SYEM_YEAST
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 03-AUG-2022, entry version 168.
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; 18.
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; P48525; -.
DR PRIDE; P48525; -.
DR TopDownProteomics; P48525; -.
DR EnsemblFungi; YOL033W_mRNA; YOL033W; YOL033W.
DR GeneID; 854124; -.
DR KEGG; sce:YOL033W; -.
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; HYINTLP; -.
DR BioCyc; YEAST:G3O-33449-MON; -.
DR SABIO-RK; P48525; -.
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; -; 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 Pfam; PF19269; Anticodon_2; 1.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF48163; SSF48163; 1.
DR TIGRFAMs; TIGR00464; gltX_bact; 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
