GATF_DEBHA
ID GATF_DEBHA Reviewed; 183 AA.
AC Q6BXL8;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
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=DEHA2B01936g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382134; CAG85037.2; -; Genomic_DNA.
DR RefSeq; XP_457051.2; XM_457051.2.
DR AlphaFoldDB; Q6BXL8; -.
DR SMR; Q6BXL8; -.
DR STRING; 4959.XP_457051.2; -.
DR PRIDE; Q6BXL8; -.
DR EnsemblFungi; CAG85037; CAG85037; DEHA2B01936g.
DR GeneID; 2913765; -.
DR KEGG; dha:DEHA2B01936g; -.
DR VEuPathDB; FungiDB:DEHA2B01936g; -.
DR eggNOG; ENOG502RK44; Eukaryota.
DR HOGENOM; CLU_127195_0_0_1; -.
DR InParanoid; Q6BXL8; -.
DR OMA; STWSINE; -.
DR OrthoDB; 1726569at2759; -.
DR Proteomes; UP000000599; Chromosome B.
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..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03151"
FT CHAIN 24..183
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT mitochondrial"
FT /id="PRO_0000413401"
SQ SEQUENCE 183 AA; 20976 MW; 7FD957F65E7158F5 CRC64;
MSRMLNQIPR LITRSFRTSS VGYKATLGPI LENKSQIQDL VNKSEWNIVD IIKFSEDEVR
NIKIDSRVIT KMLRASGLKD SLSEDQKKSL IRGLKLQMIF IKYLYEGDEA EFHKIEESND
DVFRLILSDH KAPKPITLKS LLSSIENLEN EVDAEKGEIK SSLDISKLNG NNPTYFTVRS
NKE
