SYE_SYNP2
ID SYE_SYNP2 Reviewed; 481 AA.
AC P31970; B1XMA4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 4.
DT 03-AUG-2022, entry version 146.
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=SYNPCC7002_A1394;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-160.
RX PubMed=8412664; DOI=10.1111/j.1365-2958.1993.tb01680.x;
RA Zhao J., Snyder W., Muhlenhoff U., Rhiel E., Bryant D.A.;
RT "Cloning and characterization of the psaE gene of the cyanobacterium
RT Synechococcus sp. PCC 7002: characterization of a psaE mutant and
RT overproduction of the protein in Escherichia coli.";
RL Mol. Microbiol. 9:183-194(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}.
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DR EMBL; CP000951; ACA99390.1; -; Genomic_DNA.
DR EMBL; M99379; AAA27356.1; -; Genomic_DNA.
DR RefSeq; WP_012307013.1; NC_010475.1.
DR AlphaFoldDB; P31970; -.
DR SMR; P31970; -.
DR STRING; 32049.SYNPCC7002_A1394; -.
DR EnsemblBacteria; ACA99390; ACA99390; SYNPCC7002_A1394.
DR KEGG; syp:SYNPCC7002_A1394; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_0_3; -.
DR OMA; WDEGPFF; -.
DR Proteomes; UP000001688; 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; 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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..481
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119675"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 249..253
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 252
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 481 AA; 54135 MW; 71E6FB7E30925E49 CRC64;
MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA HHHGGTFVLR VEDTDLERSK PEYTENIKTG
LQWLGLHWDE GPFFQTQRLD QYKAAIQTLL DQGLAYRCYC TPAELEAMRE QQKANNQAPR
YDNRHRNLTE AQRAEFEAQG RKPVIRFKID DAQQIVWQDL IRGTMTWKGS DLGGDMVIAR
TPEGDESFGQ PLYNLAVVVD DIDMQISHVI RGEDHIANTA KQILLYEALG AAVPQFAHTP
LILNQEGRKL SKRDGVTSID DFRQMGFLPQ AIANYMSLLG WTPTDSTQEI FTLEEAAKEF
SLERVNKAGA KFDWDKLDWI NAQYLHQMPI PALTDLLIPY LQAAGYGDYL GDRPWLESLV
ALVAPSLTRL ADVTQETRLL FGDSITLDEK ATAQLQTEGV KVILQEILQN IQASTNFTPD
EAKALINQAT KAHGVKKGVV MKSMRAGLMG ELQGPDLMQS WVLLHQKGWD IERLNQAIAS
I
