SYE_XANOR
ID SYE_XANOR Reviewed; 467 AA.
AC Q5H2R3;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=XOO1504;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW74758.1; -; Genomic_DNA.
DR RefSeq; WP_011258289.1; NC_006834.1.
DR PDB; 5H4V; X-ray; 3.00 A; A/B/C/D/E/F=1-467.
DR PDBsum; 5H4V; -.
DR AlphaFoldDB; Q5H2R3; -.
DR SMR; Q5H2R3; -.
DR STRING; 291331.XOO1504; -.
DR EnsemblBacteria; AAW74758; AAW74758; XOO1504.
DR KEGG; xoo:XOO1504; -.
DR HOGENOM; CLU_015768_6_3_6; -.
DR OMA; WDEGPFF; -.
DR Proteomes; UP000006735; 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_0000119705"
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:5H4V"
FT HELIX 17..32
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:5H4V"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:5H4V"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5H4V"
FT TURN 201..206
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:5H4V"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 279..285
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 300..313
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 316..329
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:5H4V"
FT TURN 348..350
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 405..416
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 421..433
FT /evidence="ECO:0007829|PDB:5H4V"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 441..447
FT /evidence="ECO:0007829|PDB:5H4V"
FT HELIX 449..464
FT /evidence="ECO:0007829|PDB:5H4V"
SQ SEQUENCE 467 AA; 51649 MW; 083DB8ACD9431ADF CRC64;
MACRTRFAPS PTGYLHIGGA RTALYCWLEA RRRGGQFVLR IEDTDRQRST QAAIDAILEA
MQWLGLGYDE GPIYQTQRVA RYQEVAEQLL AQGKAYYAYE TREELDAMRE AAMAKQEKPR
YDGAAREQNL PYRDDPNRVI RFKNPIGGTV VFDDLIKGRI EIANSELDDM VIFRPDGLPT
YNFAVVVDDW DMGITEVIRG DDHINNTPRQ INIYAALGAP VPKFAHMPMI LDEQGTKLSK
RTGAADVMQY KDAGYLPHAL INYLARLGWS HGDQELFTPQ ELLDLFDVKD VNSKAARLDM
AKLGWVNQHY LKTDDPASIA PQLEYQLAKL GVDLAAGPAA ADVVVALRER VHTLKEMAEK
AVVWYQPLET YDAAAVMKHL KLGAEVPLGK ARELLAAVDQ WSVDSVSAAL HDAAAALELG
MGKVAQPLRV AITGTQVSPD ISQTVYLAGR EGALKRIDAA LTKIGAA
