HAMAP rule MF_00011
General rule information
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Accession | MF_00011 |
Dates | 1-JUN-2001 (Created)
14-MAY-2024 (Last updated, Version 57) |
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
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Identifier, protein and gene names
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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
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FUNCTION | Plays 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.; |
PATHWAY | Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. |
SUBUNIT | Homodimer. |
SUBCELLULAR LOCATION | Cytoplasm. |
SIMILARITY | Belongs to the adenylosuccinate synthetase family. |
Keywords
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Gene Ontology
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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 |
GO:0005737; Cellular component:cytoplasm |
Cross-references
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Pfam | PF00709; Adenylsucc_synt; 1; |
NCBIfam | TIGR00184; purA; 1; |
PROSITE | PS01266; ADENYLOSUCCIN_SYN_1; 1; |
PROSITE | PS00513; ADENYLOSUCCIN_SYN_2; 1; |
Features
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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
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Size range | 336-459 amino acids |
Related rules |
MF_03126 MF_03127 MF_04166 |
Fusion | Nter: None Cter: None |