ID   GATF_CANTT              Reviewed;         182 AA.
AC   C5M7P6;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 40.
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};
GN   Name=GTF1 {ECO:0000255|HAMAP-Rule:MF_03151}; ORFNames=CTRG_01878;
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(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   -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC       transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC       Rule:MF_03151}.
CC   -!- SIMILARITY: Belongs to the GatF family. {ECO:0000255|HAMAP-
CC       Rule:MF_03151}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG692396; EER35016.1; -; Genomic_DNA.
DR   RefSeq; XP_002547571.1; XM_002547525.1.
DR   AlphaFoldDB; C5M7P6; -.
DR   SMR; C5M7P6; -.
DR   STRING; 5482.XP_002547571.1; -.
DR   EnsemblFungi; EER35016; EER35016; CTRG_01878.
DR   GeneID; 8300142; -.
DR   KEGG; ctp:CTRG_01878; -.
DR   VEuPathDB; FungiDB:CTRG_01878; -.
DR   eggNOG; ENOG502RK44; Eukaryota.
DR   HOGENOM; CLU_127195_0_0_1; -.
DR   OrthoDB; 1576278at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
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.
FT   CHAIN           1..182
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT                   mitochondrial"
FT                   /id="PRO_0000413399"
SQ   SEQUENCE   182 AA;  21136 MW;  31B328A2611A3A90 CRC64;
     MSKKKEKKFQ ESKISTRSYR STTMLRHQIR RITTANRLLD ELKTSKDIEK FLNNSTWSIK
     ELLQQPLTNT TTKEVSSDVV TKMLKLSGLS DSQDIQNIRK SLNLQMMFIN HLYDKSGNNA
     EKKVNDNNCM FRLLASDHIP QRPLDLDTLM DEINKLEPSE EKGEIGFGIK DLQRDSFVIN
     KK