SYE_MYCGE
ID SYE_MYCGE Reviewed; 484 AA.
AC P47700; Q49256; Q49306; Q49490;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=MG462;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-236.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=1945886; DOI=10.1093/nar/19.21.6027;
RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A random sequencing approach for placing markers on the physical map of
RT Mycoplasma genitalium.";
RL Nucleic Acids Res. 19:6027-6031(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-151 AND 362-484.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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:0000255|HAMAP-
CC Rule:MF_00022}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00022};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 1 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00022}.
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DR EMBL; L43967; AAC72482.1; -; Genomic_DNA.
DR EMBL; X61538; CAA43750.1; -; Genomic_DNA.
DR EMBL; U02183; AAD12469.1; -; Genomic_DNA.
DR EMBL; U02122; AAD12397.1; -; Genomic_DNA.
DR PIR; A64251; A64251.
DR RefSeq; WP_009885570.1; NZ_AAGX01000001.1.
DR AlphaFoldDB; P47700; -.
DR SMR; P47700; -.
DR STRING; 243273.MG_462; -.
DR EnsemblBacteria; AAC72482; AAC72482; MG_462.
DR KEGG; mge:MG_462; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_1_14; -.
DR OMA; WDEGPFF; -.
DR OrthoDB; 1409413at2; -.
DR BioCyc; MGEN243273:G1GJ2-556-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; IPR001412; aa-tRNA-synth_I_CS.
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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..484
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119601"
FT MOTIF 10..20
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 252..256
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT CONFLICT 60
FT /note="D -> EL (in Ref. 3; AAD12469)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="L -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 55941 MW; B1E81B3839A45F6D CRC64;
MEKIRTRYAP SPTGYLHVGG TRTAIFNFLL AKHFNGEFII RIEDTDTERN IKEGINSQFD
NLRWLGVIAD ESVYNPGNYG PYLQSQKLAV YKKLAFDLIE KNLAYRCFCS KEKLESDRKQ
AINNHKTPKY LGHCRNLHSK KITNHLEKND PFTIRLKINN EAEYSWNDLV RGQITIPGSA
LTDIVILKAN GVATYNFAVV IDDYDMEITD VLRGAEHISN TAYQLAIYQA LGFKRIPRFG
HLSVIVDESG KKLSKRDEKT TQFIEQFKQQ GYLPEALLNF LALLGWHPQY NQEFFNLKQL
IENFSLSRVV SAPAFFDIKK LQWINANYIK QLTDNAYFNF IDNYLDVKVD YLKDKNREIS
LLFKNQITHG VQINELIRES FATKIGVENL AKKSHILFKN IKLFLEQLAK SLQGLEEWKA
EQIKTTINKV GAVFNLKGKQ LFMPIRLIFT NKEHGPDLAH IIEIFDKESA INLIKQFINA
TNLF
