AC   MF_03125;
DC   Protein; auto
c?   <OC:Eukaryota> or <OG:Plastid>
TR   HAMAP; MF_00011; -; 1; level=0
XX
Names: Adenylosucc_synth_euk
XX
ID   PURA
case <OG:Organellar chromatophore>
DE   RecName: Full=Adenylosuccinate synthetase, organellar chromatophore;
DE            Short=AMPSase;
DE            Short=AdSS;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase;
else case <OC:Viridiplantae>
DE   RecName: Full=Adenylosuccinate synthetase, chloroplastic;
DE            Short=AMPSase;
DE            Short=AdSS;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase;
else
DE   RecName: Full=Adenylosuccinate synthetase;
DE            Short=AMPSase;
DE            Short=AdSS;
DE            EC=6.3.4.4;
DE   AltName: Full=IMP--aspartate ligase;
end case
case <OC:Viridiplantae>
GN   Name=PURA;
else case <OC:Caenorhabditis>
GN   Name=adss-1;
else case <OC:Saccharomyces>
GN   Name=ADE12;
end case
XX
case <OC:Apicomplexa> or <OC:Leishmania> or <OC:Trypanosoma>
CC   -!- FUNCTION: Plays an important role in the salvage pathway for purine
CC       nucleotide biosynthesis. Catalyzes the first commited step in the
CC       biosynthesis of AMP from IMP.
else
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.
end case
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.
case <OG:Organellar chromatophore>
CC   -!- SUBCELLULAR LOCATION: Plastid, organellar chromatophore.
else case <OC:Viridiplantae>
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
case <OC:Apicomplexa> or <OC:Leishmania> or <OC:Trypanosoma>
CC   -!- MISCELLANEOUS: Parasitic protozoa lack the de novo purine biosynthesis
CC       pathway and rely exclusively on the salvage pathway for their purine
CC       nucleotide requirements.
end case
case <OC:Viridiplantae> and not <AnyFeature:TransitC>
CC   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted.
end case
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
case <OC:Viridiplantae>
DR   General; TransitC; -; 0-1; trigger=yes
end case
XX
KW   GTP-binding
KW   Ligase
KW   Magnesium
KW   Metal-binding
KW   Nucleotide-binding
KW   Purine biosynthesis
case <OG:Organellar chromatophore>
KW   Organellar chromatophore
KW   Plastid
else case <OC:Viridiplantae>
KW   Chloroplast
KW   Plastid
else
KW   Cytoplasm
end case
XX
GO   GO:0005737; C:cytoplasm
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:0006167; P:AMP biosynthetic process
case <OG:Organellar chromatophore>
GO   GO:0070111; C:organellar chromatophore
else case <OC:Viridiplantae>
GO   GO:0009507; C:chloroplast
else
GO   GO:0005737; C:cytoplasm
end case
XX
FT   From: PURA_PLAFA (Q9U8D3)
FT   BINDING         25..31
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-D-E-G-K-G-K
FT   BINDING         53..55
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-H-[EST]
FT   BINDING         339..341
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: K-[ILMV]-D
FT   BINDING         425..427
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: G-[INTV]-G
FT   BINDING         26..29
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: D-E-G-K
FT   BINDING         51..54
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: N-[AS]-G-H
FT   BINDING         307..313
FT                   /ligand="substrate"
FT   Condition: x-x-T-x-[KR]-x-R
FT   ACT_SITE        26
FT                   /note="Proton acceptor"
FT   Condition: D
FT   ACT_SITE        54
FT                   /note="Proton donor"
FT   Condition: H
FT   BINDING         26
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: D
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Condition: G
FT   BINDING         141
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: T
FT   BINDING         155
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /ligand_note="ligand shared between dimeric partners"
FT   Condition: [KR]
FT   BINDING         232
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: [QN]
FT   BINDING         247
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: T
FT   BINDING         311
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT   Condition: [KR]
FT   BINDING         313
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: R
case <OC:Plasmodium>
FT   BINDING         62
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: K
FT   BINDING         307
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT   Condition: T
end case
XX
Size: 411-710;
Related: MF_03126!; MF_03127!;
Template: Q9U8D3; P0A7D4; Q96529;
Scope:
 Eukaryota
 Plastid
Fusion:
 Nter: None
 Cter: None
Duplicate: in CAPFR, LACBS, ORYSJ, PHYPA, RICCO, SORBI, TRYCR
Plasmid: None
Comments: None
XX
# Revision 1.13 2023/06/01
//