ID A0A452RKM5_URSAM Unreviewed; 136 AA.
AC A0A452RKM5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ECO:0000313|Ensembl:ENSUAMP00000019614.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000019614.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000019614.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A452RKM5; -.
DR STRING; 9643.ENSUAMP00000019614; -.
DR Ensembl; ENSUAMT00000021936.1; ENSUAMP00000019614.1; ENSUAMG00000015523.1.
DR GeneTree; ENSGT00390000018351; -.
DR OMA; MWARALW; -.
DR OrthoDB; 3084936at2759; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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:UP000291022}.
SQ SEQUENCE 136 AA; 15345 MW; 1E6FE4405343C5D9 CRC64;
MWARVVRLGF WSWGSWRRGF TSKADPQGSG RVTAEVIEHL ERLALVDFGS QEAVARLEKA
IAFADRLRAV DTDGVEPMES VLEDRCLYLR SDSVVEGNCA EELLQNAHRV VEEYFVAPPG
NISLPKQDEQ EPFSHN
//
