AC   MF_03127;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_03127; -; 1; level=0
XX
Names: Adenylosucc_synth_vert_acid
XX
ID   PURA2
DE   RecName: Full=Adenylosuccinate synthetase isozyme 2;
DE            Short=AMPSase 2;
DE            Short=AdSS 2;
DE            EC=6.3.4.4;
DE   AltName: Full=Adenylosuccinate synthetase, acidic isozyme;
DE   AltName: Full=Adenylosuccinate synthetase, liver isozyme;
DE            Short=L-type adenylosuccinate synthetase;
DE   AltName: Full=IMP--aspartate ligase 2;
GN   Name=ADSS; Synonyms=ADSS2;
XX
CC   -!- FUNCTION: Plays an important role in the de novo pathway and in the
CC       salvage pathway of purine nucleotide biosynthesis. Catalyzes the first
CC       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
case <FTGroup:1>
KW   Acetylation
end case
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: PURA2_HUMAN (P30520)
case <OC:Mammalia>
FT   INIT_MET        1
FT                   /note="Removed"
FT   Optional; Group: 1; Condition: M
FT   CHAIN           2..Cter
FT                   /note="Adenylosuccinate synthetase isozyme 2"
FT   Group: 1
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT   Optional; Group: 1; Condition: A
end case
FT   BINDING         39..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-D-E-G-K-G-K
FT   BINDING         67..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-H-T
FT   BINDING         362..364
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: K-L-D
FT   BINDING         444..447
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-V-G-K
FT   BINDING         40..43
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: D-E-G-K
FT   BINDING         65..68
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: N-A-G-H
FT   BINDING         330..336
FT                   /ligand="substrate"
FT   Condition: x-x-T-x-[KR]-x-R
FT   ACT_SITE        40
FT                   /note="Proton acceptor"
FT   Condition: D
FT   ACT_SITE        68
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         40
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         67
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: G
FT   BINDING         40
FT                   /ligand="substrate"
FT   Condition: D
FT   BINDING         162
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: T
FT   BINDING         176
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: R
FT   BINDING         255
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: N
FT   BINDING         270
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: T
FT   BINDING         334
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: R
FT   BINDING         336
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: R
XX
Size: 451-457;
Related: MF_03125; MF_03126;
Template: P30520; P0A7D4;
Scope:
 Eukaryota; Vertebrata
Fusion:
 Nter: None
 Cter: None
Duplicate: in XENTR
Plasmid: None
Comments: None
XX
# Revision 1.11 2023/06/01
//