HAMAP rule MF_00120
General rule information
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| 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
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Identifier, protein and gene names
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| 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
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| FUNCTION | Catalytic 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; |
| SUBUNIT | Component of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase complex composed of GatA, GatB and GatC. |
| SIMILARITY | Belongs to the amidase family. GatA subfamily. |
Keywords
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Gene Ontology
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| 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
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Features
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| 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
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| Size range | 423-524 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |
| Comments | There is a possible divergent gatA in ARCFU: AF1954 |