ID SYE_SODGM Reviewed; 473 AA.
AC Q2NSC4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 18-JAN-2017, entry version 72.
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=SG1676;
OS Sodalis glossinidius (strain morsitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Sodalis.
OX NCBI_TaxID=343509;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=morsitans;
RX PubMed=16365377; DOI=10.1101/gr.4106106;
RA Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA Hattori M., Aksoy S.;
RT "Massive genome erosion and functional adaptations provide insights
RT into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT host.";
RL Genome Res. 16:149-156(2006).
CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a
CC two-step reaction: glutamate is first activated by ATP to form
CC Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
CC {ECO:0000255|HAMAP-Rule:MF_00022}.
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC diphosphate + L-glutamyl-tRNA(Glu). {ECO:0000255|HAMAP-
CC Rule:MF_00022}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00022};
CC Note=Binds 1 zinc ion per subunit. {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
CC family. Glutamate--tRNA ligase type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00022}.
DR EMBL; AP008232; BAE74951.1; -; Genomic_DNA.
DR RefSeq; WP_011411501.1; NC_007712.1.
DR ProteinModelPortal; Q2NSC4; -.
DR STRING; 343509.SG1676; -.
DR PRIDE; Q2NSC4; -.
DR EnsemblBacteria; BAE74951; BAE74951; SG1676.
DR KEGG; sgl:SG1676; -.
DR PATRIC; 23653428; VBISodGlo61428_4003.
DR eggNOG; ENOG4105C20; Bacteria.
DR eggNOG; COG0008; LUCA.
DR KO; K01885; -.
DR OMA; HGATNVM; -.
DR OrthoDB; POG091H021W; -.
DR Proteomes; UP000001932; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
DR CDD; cd00808; GluRS_core; 1.
DR Gene3D; 1.10.10.350; -; 1.
DR Gene3D; 1.10.1160.10; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00022; Glu_tRNA_synth_type1; 1.
DR InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004527; Glu-tRNA-ligase_bac/mito.
DR InterPro; IPR000924; Glu/Gln-tRNA-synth.
DR InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
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; 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; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1 473 Glutamate--tRNA ligase.
FT /FTId=PRO_0000237402.
FT MOTIF 9 19 "HIGH" region. {ECO:0000255|HAMAP-
FT Rule:MF_00022}.
FT MOTIF 237 241 "KMSKS" region. {ECO:0000255|HAMAP-
FT Rule:MF_00022}.
FT METAL 98 98 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}.
FT METAL 100 100 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}.
FT METAL 125 125 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}.
FT METAL 127 127 Zinc. {ECO:0000255|HAMAP-Rule:MF_00022}.
FT BINDING 240 240 ATP. {ECO:0000255|HAMAP-Rule:MF_00022}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 2 461 ihamap:Glu_tRNA_synth_type1 [T]
FT MYHIT 9 20 ipat:AA_TRNA_LIGASE_I [T]
FT MYHIT 2 305 ipfam:tRNA-synt_1c [T]
SQ SEQUENCE 473 AA; 52969 MW; 756D0593D9FE2489 CRC64;
MKIKTRFAPS PTGYLHVGGA RTALYSWLFA RHLGGEFLLR IEDTDLERST QPAIDAIMDG
MNWLNLDWDE GPYFQTKRFD RYNAVIDDML SKGTAYHCYC SKERLETLRE AQMARGEKPR
YDGRCRDSHE HHADDEPCVV RFRNPQDGSV VFNDLIRGPI EFSNQELDDL IIRRIDGSPT
YNFCVVVDDF DMAITHVIRG EDHINNTPRQ INILKALGAP VPAYAHVSMI LGDDGKKLSK
RHGAVGVMQY RDDGFLPEAL LNYLVRLGWS HGDQEIFSVD EMKQLFSFEA VSKSASAFNT
EKLLWLNHHY INHLPADYVA THLVLHIEQQ GIDTRTGPQL AALVKLLGER CKTLKEIAAS
CRYFYEDFSE FDADAAKKHL RPVAVLALEA VRANLAALSE WTPATVHAAI EQTAEALQVG
MGKVGMPLRV AVTGTGQSPA LDVTVHAIGQ SRCLARIVKA LDFIACRTQE SAG
//
|
