ID   GATF_CANDC              Reviewed;         167 AA.
AC   B9WCK0;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
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}; ORFNames=CD36_23430;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(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; FM992689; CAX44123.1; -; Genomic_DNA.
DR   RefSeq; XP_002418817.1; XM_002418772.1.
DR   AlphaFoldDB; B9WCK0; -.
DR   SMR; B9WCK0; -.
DR   STRING; 42374.XP_002418817.1; -.
DR   EnsemblFungi; CAX44123; CAX44123; CD36_23430.
DR   GeneID; 8046355; -.
DR   KEGG; cdu:CD36_23430; -.
DR   CGD; CAL0000171689; Cd36_23430.
DR   VEuPathDB; FungiDB:CD36_23430; -.
DR   eggNOG; ENOG502RK44; Eukaryota.
DR   HOGENOM; CLU_127195_0_0_1; -.
DR   OrthoDB; 1576278at2759; -.
DR   Proteomes; UP000002605; Chromosome 2.
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; Transit peptide.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03151"
FT   CHAIN           20..167
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT                   mitochondrial"
FT                   /id="PRO_0000413397"
SQ   SEQUENCE   167 AA;  19120 MW;  C210BC4BD14157AF CRC64;
     MKAILRSSTR NLITSSRVFK NLRTSEEIRS FLAESTWSIS ELLQPPTGSS QTEVSPEIVK
     KMLKLSGLND LKHDKSVTKA LNLQMMLINH LYDNEQDTVT PSRERNDNNG IFRLLASDHL
     PQQPWDLDDL LKQINELKPD PSKGEVDFTI SDLQRDSFVI KKEKNVK