AC   MF_00011;
DC   Protein; auto
c?   <OC:Bacteria> or <OC:Archaea>
TR   HAMAP; MF_00011; -; 1; level=0
XX
Names: Adenylosucc_synth
XX
ID   PURA
DE   RecName: Full=Adenylosuccinate synthetase;
DE            Short=AMPSase;
DE            Short=AdSS;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase;
GN   Name=purA;
XX
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis. Catalyzes the first committed step in the
CC       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   Pfam; PF00709; Adenylsucc_synt; 1; trigger=no
DR   NCBIfam; TIGR00184; purA; 1; trigger=no
DR   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1; trigger=no
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1; trigger=no
XX
KW   Cytoplasm
KW   Purine biosynthesis
KW   Ligase
KW   GTP-binding
KW   Nucleotide-binding
KW   Magnesium
KW   Metal-binding
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: PURA_ECOLI (P0A7D4)
FT   BINDING         13..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-D-E-[GA]-K-[GA]-x
FT   BINDING         41..43
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-H-x
FT   BINDING         332..334
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: x-x-D
FT   BINDING         415..417
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: x-x-[GS]
FT   BINDING         14..17
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: D-E-[GA]-K
FT   BINDING         39..42
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: N-[AS]-G-H
FT   BINDING         300..306
FT                   /ligand="substrate"
FT   Condition: x-x-[ST]-x-[KR]-x-R
FT   ACT_SITE        14
FT                   /note="Proton acceptor"
FT   Condition: D
FT   ACT_SITE        42
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         14
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         41
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: G
FT   BINDING         130
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: T
FT   BINDING         144
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: [KR]
FT   BINDING         225
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: [QN]
FT   BINDING         240
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: T
FT   BINDING         304
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT   Condition: [KR]
FT   BINDING         306
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: R
XX
Size: 336-459;
Related: MF_03126!; MF_03127!; MF_04166!;
Template: P0A7D4;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in CHRVO, PHOLL, METAC
Plasmid: None
Comments: None
XX
# Revision 1.56 2023/06/01
//