ID SYE_CHLP6 Reviewed; 505 AA. AC P59691; F0T375; P94662; Q06560; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 2. DT 27-MAR-2024, entry version 101. 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}; GN OrderedLocusNames=CPSIT_0206, G5O_0208; OS Chlamydophila psittaci (strain ATCC VR-125 / 6BC) (Chlamydia psittaci). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=331636; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-125 / 6BC; RX PubMed=21441521; DOI=10.1128/jb.00236-11; RA Voigt A., Schofl G., Heidrich A., Sachse K., Saluz H.P.; RT "Full-length de novo sequence of the Chlamydophila psittaci type strain, RT 6BC."; RL J. Bacteriol. 193:2662-2663(2011). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-125 / 6BC; RX PubMed=21622741; DOI=10.1128/jb.05277-11; RA Grinblat-Huse V., Drabek E.F., Creasy H.H., Daugherty S.C., Jones K.M., RA Santana-Cruz I., Tallon L.J., Read T.D., Hatch T.P., Bavoil P., Myers G.S.; RT "Genome sequences of the zoonotic pathogens Chlamydia psittaci 6BC and RT Cal10."; RL J. Bacteriol. 193:4039-4040(2011). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-368. RC STRAIN=ATCC VR-125 / 6BC; RX PubMed=8491714; DOI=10.1128/jb.175.10.2936-2942.1993; RA Wichlan D.W., Hatch T.P.; RT "Identification of an early-stage gene of Chlamydia psittaci 6BC."; RL J. Bacteriol. 175:2936-2942(1993). 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 -!- SEQUENCE CAUTION: CC Sequence=AAA23122.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; CP002549; ADZ18786.1; -; Genomic_DNA. DR EMBL; CP002586; AEB55211.1; -; Genomic_DNA. DR EMBL; L13598; AAA23122.1; ALT_INIT; Genomic_DNA. DR PIR; A36909; A36909. DR RefSeq; WP_006342859.1; NC_017287.1. DR AlphaFoldDB; P59691; -. DR SMR; P59691; -. DR GeneID; 12242467; -. DR KEGG; chb:G5O_0208; -. DR KEGG; chp:CPSIT_0206; -. DR PATRIC; fig|331636.3.peg.193; -. DR HOGENOM; CLU_015768_6_3_0; -. 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; HUPs; 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 NCBIfam; TIGR00464; gltX_bact; 1. DR PANTHER; PTHR43311; GLUTAMATE--TRNA LIGASE; 1. DR PANTHER; PTHR43311:SF2; GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF19269; Anticodon_2; 1. DR Pfam; PF00749; tRNA-synt_1c; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF48163; An anticodon-binding domain of class I aminoacyl-tRNA synthetases; 1. DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis. FT CHAIN 1..505 FT /note="Glutamate--tRNA ligase" FT /id="PRO_0000119540" FT MOTIF 12..22 FT /note="'HIGH' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT MOTIF 253..257 FT /note="'KMSKS' region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" FT BINDING 256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022" SQ SEQUENCE 505 AA; 58540 MW; 9D51E741448A9B22 CRC64; MAWENVRVRV APSPTGDPHV GTAYMALFNE IFAKRFNGKM ILRIEDTDQT RSRDDYEKNI FSALKWCGIQ WDEGPDIGGP YGPYRQSERT EIYREYAELL LKTDYAYKCF ATPKELEEMR AVATTLGYRG GYDRRYRYLS PEEIEARTRE GQPYTIRLKV PLTGECVLDD YCKGRVVFPW ADVDDQVLIK SDGFPTYHFA NVVDDHLMGI THVLRGEEWL SSTPKHLLLY EAFGWEAPTF LHMPLLLNPD GTKLSKRKNP TSIFYYRDAG YVKEAFMNFL TLMGYSMEGD EEIYSLEKLI ANFDPRRIGK SGAVFDTRKL DWMNKHYLTH EKSSESLLAK LKDWLINDEF FLKILPLCQS RITTLAEFIG FTGFFFSVLP EYSKEELLPA TIVEEKAAIL LYSYVKYLEK ADLWVKDQFY QGSKWLSSAF QVHHKKVVIP LLYVAITGKK QGLPLFDSME LLGKPRTRAR LVHAQNLLGG VPKKIQTTID KVLKEEDFEN KIFEF //