ID   SYEM_YEAST              Reviewed;         536 AA.
AC   P48525; D6W232; Q08203;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Glutamate--tRNA ligase, mitochondrial;
DE            EC=6.1.1.17;
DE   AltName: Full=Glutamyl-tRNA synthetase;
DE            Short=GluRS;
GN   Name=MSE1; OrderedLocusNames=YOL033W;
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 [GENOMIC DNA].
RC   STRAIN=ATCC 24657 / D273-10B;
RA   Tzagoloff A.A., Shtanko A.;
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [3]
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   [4]
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).
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-
CC       step reaction: glutamate is first activated by ATP to form Glu-AMP and
CC       then transferred to the acceptor end of tRNA(Glu). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-
CC         glutamyl-tRNA(Glu); Xref=Rhea:RHEA:23540, Rhea:RHEA-COMP:9663,
CC         Rhea:RHEA-COMP:9680, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520,
CC         ChEBI:CHEBI:456215; EC=6.1.1.17;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       Glutamate--tRNA ligase type 1 subfamily. {ECO:0000305}.
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DR   EMBL; L39015; AAA61403.1; -; Genomic_DNA.
DR   EMBL; Z74775; CAA99033.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10748.1; -; Genomic_DNA.
DR   PIR; S66716; S66716.
DR   RefSeq; NP_014609.1; NM_001183287.1.
DR   AlphaFoldDB; P48525; -.
DR   SMR; P48525; -.
DR   BioGRID; 34367; 22.
DR   DIP; DIP-6368N; -.
DR   IntAct; P48525; 3.
DR   MINT; P48525; -.
DR   STRING; 4932.YOL033W; -.
DR   CarbonylDB; P48525; -.
DR   SwissPalm; P48525; -.
DR   MaxQB; P48525; -.
DR   PaxDb; 4932-YOL033W; -.
DR   PeptideAtlas; P48525; -.
DR   TopDownProteomics; P48525; -.
DR   EnsemblFungi; YOL033W_mRNA; YOL033W; YOL033W.
DR   GeneID; 854124; -.
DR   KEGG; sce:YOL033W; -.
DR   AGR; SGD:S000005393; -.
DR   SGD; S000005393; MSE1.
DR   VEuPathDB; FungiDB:YOL033W; -.
DR   eggNOG; KOG1149; Eukaryota.
DR   GeneTree; ENSGT00390000009759; -.
DR   HOGENOM; CLU_015768_6_3_1; -.
DR   InParanoid; P48525; -.
DR   OMA; ETQMANG; -.
DR   OrthoDB; 5404395at2759; -.
DR   BioCyc; YEAST:G3O-33449-MONOMER; -.
DR   SABIO-RK; P48525; -.
DR   BioGRID-ORCS; 854124; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P48525; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P48525; Protein.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IMP:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; ISA:SGD.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; ISA:SGD.
DR   GO; GO:0070149; P:mitochondrial glutamyl-tRNA aminoacylation; IC:SGD.
DR   GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR   CDD; cd00808; GluRS_core; 1.
DR   Gene3D; 1.10.10.350; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR   InterPro; IPR045462; aa-tRNA-synth_I_cd-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR008925; aa_tRNA-synth_I_cd-bd_sf.
DR   InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR033910; GluRS_core.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00464; gltX_bact; 1.
DR   PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1.
DR   PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF19269; Anticodon_2; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding.
FT   CHAIN           1..536
FT                   /note="Glutamate--tRNA ligase, mitochondrial"
FT                   /id="PRO_0000119740"
FT   MOTIF           53..61
FT                   /note="'HIGH' region"
FT   MOTIF           291..295
FT                   /note="'KMSKS' region"
FT   BINDING         48..50
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         84
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         235..239
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         291..295
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        464
FT                   /note="F -> L (in Ref. 1; AAA61403)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   536 AA;  61603 MW;  5CF36FBAD0E8C58C CRC64;
     MIMLRIPTRS YCSPSKLIKG VGLSPLKKSL LSKKIKEDIH PSLPVRTRFA PSPTGFLHLG
     SLRTALYNYL LARNTNGQFL LRLEDTDQKR LIEGAEENIY EILKWCNINY DETPIKQSER
     KLIYDKYVKI LLSSGKAYRC FCSKERLNDL RHSAMELKPP SMASYDRCCA HLGEEEIKSK
     LAQGIPFTVR FKSPERYPTF TDLLHGQINL QPQVNFNDKR YDDLILVKSD KLPTYHLANV
     VDDHLMGITH VIRGEEWLPS TPKHIALYNA FGWACPKFIH IPLLTTVGDK KLSKRKGDMS
     ISDLKRQGVL PEALINFCAL FGWSPPRDLA SKKHECFSME ELETIFNLNG LTKGNAKVDD
     KKLWFFNKHF LQKRILNPST LRELVDDIMP SLESIYNTST ISREKVAKIL LNCGGSLSRI
     NDFHDEFYYF FEKPKYNDND AVTKFLSKNE SRHIAHLLKK LGQFQEGTDA QEVESMVETM
     YYENGFSRKV TYQAMRFALA GCHPGAKIAA MIDILGIKES NKRLSEGLQF LQREKK
//