ID   GATF_ZYGRC              Reviewed;         171 AA.
AC   C5DU06;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 56.
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};
GN   OrderedLocusNames=ZYRO0C12782g;
OS   Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS   / NRRL Y-229) (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=559307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC   Y-229;
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   -!- 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}.
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DR   EMBL; CU928175; CAR27267.1; -; Genomic_DNA.
DR   RefSeq; XP_002496200.1; XM_002496155.1.
DR   AlphaFoldDB; C5DU06; -.
DR   SMR; C5DU06; -.
DR   STRING; 559307.C5DU06; -.
DR   EnsemblFungi; CAR27267; CAR27267; ZYRO0C12782g.
DR   GeneID; 8203419; -.
DR   KEGG; zro:ZYRO0C12782g; -.
DR   HOGENOM; CLU_120617_0_0_1; -.
DR   InParanoid; C5DU06; -.
DR   Proteomes; UP000008536; Chromosome C.
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..171
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT                   mitochondrial"
FT                   /id="PRO_0000413409"
SQ   SEQUENCE   171 AA;  19485 MW;  F3E258C3C9EDCB58 CRC64;
     MLQTFPRVAK CVRAYSSKPT LGPKFQSLDE IKEYIFKDTI SANEFLTQSE RAKDRELPVP
     PRETVLKLLK LSGLPTKGAD IERIQRNLSE QISFINILHD TDLDDSLNVK YARLLPRENA
     TLSYGDLIVR ANSGKNSELA EISGSWDSTS RASMRKDGYF IVREEFLDNR D