ID H2LSB4_ORYLA Unreviewed; 121 AA.
AC H2LSB4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03149};
DE Short=Glu-AdT subunit C {ECO:0000256|HAMAP-Rule:MF_03149};
DE EC=6.3.5.- {ECO:0000256|HAMAP-Rule:MF_03149};
GN Name=GATC {ECO:0000256|HAMAP-Rule:MF_03149};
GN Synonyms=gatc {ECO:0000313|Ensembl:ENSORLP00000008975.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000008975.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000008975.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008975.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000008975.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000008975.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC through the transamidation of misacylated Glu-tRNA(Gln) in the
CC mitochondria. The reaction takes place in the presence of glutamine and
CC ATP through an activated gamma-phospho-Glu-tRNA(Gln).
CC {ECO:0000256|HAMAP-Rule:MF_03149}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03149};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A (QRSL1), B (GATB) and C (GATC) subunits.
CC {ECO:0000256|HAMAP-Rule:MF_03149}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03149}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000256|HAMAP-
CC Rule:MF_03149}.
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DR AlphaFoldDB; H2LSB4; -.
DR Ensembl; ENSORLT00000008976.2; ENSORLP00000008975.2; ENSORLG00000007156.2.
DR GeneTree; ENSGT00390000018351; -.
DR HOGENOM; CLU_105899_0_2_1; -.
DR Proteomes; UP000001038; Chromosome 9.
DR Bgee; ENSORLG00000007156; Expressed in bone element and 15 other cell types or tissues.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IEA:UniProtKB-UniRule.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR HAMAP; MF_00122; GatC; 1.
DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR InterPro; IPR003837; GatC.
DR NCBIfam; TIGR00135; gatC; 1.
DR PANTHER; PTHR15004:SF0; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT C, MITOCHONDRIAL; 1.
DR PANTHER; PTHR15004; UNCHARACTERIZED; 1.
DR Pfam; PF02686; GatC; 1.
DR SUPFAM; SSF141000; Glu-tRNAGln amidotransferase C subunit; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03149};
KW Ligase {ECO:0000256|HAMAP-Rule:MF_03149};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03149};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03149};
KW Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_03149};
KW Reference proteome {ECO:0000313|Proteomes:UP000001038}.
SQ SEQUENCE 121 AA; 13625 MW; B3825E83941626B0 CRC64;
EPVSEDQLPL PAQIPPDLVD KLERLALVDF RTKQGLECLE KAIRFADQLH VVDTTGIEPM
DSVLEDRALY LREDTAVDGG CAEELLKLSR KTVEEYFVVP PGNIPLPKKE ERSSMLKHSE
L
//
