAN (P30520)
Key From To Description Tag Condition FTGroup
case <OC:Mammalia>
INIT_MET 1 1 /note="Removed" M 1
CHAIN 2 Cter /note="Adenylosuccinate synthetase isozyme 2" 1
MOD_RES 2 2 /note="N-acetylalanine" A 1
end case
BINDING 39 45 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 G-D-E-G-K-G-K
BINDING 67 69 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 G-H-T
BINDING 362 364 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 K-L-D
BINDING 444 447 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 G-V-G-K
BINDING 40 43 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 D-E-G-K
BINDING 65 68 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 N-A-G-H
BINDING 330 336 /ligand="substrate" x-x-T-x-[KR]-x-R
ACT_SITE 40 40 /note="Proton acceptor" D
ACT_SITE 68 68 /note="Proton donor" H
BINDING 40 40 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 D
BINDING 67 67 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 G
BINDING 40 40 /ligand="substrate" D
BINDING 162 162 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 T
BINDING 176 176 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"		 R
BINDING 255 255 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 N
BINDING 270 270 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 T
BINDING 334 334 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 R
BINDING 336 336 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 R

Additional information [?]

Size range 451-457 amino acids
Related rules MF_03125
MF_03126
Fusion Nter: None Cter: None



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