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HAMAP rule MF_00011

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General rule information [?]

Accession MF_00011
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 56)
Name Adenylosucc_synth
Scope(s) Bacteria
Archaea
Template(s) P0A7D4 (PURA_ECOLI); [ Recover all ]
Triggered by
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_00011 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PURA
Protein name RecName: Full=Adenylosuccinate synthetase;
                 Short=AMPSase;
                 Short=AdSS;
                 EC=6.3.4.4;
AltName: Full=IMP--aspartate ligase;
Gene name Name=purA;

Comments [?]

FUNCTIONPlays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
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.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the adenylosuccinate synthetase family.

Keywords [?]


Gene Ontology [?]

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:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF00709; Adenylsucc_synt; 1;
NCBIfam TIGR00184; purA; 1;
PROSITE PS01266; ADENYLOSUCCIN_SYN_1; 1;
PROSITE PS00513; ADENYLOSUCCIN_SYN_2; 1;

Features [?]

From: PURA_ECOLI (P0A7D4)
Key From To Description Tag Condition FTGroup
BINDING 13 19 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
G-D-E-[GA]-K-[GA]-x
BINDING 41 43 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
G-H-x
BINDING 332 334 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
x-x-D
BINDING 415 417 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
x-x-[GS]
BINDING 14 17 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
D-E-[GA]-K
BINDING 39 42 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
N-[AS]-G-H
BINDING 300 306 /ligand="substrate" x-x-[ST]-x-[KR]-x-R
ACT_SITE 14 14 /note="Proton acceptor" D
ACT_SITE 42 42 /note="Proton donor" H
BINDING 14 14 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
D
BINDING 41 41 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
G
BINDING 130 130 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
T
BINDING 144 144 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"
[KR]
BINDING 225 225 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
[QN]
BINDING 240 240 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
T
BINDING 304 304 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"
/ligand_note="ligand shared between dimeric partners"
/note="in other chain"
[KR]
BINDING 306 306 /ligand="GTP"
/ligand_id="ChEBI:CHEBI:37565"
R

Additional information [?]

Size range 336-459 amino acids
Related rules MF_03126
MF_03127
MF_04166
Fusion Nter: None Cter: None



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