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HAMAP rule MF_03125

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General rule information [?]

Accession MF_03125
Dates 13-AUG-2010 (Created)
24-MAY-2024 (Last updated, Version 14)
Name Adenylosucc_synth_euk
Scope(s) Eukaryota
Plastid
Template(s) Q9U8D3 (PURA_PLAFA); P0A7D4 (PURA_ECOLI); Q96529 (PURA_ARATH); [ Recover all ]
Triggered by
case c? <OC:Eukaryota> or <OG:Plastid>
HAMAP; MF_00011 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PURA
case <OG:Organellar chromatophore>
Protein name RecName: Full=Adenylosuccinate synthetase, organellar chromatophore;
                 Short=AMPSase;
                 Short=AdSS;
                 EC=6.3.4.4;
AltName: Full=IMP--aspartate ligase;
else case <OC:Viridiplantae>
Protein name RecName: Full=Adenylosuccinate synthetase, chloroplastic;
                 Short=AMPSase;
                 Short=AdSS;
                 EC=6.3.4.4;
AltName: Full=IMP--aspartate ligase;
else
Protein name RecName: Full=Adenylosuccinate synthetase;
                 Short=AMPSase;
                 Short=AdSS;
                 EC=6.3.4.4;
AltName: Full=IMP--aspartate ligase;
end case
case <OC:Viridiplantae>
Gene name Name=PURA;
else case <OC:Caenorhabditis>
Gene name Name=adss-1;
else case <OC:Saccharomyces>
Gene name Name=ADE12;
end case

Comments [?]

case <OC:Apicomplexa> or <OC:Leishmania> or <OC:Trypanosoma>
FUNCTIONPlays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
else
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.
end case
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.
case <OG:Organellar chromatophore>
SUBCELLULAR LOCATIONPlastid, organellar chromatophore.
else case <OC:Viridiplantae>
SUBCELLULAR LOCATIONPlastid, chloroplast.
else
SUBCELLULAR LOCATIONCytoplasm.
end case
case <OC:Apicomplexa> or <OC:Leishmania> or <OC:Trypanosoma>
MISCELLANEOUSParasitic protozoa lack the de novo purine biosynthesis pathway and rely exclusively on the salvage pathway for their purine nucleotide requirements.
end case
case <OC:Viridiplantae> and not <AnyFeature:TransitC>
MISCELLANEOUSThis protein may be expected to contain an N-terminal transit peptide but none has been predicted.
end case
SIMILARITYBelongs to the adenylosuccinate synthetase family.

Keywords [?]

GTP-binding
Ligase
Magnesium
Metal-binding
Nucleotide-binding
Purine biosynthesis
case <OG:Organellar chromatophore>
Organellar chromatophore
Plastid
else case <OC:Viridiplantae>
Chloroplast
Plastid
else
Cytoplasm
end case

Gene Ontology [?]

GO:0005737; Cellular component:cytoplasm
GO:0004019; Molecular function:adenylosuccinate synthase activity
GO:0005525; Molecular function:GTP binding
GO:0000287; Molecular function:magnesium ion binding
GO:0044208; Biological process:'de novo' AMP biosynthetic process
case <OG:Organellar chromatophore>
GO:0070111; Cellular component:organellar chromatophore
else case <OCellular component:Viridiplantae>
GO:0009507; Cellular component:chloroplast
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0005737; Cellular component:cytoplasm
end case

Cross-references [?]

PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1;
PROSITE PS00513; ADENYLOSUCCIN_SYN_2; 1;
Pfam PF00709; Adenylsucc_synt; 1;
NCBIfam TIGR00184; PurA; 1;
General TransitC; -; 0-1;

Features [?]

From: PURA_PLAFA (Q9U8D3)
Key From To Description Tag Condition FTGroup
BINDING 25 31 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 G-D-E-G-K-G-K
BINDING 53 55 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 G-H-[EST]
BINDING 339 341 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 K-[ILMV]-D
BINDING 425 427 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 G-[INTV]-G
BINDING 26 29 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 D-E-G-K
BINDING 51 54 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 N-[AS]-G-H
BINDING 307 313 /ligand="substrate" x-x-T-x-[KR]-x-R
ACT_SITE 26 26 /note="Proton acceptor" D
ACT_SITE 54 54 /note="Proton donor" H
BINDING 26 26 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 D
BINDING 53 53 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"		 G
BINDING 141 141 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 T
BINDING 155 155 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"		 [KR]
BINDING 232 232 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 [QN]
BINDING 247 247 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 T
BINDING 311 311 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 [KR]
BINDING 313 313 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 R
case <OC:Plasmodium>
BINDING 62 62 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 K
BINDING 307 307 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"		 T
end case

Additional information [?]

Size range 411-710 amino acids
Related rules MF_03126
MF_03127
Fusion Nter: None Cter: None



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