GATF_CANAL
ID GATF_CANAL Reviewed; 165 AA.
AC Q59X39; A0A1D8PIC0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=CAALFM_C209310CA; ORFNames=CaO19.11573, CaO19.4092;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017624; AOW27914.1; -; Genomic_DNA.
DR RefSeq; XP_714263.1; XM_709170.1.
DR AlphaFoldDB; Q59X39; -.
DR SMR; Q59X39; -.
DR STRING; 237561.Q59X39; -.
DR PRIDE; Q59X39; -.
DR GeneID; 3644104; -.
DR KEGG; cal:CAALFM_C209310CA; -.
DR CGD; CAL0000201078; orf19.11573.
DR VEuPathDB; FungiDB:C2_09310C_A; -.
DR eggNOG; ENOG502RK44; Eukaryota.
DR HOGENOM; CLU_127195_0_0_1; -.
DR InParanoid; Q59X39; -.
DR OMA; STWSINE; -.
DR OrthoDB; 1576278at2759; -.
DR PRO; PR:Q59X39; -.
DR Proteomes; UP000000559; 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; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03151"
FT CHAIN 20..165
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT mitochondrial"
FT /id="PRO_0000413396"
SQ SEQUENCE 165 AA; 18977 MW; 07E497E7ADAB1461 CRC64;
MKSILRSTTR NLITSSRRFE NLKTTEEIRN FLAESTWSIN ELLKSPTGSS QPEVSPEIVK
KMLKLSGLND LKDDQSVTKA LNLQMMFINH LYDNDHETVT PSPKRNENNG IFRLLASDHL
PQRPLELNNL LKQINELKPD PSKGEVDFTI SDLQRDSFVI NKRKE
