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HAMAP rule MF_00120

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_00120
Accession MF_00120
Dates 28-FEB-2005 (Created)
22-MAY-2026 (Last updated, Version )
Name GatA
Scope(s) Bacteria
Archaea
Template(s) O06491 (GATA_BACSU); Q9LCX3 (GATA_THET8); P63488 (GATA_STAAM); [ Recover all ]
Triggered by
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_00120 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier GATA
Protein name RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A;
                 Short=Asp/Glu-ADT subunit A;
                 EC=3.5.1.2;
AltName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
                 Short=Glu-ADT subunit A;
Gene name Name=gatA;

Comments [?]

FUNCTIONCatalytic subunit of the Asp/Glu-tRNA(Asn/Gln) amidotransferase complex GatCAB. GatCAB allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the multi-step transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl- tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu- tRNA(Gln). This subunit catalyzes the hydrolysis of the amido donor Gln, releasing ammonia that is sequestered within a channel in the GatCAB complex and made available to subunit B for downstream aminolysis of Glu-tRNA(Gln); may also be able to use Asn as the amido donor.
CATALYTIC ACTIVITY Reaction=L-glutamine + H2O = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
SUBUNITComponent of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase complex composed of GatA, GatB and GatC.
SIMILARITYBelongs to the amidase family. GatA subfamily.

Keywords [?]


Gene Ontology [?]

GO:0030956; Cellular component:glutamyl-tRNA(Gln) amidotransferase complex
GO:0004359; Molecular function:glutaminase activity
GO:0070681; Biological process:glutaminyl-tRNAGln biosynthesis via transamidation
GO:0006412; Biological process:translation

Cross-references [?]

Pfam PF01425; Amidase; 1;
NCBIfam TIGR00132; GatA; 1;
PROSITE PS00571; AMIDASES; 1;

Features [?]

From: GATA_BACSU (O06491)
Key From To Description Tag Condition FTGroup
ACT_SITE 79 79 /note="Charge relay system" K
ACT_SITE 154 154 /note="Charge relay system" S
ACT_SITE 178 178 /note="Acyl-ester intermediate" S
BINDING 128 128 /ligand="L-glutamine"
/ligand_id="ChEBI:CHEBI:58359"
A
BINDING 130 130 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
G
BINDING 130 130 /ligand="L-glutamine"
/ligand_id="ChEBI:CHEBI:58359"
G
BINDING 154 154 /ligand="L-glutamine"
/ligand_id="ChEBI:CHEBI:58359"
S
BINDING 175 175 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
T
BINDING 176 176 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
G
BINDING 178 178 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
S
BINDING 309 309 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
Y
BINDING 309 309 /ligand="L-glutamine"
/ligand_id="ChEBI:CHEBI:58359"
Y
BINDING 310 310 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
Y
BINDING 358 358 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
R
BINDING 358 358 /ligand="L-glutamine"
/ligand_id="ChEBI:CHEBI:58359"
R
BINDING 425 425 /ligand="L-asparagine"
/ligand_id="ChEBI:CHEBI:58048"
D
BINDING 425 425 /ligand="L-glutamine"
/ligand_id="ChEBI:CHEBI:58359"
D

Additional information [?]

Size range 423-524 amino acids
Related rules None
Fusion Nter: None Cter: None
Comments There is a possible divergent gatA in ARCFU: AF1954



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