GATB (glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial; formerly PET112) is the GatB subunit of the heterotrimeric mitochondrial glutamyl-tRNA(Gln) amidotransferase GatCAB, formed with QRSL1 (GatA) and GATC. Mammalian mitochondria lack a glutaminyl-tRNA synthetase: EARS2 misacylates tRNA(Gln) with glutamate, and GatCAB converts Glu-tRNA(Gln) to Gln-tRNA(Gln). GATB, a member of the GatB/GatE family, is the tRNA-recognising and amidotransferase subunit: with ATP and Mg2+ it phosphorylates the tRNA-bound glutamate to a gamma-phospho intermediate and amidates it with ammonia supplied by the QRSL1 glutaminase. The complex is the only mitochondrial source of Gln-tRNA(Gln) and is required for mitochondrial protein synthesis. Biallelic GATB variants cause combined oxidative phosphorylation deficiency 41 (COXPD41), a lethal infantile metabolic cardiomyopathy with lactic acidosis and respiratory chain deficiency.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003824 catalytic activity | IEA GO_REF:0000002 | MODIFY | Summary: catalytic activity from InterPro/UniRule mapping of GatB/GatE family domains. Reason: Correct but more general than necessary: catalytic activity is an ancestor of glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity (EC 6.3.5.7), the reaction to which GATB contributes the ATP-dependent activation and amidation of tRNA-bound glutamate. The specific term should be used, with the activity understood as that of the GatCAB complex. Proposed replacements: glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Supporting Evidence: file:human/GATB/GATB-uniprot.txt Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl- tRNA(Gln) + L-glutamate + ADP + phosphate + H(+); file:human/GATB/GATB-uniprot.txt 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 |
| GO:0005515 protein binding | IPI PMID:19805282 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. | REMOVE | Summary: Protein binding with QRSL1 (PMID:19805282). Reason: Protein binding is uninformative. The GATB-QRSL1 interaction reflects co-membership of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase, captured by the GO:0030956 complex annotations. Removal does not dispute the interaction. Supporting Evidence: file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Protein binding with LINC01561 (PMID:28514442). Reason: Protein binding is uninformative. The partner Q8N1V8 is a putative protein encoded by the long non-coding RNA LINC01561, detected in a proteome-scale binary interaction screen, with no link to GatCAB function or to mitochondria. Removal does not dispute the screen result. Supporting Evidence: file:human/GATB/GATB-uniprot.txt O75879; Q8N1V8: LINC01561; NbExp=2; |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Protein binding with QRSL1 (PMID:28514442). Reason: Protein binding is uninformative. The GATB-QRSL1 interaction reflects co-membership of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase, captured by the GO:0030956 complex annotations. Removal does not dispute the interaction. Supporting Evidence: file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding with LINC01561 (PMID:33961781). Reason: Protein binding is uninformative. The partner Q8N1V8 is a putative protein encoded by the long non-coding RNA LINC01561, detected in a proteome-scale binary interaction screen, with no link to GatCAB function or to mitochondria. Removal does not dispute the screen result. Supporting Evidence: file:human/GATB/GATB-uniprot.txt O75879; Q8N1V8: LINC01561; NbExp=2; |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Protein binding with QRSL1 (PMID:33961781). Reason: Protein binding is uninformative. The GATB-QRSL1 interaction reflects co-membership of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase, captured by the GO:0030956 complex annotations. Removal does not dispute the interaction. Supporting Evidence: file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Protein binding with QRSL1 (PMID:40205054). Reason: Protein binding is uninformative. The GATB-QRSL1 interaction reflects co-membership of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase, captured by the GO:0030956 complex annotations. Removal does not dispute the interaction. Supporting Evidence: file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: Mitochondrion (HTP, PMID:34800366). Reason: GATB is a nuclear-encoded mitochondrial protein. Human PET112 is imported into mitochondria in vitro, V5-tagged GatB is strictly mitochondrial in U2OS cells, and the protein is found in the mitochondrial proteome. GatCAB charges the mitochondrially encoded tRNA(Gln). Supporting Evidence: file:human/GATB/GATB-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion PMID:30283131 A transient transfection experiment in U2OS cells revealed that the location of the V5-GatB protein was strictly mitochondrial, confirming correct cellular localization and is compatible with its