GATF_YEAST
ID GATF_YEAST Reviewed; 183 AA.
AC P53260; D6VUN4; Q6Q591;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
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}; OrderedLocusNames=YGR102C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [7]
RP FUNCTION, INTERACTION WITH PET112 AND HER2, AND SUBCELLULAR LOCATION.
RX PubMed=19417106; DOI=10.1101/gad.518109;
RA Frechin M., Senger B., Braye M., Kern D., Martin R.P., Becker H.D.;
RT "Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated
RT transamidation pathway involving Arc1p-controlled subcellular sorting of
RT cytosolic GluRS.";
RL Genes Dev. 23:1119-1130(2009).
RN [8]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21799017; DOI=10.1074/jbc.m111.265371;
RA Barros M.H., Rak M., Paulela J.A., Tzagoloff A.;
RT "Characterization of Gtf1p, the connector subunit of yeast mitochondrial
RT tRNA-dependent amidotransferase.";
RL J. Biol. Chem. 286:32937-32947(2011).
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, ECO:0000269|PubMed:19417106,
CC ECO:0000269|PubMed:21799017}.
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 (HER2), B (PET112) and F (YGR102C) subunits.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03151, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19417106,
CC ECO:0000269|PubMed:21799017}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03151, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19417106,
CC ECO:0000269|PubMed:21799017}; Matrix side {ECO:0000255|HAMAP-
CC Rule:MF_03151, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:19417106,
CC ECO:0000269|PubMed:21799017}.
CC -!- MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; Z72887; CAA97105.1; -; Genomic_DNA.
DR EMBL; Z72888; CAA97107.1; -; Genomic_DNA.
DR EMBL; AY558325; AAS56651.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08195.1; -; Genomic_DNA.
DR PIR; S64407; S64407.
DR RefSeq; NP_011616.3; NM_001181231.3.
DR PDB; 4N0H; X-ray; 1.95 A; F=24-183.
DR PDB; 4N0I; X-ray; 2.00 A; F=24-183.
DR PDBsum; 4N0H; -.
DR PDBsum; 4N0I; -.
DR AlphaFoldDB; P53260; -.
DR SMR; P53260; -.
DR BioGRID; 33345; 28.
DR ComplexPortal; CPX-416; Glutamyl-tRNA(Gln) amidotransferase complex.
DR DIP; DIP-6840N; -.
DR IntAct; P53260; 3.
DR MINT; P53260; -.
DR STRING; 4932.YGR102C; -.
DR MaxQB; P53260; -.
DR PaxDb; P53260; -.
DR PRIDE; P53260; -.
DR EnsemblFungi; YGR102C_mRNA; YGR102C; YGR102C.
DR GeneID; 852994; -.
DR KEGG; sce:YGR102C; -.
DR SGD; S000003334; GTF1.
DR VEuPathDB; FungiDB:YGR102C; -.
DR eggNOG; ENOG502S3RS; Eukaryota.
DR HOGENOM; CLU_120617_0_0_1; -.
DR InParanoid; P53260; -.
DR OMA; CHDGSHR; -.
DR BioCyc; YEAST:G3O-30812-MON; -.
DR PRO; PR:P53260; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53260; protein.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IDA:SGD.
DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03151; GatF; 1.
DR InterPro; IPR027499; GatF.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..183
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit F,
FT mitochondrial"
FT /id="PRO_0000202811"
FT CONFLICT 9
FT /note="R -> G (in Ref. 3; AAS56651)"
FT /evidence="ECO:0000305"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:4N0H"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:4N0H"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:4N0H"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4N0H"
SQ SEQUENCE 183 AA; 20787 MW; 6A6D2E2007817AF6 CRC64;
MYKTWRLCRT HTVGGLCHDG SHRFVSTGGA KIGKKFENMN QIRDYLSRPV WSVHEYLGIN
TKEEKLEPPS AEAVKKLLRL SGLPLEGADI KEIQMRLAKQ LSFINKLHNI PVEGEKHTKE
YDARLVQRNT KQLNYTKLLE GISHQKQDAE LGEVSGSWKA TGLAAESKNA YFVVKEGLLK
NRK
