SYE_MYCTU
ID SYE_MYCTU Reviewed; 490 AA.
AC P9WFV9; L0TE59; O53241; P0A636;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
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}; Synonyms=gltS;
GN OrderedLocusNames=Rv2992c; ORFNames=MTV012.06c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
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; AL123456; CCP45797.1; -; Genomic_DNA.
DR PIR; C70854; C70854.
DR RefSeq; WP_003415122.1; NZ_NVQJ01000041.1.
DR RefSeq; YP_177915.1; NC_000962.3.
DR PDB; 2JA2; X-ray; 1.65 A; A=1-490.
DR PDB; 3PNV; X-ray; 1.95 A; A/B=1-490.
DR PDB; 3PNY; X-ray; 1.70 A; A/B=1-490.
DR PDBsum; 2JA2; -.
DR PDBsum; 3PNV; -.
DR PDBsum; 3PNY; -.
DR AlphaFoldDB; P9WFV9; -.
DR SASBDB; P9WFV9; -.
DR SMR; P9WFV9; -.
DR STRING; 83332.Rv2992c; -.
DR PaxDb; P9WFV9; -.
DR DNASU; 887850; -.
DR GeneID; 887850; -.
DR KEGG; mtu:Rv2992c; -.
DR PATRIC; fig|83332.111.peg.3335; -.
DR TubercuList; Rv2992c; -.
DR eggNOG; COG0008; Bacteria.
DR OMA; WDEGPFF; -.
DR PhylomeDB; P9WFV9; -.
DR BRENDA; 6.1.1.17; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; 1.10.1160.10; -; 1.
DR Gene3D; 1.10.8.70; -; 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; IPR020752; Glu-tRNA-synth_I_codon-bd_sub1.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020061; Glu_tRNA_lig_a-bdl.
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 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..490
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119610"
FT MOTIF 13..23
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 257..261
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:2JA2"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2JA2"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2JA2"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:3PNY"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 267..273
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 359..369
FT /evidence="ECO:0007829|PDB:2JA2"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:3PNV"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 379..383
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:2JA2"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 395..401
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 404..418
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 425..436
FT /evidence="ECO:0007829|PDB:2JA2"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:2JA2"
FT STRAND 457..460
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 464..471
FT /evidence="ECO:0007829|PDB:2JA2"
FT HELIX 473..483
FT /evidence="ECO:0007829|PDB:2JA2"
SQ SEQUENCE 490 AA; 53864 MW; DE4EA5D5C7B9AD7E CRC64;
MTATETVRVR FCPSPTGTPH VGLVRTALFN WAYARHTGGT FVFRIEDTDA QRDSEESYLA
LLDALRWLGL DWDEGPEVGG PYGPYRQSQR AEIYRDVLAR LLAAGEAYHA FSTPEEVEAR
HVAAGRNPKL GYDNFDRHLT DAQRAAYLAE GRQPVVRLRM PDDDLAWNDL VRGPVTFAAG
SVPDFALTRA SGDPLYTLVN PCDDALMKIT HVLRGEDLLP STPRQLALHQ ALIRIGVAER
IPKFAHLPTV LGEGTKKLSK RDPQSNLFAH RDRGFIPEGL LNYLALLGWS IADDHDLFGL
DEMVAAFDVA DVNSSPARFD QKKADALNAE HIRMLDVGDF TVRLRDHLDT HGHHIALDEA
AFAAAAELVQ TRIVVLGDAW ELLKFFNDDQ YVIDPKAAAK ELGPDGAAVL DAALAALTSV
TDWTAPLIEA ALKDALIEGL ALKPRKAFSP IRVAATGTTV SPPLFESLEL LGRDRSMQRL
RAARQLVGHA
