GATF_PICST
ID GATF_PICST Reviewed; 177 AA.
AC A3LU55;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
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};
DE Flags: Precursor;
GN Name=GTF1 {ECO:0000255|HAMAP-Rule:MF_03151}; ORFNames=PICST_59241;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN66527.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; CP000498; ABN66527.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001384556.2; XM_001384519.1.
DR AlphaFoldDB; A3LU55; -.
DR SMR; A3LU55; -.
DR STRING; 4924.XP_001384556.2; -.
DR EnsemblFungi; ABN66527; ABN66527; PICST_59241.
DR GeneID; 4838781; -.
DR KEGG; pic:PICST_59241; -.
DR eggNOG; ENOG502RK44; Eukaryota.
DR HOGENOM; CLU_127195_0_0_1; -.
DR InParanoid; A3LU55; -.
DR OrthoDB; 1638957at2759; -.
DR Proteomes; UP000002258; Chromosome 4.
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..16
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03151"
FT CHAIN 17..177
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT mitochondrial"
FT /id="PRO_0000413406"
FT REGION 148..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 19812 MW; F1D3A93A3C7702BE CRC64;
MIRINSRGLT VSTRRFQTLS KIGSTLKTKE DIRNALNSPV WSLKELISSN EKDMKSVEVS
AKTINKVLKL SAFDTNITAE QEKSLVSALS AQMVFIKHLY ENDEKSDSVV EENDTHFRLI
ASDHNPGEPL TLKQLLAQIE ELPEKVDPAK GETQGSFNVA NMNPRNRPFA TIRSKQG
