GATF_LACTC
ID GATF_LACTC Reviewed; 175 AA.
AC C5DHL6;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03151};
DE Short=Glu-AdT subunit F {ECO:0000255|HAMAP-Rule:MF_03151};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_03151};
DE Flags: Precursor;
GN Name=GTF1 {ECO:0000255|HAMAP-Rule:MF_03151};
GN OrderedLocusNames=KLTH0E05368g;
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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). Required for
CC proper protein synthesis within the mitochondrion. {ECO:0000255|HAMAP-
CC Rule:MF_03151}.
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_03151};
CC -!- SUBUNIT: Subunit of the heterotrimeric GatFAB amidotransferase (AdT)
CC complex, composed of A, B and F subunits. {ECO:0000255|HAMAP-
CC Rule:MF_03151}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03151}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03151}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03151}.
CC -!- SIMILARITY: Belongs to the GatF family. {ECO:0000255|HAMAP-
CC Rule:MF_03151}.
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DR EMBL; CU928169; CAR23277.1; -; Genomic_DNA.
DR RefSeq; XP_002553714.1; XM_002553668.1.
DR AlphaFoldDB; C5DHL6; -.
DR SMR; C5DHL6; -.
DR STRING; 559295.C5DHL6; -.
DR EnsemblFungi; CAR23277; CAR23277; KLTH0E05368g.
DR GeneID; 8291867; -.
DR KEGG; lth:KLTH0E05368g; -.
DR eggNOG; ENOG502S3RS; Eukaryota.
DR HOGENOM; CLU_120617_0_0_1; -.
DR InParanoid; C5DHL6; -.
DR OMA; CHDGSHR; -.
DR OrthoDB; 1579170at2759; -.
DR Proteomes; UP000002036; Chromosome E.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; 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 HAMAP; MF_03151; GatF; 1.
DR InterPro; IPR027499; GatF.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03151"
FT CHAIN 20..175
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT mitochondrial"
FT /id="PRO_0000413403"
SQ SEQUENCE 175 AA; 19648 MW; EAA09E1B13E8D996 CRC64;
MLKVSARHAP VLRLPRRFYA QKTRVVIGPR LKNLDEIKEY LGKPTWSVEK YLQSSSNGET
QPPSRETVEK LLKLSGLPNE NVEMFQATLG KQLAFINKVQ SLPVDESLDP SHARIIDRNS
EALDYESLSC SVEQQETEKD SKMGEVGGSW DGTGLAAISE NGFYVLREGL LKNRK