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HAMAP rule MF_03147

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General rule information [?]

PURL https://purl.expasy.org/hamap/rule/MF_03147
Accession MF_03147
Dates 22-AUG-2012 (Created)
22-MAY-2026 (Last updated, Version )
Name GatB_euk
Scope(s) Eukaryota
Plastid
Template(s) O75879 (GATB_HUMAN); Q9FV81 (GATB_ARATH); P33893 (GATB_YEAST); [ Recover all ]
Triggered by
case c? <OC:Eukaryota> or <OG:Plastid>
HAMAP; MF_00121 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier GATB
case <OC:Viridiplantae>
Protein name RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial;
                 Short=Glu-AdT subunit B;
                 EC=6.3.5.7;
else case <OG:Organellar chromatophore>
Protein name RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, organellar chromatophore;
                 Short=Glu-AdT subunit B;
                 EC=6.3.5.7;
else case <OC:Mammalia>
Protein name RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial;
                 Short=Glu-AdT subunit B;
                 EC=6.3.5.7;
AltName: Full=Cytochrome oxidase assembly factor PET112 homolog;
AltName: Full=PET112-like;
                 Flags: Precursor;
else case <OC:Vertebrata>
Protein name RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial;
                 Short=Glu-AdT subunit B;
                 EC=6.3.5.7;
AltName: Full=Cytochrome oxidase assembly factor PET112 homolog;
AltName: Full=PET112-like;
else
Protein name RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial;
                 Short=Glu-AdT subunit B;
                 EC=6.3.5.7;
end case
case <OC:Vertebrata>
Gene name Name=GATB; Synonyms=PET112, PET112L;
else case <OC:Saccharomycotina>
Gene name Name=PET112;
else case <OC:Viridiplantae>
Gene name Name=GATB;
end case

Comments [?]

case <OC:Viridiplantae>
FUNCTIONCatalytic subunit of the mitochondrial Glu-tRNA(Gln) amidotransferase complex GatCAB. GatCAB allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in chloroplasts and mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). This subunit probably recognizes tRNA(Gln) and mediates the transamidation of misloaded Glu by catalyzing formation of the activated gamma-phospho-intermediate and its subsequent aminolysis using ammonia produced by the gatA subunit.
else case <OG:Organellar chromatophore>
FUNCTIONCatalytic subunit of the mitochondrial Glu-tRNA(Gln) amidotransferase complex GatCAB. GatCAB allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln). The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). This subunit probably recognizes tRNA(Gln) and mediates the transamidation of misloaded Glu by catalyzing formation of the activated gamma-phospho-intermediate and its subsequent aminolysis using ammonia produced by the gatA subunit.
else
FUNCTIONCatalytic subunit of the mitochondrial Glu-tRNA(Gln) amidotransferase complex GatCAB. GatCAB allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma- phospho-Glu-tRNA(Gln). This subunit probably recognizes tRNA(Gln) and mediates the transamidation of misloaded Glu by catalyzing formation of the activated gamma-phospho-intermediate and its subsequent aminolysis using ammonia produced by the gatA subunit.
end case
CATALYTIC ACTIVITY Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl- tRNA(Gln) + L-glutamate + ADP + phosphate + H(+); Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CATALYTIC ACTIVITY Reaction=L-glutamyl-tRNA(Gln) + ATP = 5-phospho-L-glutamyl-tRNA(Gln) + ADP; Xref=Rhea:RHEA:57908, Rhea:RHEA-COMP:9684, Rhea:RHEA-COMP:15032, ChEBI:CHEBI:30616, ChEBI:CHEBI:78520, ChEBI:CHEBI:142449, ChEBI:CHEBI:456216;
CATALYTIC ACTIVITY Reaction=5-phospho-L-glutamyl-tRNA(Gln) + NH4(+) = L-glutaminyl- tRNA(Gln) + phosphate + H(+); Xref=Rhea:RHEA:57912, Rhea:RHEA- COMP:9681, Rhea:RHEA-COMP:15032, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:43474, ChEBI:CHEBI:78521, ChEBI:CHEBI:142449;
COFACTOR Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 Mg(2+) ions, a primary Mg(2+) ion involved in positioning of the gamma-carbonyl group of the amino acid in Glu-tRNA(Gln), and a secondary transient Mg(2+) ion that participates in phosphoryl transfer by polarizing the gamma-phosphate group of ATP.
case <OC:Vertebrata>
SUBUNITSubunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (@gn(QRSL1)), B (@gn(GATB)) and C (@gn(GATC)) subunits.
else case <OC:Saccharomycotina>
SUBUNITSubunit of the heterotrimeric GatFAB amidotransferase (AdT) complex, composed of A, B and F subunits.
else
SUBUNITSubunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A, B and C subunits.
end case
case <OC:Viridiplantae>
SUBCELLULAR LOCATIONMitochondrion. Plastid, chloroplast.
else case <OG:Organellar chromatophore>
SUBCELLULAR LOCATIONPlastid, organellar chromatophore.
else
SUBCELLULAR LOCATIONMitochondrion.
end case
case not (<OC:Viridiplantae> or <OC:Mammalia>) and not <AnyFeature:TransitM>
MISCELLANEOUSThis protein may be expected to contain an N-terminal transit peptide but none has been predicted.
end case
SIMILARITYBelongs to the GatB/GatE family. GatB subfamily.

