SYE_STRMK
ID SYE_STRMK Reviewed; 467 AA.
AC B2FHI7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Smlt1441;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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}.
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; AM743169; CAQ44980.1; -; Genomic_DNA.
DR RefSeq; WP_012479577.1; NC_010943.1.
DR PDB; 7K86; X-ray; 2.05 A; A/B=1-467.
DR PDBsum; 7K86; -.
DR AlphaFoldDB; B2FHI7; -.
DR SMR; B2FHI7; -.
DR STRING; 522373.Smlt1441; -.
DR EnsemblBacteria; CAQ44980; CAQ44980; Smlt1441.
DR KEGG; sml:Smlt1441; -.
DR PATRIC; fig|522373.3.peg.1379; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_0_6; -.
DR OMA; HYINTLP; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000008840; 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:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 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..467
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_1000090111"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 237..241
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:7K86"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:7K86"
FT TURN 124..128
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:7K86"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 257..268
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:7K86"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:7K86"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 354..361
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 384..396
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 403..417
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:7K86"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:7K86"
FT HELIX 441..463
FT /evidence="ECO:0007829|PDB:7K86"
SQ SEQUENCE 467 AA; 51958 MW; A0FE17022FCF539B CRC64;
MTCRTRFAPS PTGYLHIGGA RTALYCWLEA RHRGGEFVLR IEDTDRERST QGAIDAILEA
MEWLGLDYDE GPIYQTDRVA RYLEVAEQLV ADGKAYYAYE TREELDAMRE AAMARQEKPR
YNGAARDLGL PRRDDPNRVI RFKNPLEGTV VFDDLIKGRI EIANSELDDM VIFRPDGYPT
YNFAVVVDDW DMGITEVIRG DDHINNTPRQ INLYEGIGAP VPKFGHMPMI LDEQGAKLSK
RTGAADVMQY KDAGYLPDAL LSYLARLGWS HGDQELFSRQ ELIELFDVKD CNSKASRLDM
AKLGWVNQHF LKTEDVAAIV PHLVYQLQKL GLDVAAGPAP EDVVVALRER VQTLKEMAEK
AVVWYQPLTE YDEAAVAKHF KAGAEVALGK ARELLAALPE WTAESVGVAL HDAAAALEIG
MGKVAQPLRV AITGTQVSPD ISHTVYLAGR EQALKRIDVA ITKVATA
