GATC_BRAFL
ID GATC_BRAFL Reviewed; 149 AA.
AC C3XVM1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03149};
DE Short=Glu-AdT subunit C {ECO:0000255|HAMAP-Rule:MF_03149};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03149};
DE Flags: Precursor;
GN ORFNames=BRAFLDRAFT_270748;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_03149};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatCAB amidotransferase (AdT)
CC complex, composed of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03149}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03149}.
CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000255|HAMAP-
CC Rule:MF_03149}.
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DR EMBL; GG666469; EEN67814.1; -; Genomic_DNA.
DR RefSeq; XP_002611805.1; XM_002611759.1.
DR AlphaFoldDB; C3XVM1; -.
DR SMR; C3XVM1; -.
DR STRING; 7739.XP_002611805.1; -.
DR eggNOG; KOG4247; Eukaryota.
DR InParanoid; C3XVM1; -.
DR OMA; HINTENV; -.
DR OrthoDB; 1496962at2759; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR HAMAP; MF_00122; GatC; 1.
DR InterPro; IPR003837; Asp/Glu-ADT_csu.
DR InterPro; IPR036113; Asp/Glu-ADT_sf_sub_c.
DR PANTHER; PTHR15004; PTHR15004; 1.
DR Pfam; PF02686; Glu-tRNAGln; 1.
DR SUPFAM; SSF141000; SSF141000; 1.
DR TIGRFAMs; TIGR00135; gatC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03149"
FT CHAIN 26..149
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit C,
FT mitochondrial"
FT /id="PRO_0000413294"
SQ SEQUENCE 149 AA; 17085 MW; D699EAFC9B7A3DBC CRC64;
MNHLHRLFRI TQVDRPVLLA ITRRLSSKVP TEPTWKEVDE SKLPNPTKID QDTIAHLERL
ALVDFANKEG IRRLEAAIRF ADQMFLVDTT GVEPMDSVLE DRELYLRDDV VTEGNCKDDI
LRNAGKVVED YFVAPPGNIP LPKKEEYDS