Keywords [?]

case <OC:Viridiplantae>
Chloroplast
Plastid
else case <OG:Organellar chromatophore>
Organellar chromatophore
Plastid
end case
case not <OG:Organellar chromatophore>
Mitochondrion
end case
case <OC:Mammalia>
Transit peptide
end case
ATP-binding
Ligase
Magnesium
Metal-binding
Nucleotide-binding
Protein biosynthesis

Gene Ontology [?]

case <OCellular component:Viridiplantae>
GO:0009507; Cellular component:chloroplast
else case <OG:Organellar chromatophore>
GO:0070111; Cellular component:organellar chromatophore
end case
case not <OG:Organellar chromatophore>
GO:0005739; Cellular component:mitochondrion
end case
GO:0030956; Cellular component:glutamyl-tRNA(Gln) amidotransferase complex
GO:0050567; Molecular function:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
GO:0016884; Molecular function:carbon-nitrogen ligase activity, with glutamine as amido-N-donor
GO:0070681; Biological process:glutaminyl-tRNAGln biosynthesis via transamidation
GO:0032543; Biological process:mitochondrial translation

Cross-references [?]

PROSITE PS01234; GATB; 1;
Pfam PF02934; GatB_N; 1;
Pfam PF02637; GatB_Yqey; 1;
NCBIfam TIGR00133; GatB; 1;
General TransitM; -; 0-1;

Features [?]

From: GATB_HUMAN (O75879)
Key From To Description Tag Condition FTGroup
case <OC:Mammalia>
TRANSIT Nter 30 /note="Mitochondrion"
CHAIN 31 Cter /note=""
end case
From: GATB_STAAM (P64201)
Key From To Description Tag Condition FTGroup
REGION Nter 294 /note="Cradle"
REGION 412 Cter /note="Tail"
BINDING 10 10 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
E
BINDING 12 12 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"
H
BINDING 124 124 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"
E
BINDING 150 150 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="1"
E
BINDING 153 153 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[ST]
BINDING 192 192 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
D
BINDING 196 196 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
S
BINDING 206 206 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
G
BINDING 208 208 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[KR]
BINDING 210 210 /ligand="Mg(2+)"
/ligand_id="ChEBI:CHEBI:18420"
/ligand_label="2"
E

Additional information [?]

Size range 484-654 amino acids
Related rules None
Fusion Nter: None Cter: None



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