SYE_METTH
ID SYE_METTH Reviewed; 553 AA.
AC O26157;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02076};
DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_02076};
DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02076};
DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_02076};
GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_02076}; OrderedLocusNames=MTH_51;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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_02076}.
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_02076};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02076}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC Glutamate--tRNA ligase type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_02076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000666; AAB84558.1; -; Genomic_DNA.
DR PIR; B69167; B69167.
DR RefSeq; WP_010875691.1; NC_000916.1.
DR PDB; 3AII; X-ray; 1.65 A; A=1-553.
DR PDBsum; 3AII; -.
DR AlphaFoldDB; O26157; -.
DR SMR; O26157; -.
DR STRING; 187420.MTH_51; -.
DR EnsemblBacteria; AAB84558; AAB84558; MTH_51.
DR GeneID; 1470013; -.
DR KEGG; mth:MTH_51; -.
DR PATRIC; fig|187420.15.peg.49; -.
DR HOGENOM; CLU_001882_1_3_2; -.
DR OMA; MRFAPNP; -.
DR BRENDA; 6.1.1.17; 7219.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.240.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00749; tRNA-synt_1c; 1.
DR Pfam; PF03950; tRNA-synt_1c_C; 1.
DR PRINTS; PR00987; TRNASYNTHGLU.
DR SUPFAM; SSF50715; SSF50715; 1.
DR TIGRFAMs; TIGR00463; gltX_arch; 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..553
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119721"
FT MOTIF 103..113
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02076"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 172..184
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:3AII"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 333..341
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 355..360
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 386..397
FT /evidence="ECO:0007829|PDB:3AII"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 406..416
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 422..428
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 437..449
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 455..460
FT /evidence="ECO:0007829|PDB:3AII"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 480..486
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 511..516
FT /evidence="ECO:0007829|PDB:3AII"
FT HELIX 518..522
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:3AII"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:3AII"
FT STRAND 543..552
FT /evidence="ECO:0007829|PDB:3AII"
SQ SEQUENCE 553 AA; 63090 MW; C6DB8AE92C2FEE6B CRC64;
MVPVEDLVYR YALLNAVKHR GRANPGAVMG AVMSNEPELR KMAPQVKEAV EAAVERVNSL
SPEEQQQEME RLGLEITERK QKKRKGLREL AGVKGEVVLR FAPNPSGPLH IGHARAAILN
HEYARKYDGR LILRIEDTDP RRVDPEAYDM IPADLEWLGV EWDETVIQSD RMETYYEYTE
KLIERGGAYV CTCRPEEFRE LKNRGEACHC RSLGFRENLQ RWREMFEMKE GSAVVRVKTD
LNHPNPAIRD WVSMRIVEAE HPRTGTRYRV YPMMNFSVAV DDHLLGVTHV LRGKDHLANR
EKQEYLYRHL GWEPPEFIHY GRLKMDDVAL STSGAREGIL RGEYSGWDDP RLGTLRAIAR
RGIRPEAIRK LMVEIGVKIA DSTMSWKKIY GLNRSILEEE ARRYFFAADP VKLEVVGLPG
PVRVERPLHP DHPEIGNRVL ELRGEVYLPG DDLGEGPLRL IDAVNVIYSG GELRYHSEGI
EEARELGASM IHWVPAESAL EAEVIMPDAS RVRGVIEADA SELEVDDVVQ LERFGFARLD
SAGPGMVFYY AHK
