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HAMAP rule MF_03125

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General rule information [?]

Accession MF_03125
Dates 13-AUG-2010 (Created)
19-NOV-2022 (Last updated, Version 12)
Name Adenylosucc_synth_euk
Scope
Eukaryota; except Vertebrata
Plastid
Templates Q9U8D3 (PURA_PLAFA); P0A7D4 (PURA_ECOLI); Q96529 (PURA_ARATH): [Recover all]
case <OC:Eukaryota> or <OG:Plastid>
Triggered by
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
PURA
else case <OC:Caenorhabditis>
Gene name
adss-1
else case <OC:Saccharomyces>
Gene name
ADE12
end case

Comments [?]

case <OC:Apicomplexa> or <OC:Leishmania> or <OC:Trypanosoma>
Function Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
else
Function Plays 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 RHEA:15753: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
EC 6.3.4.4
Cofactor Mg(2+)
Note: Binds 1 Mg(2+) ion per subunit.
Pathway Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Subunit Homodimer.
case <OG:Organellar chromatophore>
Subcellular location Plastid, organellar chromatophore.
else case <OC:Viridiplantae>
Subcellular location Plastid, chloroplast.
else
Subcellular location Cytoplasm.
end case
case <OC:Apicomplexa> or <OC:Leishmania> or <OC:Trypanosoma>
Miscellaneous Parasitic 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>
Miscellaneous This protein may be expected to contain an N-terminal transit peptide but none has been predicted.
end case
Similarity Belongs 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:0006164; Biological process: purine nucleotide biosynthetic process.
GO:0006167; Biological process: AMP biosynthetic process.
case <OG:Organellar chromatophore>
GO:0070111; Cellular component: organellar chromatophore.
else case <OC:Viridiplantae>
GO:0009507; Cellular component: chloroplast.
else
GO:0005737; Cellular component: cytoplasm.
end case

Cross-references [?]

PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1;
PS00513; ADENYLOSUCCIN_SYN_2; 1;
Pfam PF00709; Adenylsucc_synt; 1;
TIGRFAMs TIGR00184; PurA; 1;

Computed features [?]

case <OC:Viridiplantae>
General TransitC; -; 0-1; trigger=yes;
end case

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       Proton acceptor     D  
ACT_SITE     54     54       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 (PURA1 supersedes the current rule); MF_03127 (PURA2 supersedes the current rule)
Fusion None


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