function as part of the mitochondrial GatCAB complex |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: Mitochondrion (IBA, GO_REF:0000033). Reason: GATB is a nuclear-encoded mitochondrial protein. Human PET112 is imported into mitochondria in vitro, V5-tagged GatB is strictly mitochondrial in U2OS cells, and the protein is found in the mitochondrial proteome. GatCAB charges the mitochondrially encoded tRNA(Gln). Supporting Evidence: file:human/GATB/GATB-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion PMID:30283131 A transient transfection experiment in U2OS cells revealed that the location of the V5-GatB protein was strictly mitochondrial, confirming correct cellular localization and is compatible with its function as part of the mitochondrial GatCAB complex |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | ACCEPT | Summary: Mitochondrion (IDA, GO_REF:0000052). Reason: GATB is a nuclear-encoded mitochondrial protein. Human PET112 is imported into mitochondria in vitro, V5-tagged GatB is strictly mitochondrial in U2OS cells, and the protein is found in the mitochondrial proteome. GatCAB charges the mitochondrially encoded tRNA(Gln). Supporting Evidence: file:human/GATB/GATB-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion PMID:30283131 A transient transfection experiment in U2OS cells revealed that the location of the V5-GatB protein was strictly mitochondrial, confirming correct cellular localization and is compatible with its function as part of the mitochondrial GatCAB complex |
| GO:0005739 mitochondrion | IDA PMID:19805282 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. | ACCEPT | Summary: Mitochondrion (IDA, PMID:19805282). Reason: GATB is a nuclear-encoded mitochondrial protein. Human PET112 is imported into mitochondria in vitro, V5-tagged GatB is strictly mitochondrial in U2OS cells, and the protein is found in the mitochondrial proteome. GatCAB charges the mitochondrially encoded tRNA(Gln). Supporting Evidence: file:human/GATB/GATB-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion PMID:30283131 A transient transfection experiment in U2OS cells revealed that the location of the V5-GatB protein was strictly mitochondrial, confirming correct cellular localization and is compatible with its function as part of the mitochondrial GatCAB complex |
| GO:0005739 mitochondrion | IDA PMID:9878253 Identification and characterization of human cDNAs specific ... | ACCEPT | Summary: Mitochondrion (IDA, PMID:9878253). Reason: GATB is a nuclear-encoded mitochondrial protein. Human PET112 is imported into mitochondria in vitro, V5-tagged GatB is strictly mitochondrial in U2OS cells, and the protein is found in the mitochondrial proteome. GatCAB charges the mitochondrially encoded tRNA(Gln). Supporting Evidence: PMID:9878253 Mitochondrial targeting of the human gene products, suggested by computer analysis of the protein sequences, was confirmed by an in vitro import and protease-protection assay. |
| GO:0005739 mitochondrion | IEA GO_REF:0000120 | ACCEPT | Summary: Mitochondrion (IEA, GO_REF:0000120). Reason: GATB is a nuclear-encoded mitochondrial protein. Human PET112 is imported into mitochondria in vitro, V5-tagged GatB is strictly mitochondrial in U2OS cells, and the protein is found in the mitochondrial proteome. GatCAB charges the mitochondrially encoded tRNA(Gln). Supporting Evidence: file:human/GATB/GATB-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion PMID:30283131 A transient transfection experiment in U2OS cells revealed that the location of the V5-GatB protein was strictly mitochondrial, confirming correct cellular localization and is compatible with its function as part of the mitochondrial GatCAB complex |
| GO:0005739 mitochondrion | IMP PMID:30283131 Pathogenic variants in glutamyl-tRNA(Gln) amidotransferase s... | ACCEPT | Summary: Mitochondrion (IMP, PMID:30283131). Reason: GATB is a nuclear-encoded mitochondrial protein. Human PET112 is imported into mitochondria in vitro, V5-tagged GatB is strictly mitochondrial in U2OS cells, and the protein is found in the mitochondrial proteome. GatCAB charges the mitochondrially encoded tRNA(Gln). Supporting Evidence: file:human/GATB/GATB-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion PMID:30283131 A transient transfection experiment in U2OS cells revealed that the location of the V5-GatB protein was strictly mitochondrial, confirming correct cellular localization and is compatible with its function as part of the mitochondrial GatCAB complex |
