SYE_PROMA
ID SYE_PROMA Reviewed; 476 AA.
AC Q7VDB2;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=Pro_0471;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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; AE017126; AAP99516.1; -; Genomic_DNA.
DR RefSeq; NP_874864.1; NC_005042.1.
DR AlphaFoldDB; Q7VDB2; -.
DR SMR; Q7VDB2; -.
DR STRING; 167539.Pro_0471; -.
DR EnsemblBacteria; AAP99516; AAP99516; Pro_0471.
DR KEGG; pma:Pro_0471; -.
DR PATRIC; fig|167539.5.peg.484; -.
DR eggNOG; COG0008; Bacteria.
DR HOGENOM; CLU_015768_6_0_3; -.
DR OMA; WDEGPFF; -.
DR OrthoDB; 1409413at2; -.
DR Proteomes; UP000001420; 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..476
FT /note="Glutamate--tRNA ligase"
FT /id="PRO_0000119624"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT MOTIF 248..252
FT /note="'KMSKS' region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00022"
SQ SEQUENCE 476 AA; 54477 MW; 0FDDFD8035A9F910 CRC64;
MKVRVRLAPS PTGSLHIGTA RTALFNWLFA QRNKGSFLIR IEDTDKERSK DEFTSNILEG
LQWLGLKWDE APIIQSKRIH EHKEAIKSLI NKGLAYRCFA TEEELQTMRD AQINSGEAPR
YDNRHRKLTK EQEQKFIKDG RSAVIRFRIE DEESVHWNDM VRGPIHWNSK DLGGDMVISR
RAPANEIGDP LYNLVVVLDD AAMEITHVIR GEDHIANTAK QLLLYKALGF KEPSFAHTPL
ILNKDGRKLS KRDGVTSISD FKTMGYTSQA MTNYMTLLGW SPPEGMGEKF TLKESSSVFD
FDRVNNAGAK FDWDKLQWLN SQEIHNWSNE KLLDSLIPLW TKEGWNLSSK DWGLKLVHLI
KPSLILINDG IEESRVFFEE PLLKKDAIQQ LEIPRAKEAL KFICRKLEET PWHGKENEIA
IELITSCSKS LDIKKGIIMK SLRAALLGTL QGPDLITSWG LLAMMENDQA RIKRCL
