(data stored in ACNUC7421 zone)

HOGENOM: MYCTK_1_PE1000

ID   MYCTK_1_PE1000                       STANDARD;      PRT;   490 AA.
AC   MYCTK_1_PE1000; C6DW57;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Glutamyl-tRNA synthetase; EC=6.1.1 17;AltName:
DE   Full=Glutamate--tRNA ligase; (MYCTK_1.PE1000).
GN   Name=gltX; OrderedLocusNames=TBMG_00977;
OS   MYCOBACTERIUM TUBERCULOSIS KZN 1435.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium; Mycobacterium
OC   tuberculosis complex.
OX   NCBI_TaxID=478434;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MYCTK_1.PE1000.
CC       Mycobacterium tuberculosis KZN 1435, complete genome.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C6DW57_MYCTK
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) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- GENE_FAMILY: HOG000252720 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6DW57; -.
DR   EMBL; CP001658; ACT24021.1; -; Genomic_DNA.
DR   RefSeq; YP_003030916.1; NC_012943.1.
DR   ProteinModelPortal; C6DW57; -.
DR   STRING; C6DW57; -.
DR   EnsemblBacteria; EBMYCT00000093040; EBMYCP00000089017; EBMYCG00000094399.
DR   GeneID; 8162268; -.
DR   GenomeReviews; CP001658_GR; TBMG_00977.
DR   KEGG; mtb:TBMG_00977; -.
DR   GeneTree; EBGT00050000016746; -.
DR   ProtClustDB; PRK01406; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00022_B; Glu_tRNA_synth_B; 1; -.
DR   InterPro; IPR008925; aa-tRNA-synth_I_codon-bd.
DR   InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2.
DR   InterPro; IPR004527; Glu-tRNA-synth_Ib_bac/mito.
DR   InterPro; IPR000924; Glu/Gln-tRNA-synth_Ib.
DR   InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl.
DR   InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:1.10.1160.10; Glu/Gln-tRNA-synth_Ic_a-bdl; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 2.
DR   Gene3D; G3DSA:1.10.10.350; tRNA_synt_bd; 1.
DR   PANTHER; PTHR10119; Glu_tRNA-synt_1c; 1.
DR   Pfam; PF00749; tRNA-synt_1c; 1.
DR   PRINTS; PR00987; TRNASYNTHGLU.
DR   SUPFAM; SSF48163; tRNA-synt_bind; 1.
DR   TIGRFAMs; TIGR00464; GltX_bact; 1.
DR   HOGENOMDNA; MYCTK_1.PE1000; -.
KW   glutamyl-tRNA synthetase;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   490 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTATETVRVR FCPSPTGTPH VGLVRTALFN WAYARHTGGT FVFRIEDTDA QRDSEESYLA
     LLDALRWLGL DWDEGPEVGG PYGPYRQSQR AEIYRDVLAR LLAAGEAYHA FSTPEEVEAR
     HVAAGRNPKL GYDNFDRHLT DAQRAAYLAE GRQPVVRLRM PDDDLAWNDL VRGPVTFAAG
     SVPDFALTRA SGDPLYTLVN PCDDALMKIT HVLRGEDLLP STPRQLALHQ ALIRIGVAER
     IPKFAHLPTV LGEGTKKLSK RDPQSNLFAH RDRGFIPEGL LNYLALLGWS IADDHDLFGL
     DEMVAAFDVA DVNSSPARFD QKKADALNAE HIRMLDVGDF TVRLRDHLDT HGHHIALDEA
     AFAAAAELVQ TRIVVLGDAW ELLKFFNDDQ YVIDPKAAAK ELGPDGAAVL DAALAALTSV
     TDWTAPLIEA ALKDALIEGL ALKPRKAFSP IRVAATGTTV SPPLFESLEL LGRDRSMQRL
     RAARQLVGHA
//

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