HAMAP rule MF_03147
General rule information
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| 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
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Identifier, protein and gene names
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| 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
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| case <OC:Viridiplantae> | |
| FUNCTION | Catalytic 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> | |
| FUNCTION | Catalytic 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 | |
| FUNCTION | Catalytic 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> | |
| SUBUNIT | Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (@gn(QRSL1)), B (@gn(GATB)) and C (@gn(GATC)) subunits. |
| else case <OC:Saccharomycotina> | |
| SUBUNIT | Subunit of the heterotrimeric GatFAB amidotransferase (AdT) complex, composed of A, B and F subunits. |
| else | |
| SUBUNIT | Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A, B and C subunits. |
| end case | |
| case <OC:Viridiplantae> | |
| SUBCELLULAR LOCATION | Mitochondrion. Plastid, chloroplast. |
| else case <OG:Organellar chromatophore> | |
| SUBCELLULAR LOCATION | Plastid, organellar chromatophore. |
| else | |
| SUBCELLULAR LOCATION | Mitochondrion. |
| end case | |
| case not (<OC:Viridiplantae> or <OC:Mammalia>) and not <AnyFeature:TransitM> | |
| MISCELLANEOUS | This protein may be expected to contain an N-terminal transit peptide but none has been predicted. |
| end case | |
| SIMILARITY | Belongs to the GatB/GatE family. GatB subfamily. |
Keywords
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| 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
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| 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
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| PROSITE | PS01234; GATB; 1; |
| Pfam | PF02934; GatB_N; 1; |
| Pfam | PF02637; GatB_Yqey; 1; |
| NCBIfam | TIGR00133; GatB; 1; |
| General | TransitM; -; 0-1; |
Features
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| 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
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| Size range | 484-654 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |