AC   MF_03126;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_03126; -; 1; level=0
XX
Names: Adenylosucc_synth_vert_basic
XX
ID   PURA1
DE   RecName: Full=Adenylosuccinate synthetase isozyme 1;
DE            Short=AMPSase 1;
DE            Short=AdSS 1;
DE            EC=6.3.4.4;
DE   AltName: Full=Adenylosuccinate synthetase, basic isozyme;
DE   AltName: Full=Adenylosuccinate synthetase, muscle isozyme;
DE            Short=M-type adenylosuccinate synthetase;
DE   AltName: Full=IMP--aspartate ligase 1;
GN   Name=ADSSL1; Synonyms=ADSS1;
XX
CC   -!- FUNCTION: Component of the purine nucleotide cycle (PNC), which
CC       interconverts IMP and AMP to regulate the nucleotide levels in various
CC       tissues, and which contributes to glycolysis and ammoniagenesis.
CC       Catalyzes the first commited step in the biosynthesis of AMP from IMP.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-
CC         dicarboxyethyl)-AMP + phosphate; Xref=Rhea:RHEA:15753,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29991, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57567, ChEBI:CHEBI:58053,
CC         ChEBI:CHEBI:58189; EC=6.3.4.4;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 1/2.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
XX
DR   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1; trigger=no
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1; trigger=no
DR   Pfam; PF00709; Adenylsucc_synt; 1; trigger=no
DR   NCBIfam; TIGR00184; PurA; 1; trigger=no
XX
KW   Cytoplasm
KW   GTP-binding
KW   Ligase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Purine biosynthesis
XX
GO   GO:0004019; F:adenylosuccinate synthase activity
GO   GO:0005525; F:GTP binding
GO   GO:0000287; F:magnesium ion binding
GO   GO:0006164; P:purine nucleotide biosynthetic process
GO   GO:0005737; C:cytoplasm
XX
FT   From: PURA1_MOUSE (P28650)
FT   BINDING         42..48
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-D-E-G-K-G-K
FT   BINDING         70..72
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-H-T
FT   BINDING         363..365
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: K-L-D
FT   BINDING         445..448
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-V-G-K
FT   BINDING         43..46
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: D-E-G-K
FT   BINDING         68..71
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: N-A-G-H
FT   BINDING         331..337
FT                   /ligand="substrate"
FT   Condition: x-x-T-x-[KR]-x-R
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT   Condition: D
FT   ACT_SITE        71
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         43
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         70
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: G
FT   BINDING         43
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         163
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: T
FT   BINDING         177
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: R
FT   BINDING         256
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: N
FT   BINDING         271
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: T
FT   BINDING         335
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: R
FT   BINDING         337
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: R
XX
Size: 449-459;
Related: MF_03125; MF_03127;
Template: P28650; P0A7D4;
Scope:
 Eukaryota; Vertebrata
Fusion:
 Nter: None
 Cter: None
Duplicate: in SALSA, XENLA
Plasmid: None
Comments: None
XX
# Revision 1.10 2023/06/01
//