SYE2_THEMA
ID SYE2_THEMA Reviewed; 487 AA.
AC Q9X2I8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glutamate--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022};
DE AltName: Full=Glutamyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00022};
DE Short=GluRS 2 {ECO:0000255|HAMAP-Rule:MF_00022};
GN Name=gltX2 {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=TM_1875;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36937.1; -; Genomic_DNA.
DR PIR; F72200; F72200.
DR RefSeq; NP_229671.1; NC_000853.1.
DR PDB; 3AFH; X-ray; 2.00 A; A=2-487.
DR PDB; 3AKZ; X-ray; 2.90 A; A/B/C/D=1-487.
DR PDB; 3AL0; X-ray; 3.37 A; C=1-487.
DR PDBsum; 3AFH; -.
DR PDBsum; 3AKZ; -.
DR PDBsum; 3AL0; -.
DR AlphaFoldDB; Q9X2I8; -.
DR SMR; Q9X2I8; -.
DR DIP; DIP-59231N; -.
DR IntAct; Q9X2I8; 1.
DR STRING; 243274.THEMA_04795; -.
DR EnsemblBacteria; AAD36937; AAD36937; TM_1875.
DR KEGG; tma:TM1875; -.
DR PATRIC; fig|243274.5.peg.1896; -.
DR eggNOG; COG0008; Bacteria.
DR InParanoid; Q9X2I8; -.
DR OMA; WDEGPFF; -.
DR BRENDA; 6.1.1.24; 6331.
DR EvolutionaryTrace; Q9X2I8; -.
DR Proteomes; UP000008183; 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; 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; 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; 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.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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..487
FT /note="Glutamate--tRNA ligase 2"
FT /id="PRO_0000119681"
FT MOTIF 31..41
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 254..258
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:3AFH"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 73..85
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:3AFH"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:3AFH"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3AFH"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:3AKZ"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3AFH"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 317..330
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 333..347
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:3AFH"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:3AKZ"
FT HELIX 373..384
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 392..397
FT /evidence="ECO:0007829|PDB:3AFH"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 404..416
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 423..435
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 441..453
FT /evidence="ECO:0007829|PDB:3AFH"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:3AKZ"
FT HELIX 461..468
FT /evidence="ECO:0007829|PDB:3AFH"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:3AFH"
SQ SEQUENCE 487 AA; 57382 MW; 5E15A2E9E1580791 CRC64;
MFITGAFFDI LEVGPKKIRR CFELVRVRFA PSPTGHLHVG GARTALFNWM FARKEGGKFI
LRIEDTDTER SSREYEQQIL ESLRWCGLDW DEGPDIGGDF GPYRQSERLE IYREYAEKLV
EDKRAYYVVY DKEDPSKELF TTYEYPHEYK EKGHPVTIKF KVLPGKTSFE DLLKGYMEFD
NSTLEDFIIM KSNGFPTYNF AVVVDDHLMR ISHVFRGEDH LSNTPKQLMI YEAFGWEAPV
FMHIPLILGS DRTPLSKRHG ATSVEHFRRE GILSRALMNY LALLGWRVEG DEIFTIEEKL
QSFDPKDISN KGVIFDYQKL EWVNGKHMRR IDLEDLKREF IEWAKYAGKE IPSVDERYFS
ETLRICREKV NTLSQLYDIM YPFMNDDYEY EKDYVEKFLK REEAERVLEE AKKAFKDLNS
WNMEEIEKTL RDLSEKGLAS KKVVFQLIRG AVTGKLVTPG LFETIEVLGK ERTLKRLERT
LQFLKKT