| GO:0016874 ligase activity | IEA GO_REF:0000002 | MODIFY | Summary: ligase activity from InterPro/UniRule mapping of GatB/GatE family domains. Reason: Correct but more general than necessary: ligase activity is an ancestor of glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity (EC 6.3.5.7), the reaction to which GATB contributes the ATP-dependent activation and amidation of tRNA-bound glutamate. The specific term should be used, with the activity understood as that of the GatCAB complex. Proposed replacements: glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Supporting Evidence: file:human/GATB/GATB-uniprot.txt Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl- tRNA(Gln) + L-glutamate + ADP + phosphate + H(+); file:human/GATB/GATB-uniprot.txt 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 |
| GO:0016884 carbon-nitrogen ligase activity, with glutamine as amido-N-donor | IEA GO_REF:0000120 | MODIFY | Summary: carbon-nitrogen ligase activity, with glutamine as amido-N-donor from InterPro/UniRule mapping of GatB/GatE family domains. Reason: Correct but more general than necessary: carbon-nitrogen ligase activity, with glutamine as amido-N-donor is an ancestor of glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity (EC 6.3.5.7), the reaction to which GATB contributes the ATP-dependent activation and amidation of tRNA-bound glutamate. The specific term should be used, with the activity understood as that of the GatCAB complex. Proposed replacements: glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Supporting Evidence: file:human/GATB/GATB-uniprot.txt Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl- tRNA(Gln) + L-glutamate + ADP + phosphate + H(+); file:human/GATB/GATB-uniprot.txt 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 |
| GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Glutamyl-tRNA(Gln) amidotransferase complex (IBA). Reason: Core complex membership. GATB is the B subunit of the human GatCAB heterotrimer, which was identified and reconstituted with recombinant subunits. Supporting Evidence: PMID:19805282 In addition, we have identified a human homolog of the Glu-tRNA(Gln) amidotransferase, the hGatCAB heterotrimer. PMID:30283131 This latter conversion is performed by GatCAB, the glutamyl-tRNAGln amidotransferase protein complex, that consists of three subunits: GatA encoded by QRSL1, GatB encoded by GATB, and GatC encoded by GATC5,6. file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex | IDA PMID:19805282 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. | ACCEPT | Summary: Glutamyl-tRNA(Gln) amidotransferase complex (IDA). Reason: Core complex membership. GATB is the B subunit of the human GatCAB heterotrimer, which was identified and reconstituted with recombinant subunits. Supporting Evidence: PMID:19805282 In addition, we have identified a human homolog of the Glu-tRNA(Gln) amidotransferase, the hGatCAB heterotrimer. PMID:30283131 This latter conversion is performed by GatCAB, the glutamyl-tRNAGln amidotransferase protein complex, that consists of three subunits: GatA encoded by QRSL1, GatB encoded by GATB, and GatC encoded by GATC5,6. file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex | IEA GO_REF:0000104 | ACCEPT | Summary: Glutamyl-tRNA(Gln) amidotransferase complex (IEA). Reason: Core complex membership. GATB is the B subunit of the human GatCAB heterotrimer, which was identified and reconstituted with recombinant subunits. Supporting Evidence: PMID:19805282 In addition, we have identified a human homolog of the Glu-tRNA(Gln) amidotransferase, the hGatCAB heterotrimer. PMID:30283131 This latter conversion is performed by GatCAB, the glutamyl-tRNAGln amidotransferase protein complex, that consists of three subunits: GatA encoded by QRSL1, GatB encoded by GATB, and GatC encoded by GATC5,6. file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex | IPI PMID:19805282 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. | ACCEPT | Summary: Glutamyl-tRNA(Gln) amidotransferase complex (IPI). Reason: Core complex membership. GATB is the B subunit of the human GatCAB heterotrimer, which was identified and reconstituted with recombinant subunits. Supporting Evidence: PMID:19805282 In addition, we have identified a human homolog of the Glu-tRNA(Gln) amidotransferase, the hGatCAB heterotrimer. PMID:30283131 This latter conversion is performed by GatCAB, the glutamyl-tRNAGln amidotransferase protein complex, that consists of three subunits: GatA encoded by QRSL1, GatB encoded by GATB, and GatC encoded by GATC5,6. file:human/GATB/GATB-uniprot.txt Subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits. |
| GO:0032543 mitochondrial translation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Mitochondrial translation (IBA). Reason: Kept as non-core context, not core. GatCAB transamidates Glu-tRNA(Gln) to Gln-tRNA(Gln), preparing the charged tRNA that mitochondrial translation consumes; it does not itself perform a step of translation on the mitoribosome. The knockdown and patient data show that GatCAB is necessary for mitochondrial protein synthesis, which is necessity evidence, not participation. The MTO1 review takes the same line for a tRNA-preparing enzyme. The core process for this subunit is GO:0019988 charged-tRNA amino acid modification. Supporting Evidence: PMID:19805282 When any of the hGatCAB subunits were inactivated by siRNA-mediated knock down in human cells, the Glu-charged form of tRNA(Gln) accumulated and defects in respiration could be observed. PMID:30283131 Patients present with metabolic cardiomyopathy and have defective Gln-mt-tRNAGln acylation, resulting in reduced mitochondrial protein translation with an influence of the amount of glutamine available. PMID:30283131 The expression of the transgene in the affected subject’s fibroblasts resulted in a complete rescue of the respiratory chain enzyme deficiencies, indicating that indeed the GATB gene variants in this subject caused the enzyme deficiencies |
| GO:0032543 mitochondrial translation | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: Mitochondrial translation (IEA). Reason: Kept as non-core context, not core. GatCAB transamidates Glu-tRNA(Gln) to Gln-tRNA(Gln), preparing the charged tRNA that mitochondrial translation consumes; it does not itself perform a step of translation on the mitoribosome. The knockdown and patient data show that GatCAB is necessary for mitochondrial protein synthesis, which is necessity evidence, not participation. The MTO1 review takes the same line for a tRNA-preparing enzyme. The core process for this subunit is GO:0019988 charged-tRNA amino acid modification. Supporting Evidence: PMID:19805282 When any of the hGatCAB subunits were inactivated by siRNA-mediated knock down in human cells, the Glu-charged form of tRNA(Gln) accumulated and defects in respiration could be observed. PMID:30283131 Patients present with metabolic cardiomyopathy and have defective Gln-mt-tRNAGln acylation, resulting in reduced mitochondrial protein translation with an influence of the amount of glutamine available. PMID:30283131 The expression of the transgene in the affected subject’s fibroblasts resulted in a complete rescue of the respiratory chain enzyme deficiencies, indicating that indeed the GATB gene variants in this subject caused the enzyme deficiencies |
| GO:0032543 mitochondrial translation | IMP PMID:19805282 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. | KEEP AS NON CORE | Summary: Mitochondrial translation (IMP). Reason: Kept as non-core context, not core. GatCAB transamidates Glu-tRNA(Gln) to Gln-tRNA(Gln), preparing the charged tRNA that mitochondrial translation consumes; it does not itself perform a step of translation on the mitoribosome. The knockdown and patient data show that GatCAB is necessary for mitochondrial protein synthesis, which is necessity evidence, not participation. The MTO1 review takes the same line for a tRNA-preparing enzyme. The core process for this subunit is GO:0019988 charged-tRNA amino acid modification. Supporting Evidence: PMID:19805282 When any of the hGatCAB subunits were inactivated by siRNA-mediated knock down in human cells, the Glu-charged form of tRNA(Gln) accumulated and defects in respiration could be observed. PMID:30283131 Patients present with metabolic cardiomyopathy and have defective Gln-mt-tRNAGln acylation, resulting in reduced mitochondrial protein translation with an influence of the amount of glutamine available. PMID:30283131 The expression of the transgene in the affected subject’s fibroblasts resulted in a complete rescue of the respiratory chain enzyme deficiencies, indicating that indeed the GATB gene variants in this subject caused the enzyme deficiencies |
| GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | IBA GO_REF:0000033 | ACCEPT | Summary: Contributes to glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity (IBA). Reason: Core activity. Recombinant human GatCAB converts Glu-tRNA(Gln) to Gln-tRNA(Gln) in vitro; GATB is the subunit that activates and amidates the tRNA-bound glutamate. contributes_to correctly reflects that the activity belongs to the complex. Supporting Evidence: PMID:19805282 We successfully reconstituted in vitro Gln-tRNA(Gln) formation catalyzed by the recombinant mtGluRS and hGatCAB. file:human/GATB/GATB-uniprot.txt 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 PMID:30283131 In GatB, Phe136 mutated in P1A is located in a hydrophobic region, in close proximity to the catalytic residues of the amidotransferase site and to the GatA–GatB interface |
| GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | IDA PMID:19805282 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. | ACCEPT | Summary: Contributes to glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity (IDA). Reason: Core activity. Recombinant human GatCAB converts Glu-tRNA(Gln) to Gln-tRNA(Gln) in vitro; GATB is the subunit that activates and amidates the tRNA-bound glutamate. contributes_to correctly reflects that the activity belongs to the complex. Supporting Evidence: PMID:19805282 We successfully reconstituted in vitro Gln-tRNA(Gln) formation catalyzed by the recombinant mtGluRS and hGatCAB. file:human/GATB/GATB-uniprot.txt 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 PMID:30283131 In GatB, Phe136 mutated in P1A is located in a hydrophobic region, in close proximity to the catalytic residues of the amidotransferase site and to the GatA–GatB interface |
| GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | IEA GO_REF:0000120 | ACCEPT | Summary: Glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity from the Rhea/EC 6.3.5.7 mapping. Reason: Correct core activity. GATB carries the amidotransferase site, but the reaction requires the glutaminase activity of QRSL1 within GatCAB, so the activity is more precisely expressed with the contributes_to qualifier used in this gene's IBA and IDA rows. Supporting Evidence: file:human/GATB/GATB-uniprot.txt Reaction=L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl- tRNA(Gln) + L-glutamate + ADP + phosphate + H(+); PMID:30283131 In the bacterial GatCAB complex, GatA and GatB possess the catalytic amidase and kinase functions, respectively, while GatC serves as a stabilizing linker between them16. |
| GO:0070681 obsolete glutaminyl-tRNAGln biosynthesis via transamidation | IBA GO_REF:0000033 | MODIFY | Summary: Obsolete term glutaminyl-tRNAGln biosynthesis via transamidation (IBA). Reason: The biology is correct (GatCAB converts Glu-tRNA(Gln) to Gln-tRNA(Gln)), but GO:0070681 is obsolete as a pathway-variant term and GO says such annotations need review rather than automatic migration. Because GatCAB amidates glutamate already attached to tRNA(Gln), the process is captured by charged-tRNA amino acid modification, consistent with the GATC and QRSL1 reviews; the activity is captured by GO:0050567. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000183793 SUPPORTS TRANSFER The GatB-family node correctly carries the transamidation function to human GATB; only the term has since been obsoleted, so the row is re-expressed with GO:0019988. Proposed replacements: charged-tRNA amino acid modification Supporting Evidence: PMID:19805282 We successfully reconstituted in vitro Gln-tRNA(Gln) formation catalyzed by the recombinant mtGluRS and hGatCAB. PMID:30283131 mt-tRNAGln is indirectly charged by a transamidation reaction involving the GatCAB aminoacyl-tRNA amidotransferase complex. |
| GO:0070681 obsolete glutaminyl-tRNAGln biosynthesis via transamidation | IDA PMID:19805282 Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. | MODIFY | Summary: Obsolete term glutaminyl-tRNAGln biosynthesis via transamidation (IDA). Reason: The biology is correct (GatCAB converts Glu-tRNA(Gln) to Gln-tRNA(Gln)), but GO:0070681 is obsolete as a pathway-variant term and GO says such annotations need review rather than automatic migration. Because GatCAB amidates glutamate already attached to tRNA(Gln), the process is captured by charged-tRNA amino acid modification, consistent with the GATC and QRSL1 reviews; the activity is captured by GO:0050567. Proposed replacements: charged-tRNA amino acid modification Supporting Evidence: PMID:19805282 We successfully reconstituted in vitro Gln-tRNA(Gln) formation catalyzed by the recombinant mtGluRS and hGatCAB. PMID:30283131 mt-tRNAGln is indirectly charged by a transamidation reaction involving the GatCAB aminoacyl-tRNA amidotransferase complex. |
| GO:0070681 obsolete glutaminyl-tRNAGln biosynthesis via transamidation | IEA GO_REF:0000104 | MODIFY | Summary: Obsolete term glutaminyl-tRNAGln biosynthesis via transamidation (IEA). Reason: The biology is correct (GatCAB converts Glu-tRNA(Gln) to Gln-tRNA(Gln)), but GO:0070681 is obsolete as a pathway-variant term and GO says such annotations need review rather than automatic migration. Because GatCAB amidates glutamate already attached to tRNA(Gln), the process is captured by charged-tRNA amino acid modification, consistent with the GATC and QRSL1 reviews; the activity is captured by GO:0050567. Proposed replacements: charged-tRNA amino acid modification Supporting Evidence: PMID:19805282 We successfully reconstituted in vitro Gln-tRNA(Gln) formation catalyzed by the recombinant mtGluRS and hGatCAB. PMID:30283131 mt-tRNAGln is indirectly charged by a transamidation reaction involving the GatCAB aminoacyl-tRNA amidotransferase complex. |
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Download this section (compressed HTML)Q: Which identity elements of mt-tRNA(Gln) does human GATB recognise, and how does GatCAB act on Glu-tRNA(Gln) but not on mt-tRNA(Glu) charged by the same EARS2?
Q: Why did fibroblasts of GATB patients, unlike those of QRSL1 and GATC patients, show clear respiratory chain deficiencies under standard culture conditions?
Experiment: Assay ATP-dependent Glu-tRNA(Gln) phosphorylation and amidation by recombinant human GatCAB carrying GATB patient variants (for example Phe136Leu), with ammonia supplied directly versus from glutamine, to separate kinase and amidation defects from loss of GatA coupling.
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