(data stored in SCRATCH zone)

SWISSPROT: D4YXS2_SPHJU

ID   D4YXS2_SPHJU            Unreviewed;       443 AA.
AC   D4YXS2;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   RecName: Full=Glutamate--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            EC=6.1.1.17 {ECO:0000256|HAMAP-Rule:MF_00022};
DE   AltName: Full=Glutamyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022};
DE            Short=GluRS {ECO:0000256|HAMAP-Rule:MF_00022};
GN   Name=gltX {ECO:0000256|HAMAP-Rule:MF_00022,
GN   ECO:0000313|EMBL:BAI95154.1};
GN   OrderedLocusNames=SJA_C1-03200 {ECO:0000313|EMBL:BAI95154.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95154.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95154.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(2010).
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:0000256|HAMAP-Rule:MF_00022}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
CC       diphosphate + L-glutamyl-tRNA(Glu). {ECO:0000256|HAMAP-
CC       Rule:MF_00022}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. Glutamate--tRNA ligase type 1 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00022}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00022}.
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DR   EMBL; AP010803; BAI95154.1; -; Genomic_DNA.
DR   RefSeq; WP_013038941.1; NC_014006.1.
DR   ProteinModelPortal; D4YXS2; -.
DR   STRING; 452662.SJA_C1-03200; -.
DR   EnsemblBacteria; BAI95154; BAI95154; SJA_C1-03200.
DR   GeneID; 29272022; -.
DR   KEGG; sjp:SJA_C1-03200; -.
DR   eggNOG; ENOG4105C20; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000252721; -.
DR   KO; K01885; -.
DR   OMA; LYPCYET; -.
DR   OrthoDB; POG091H021W; -.
DR   Proteomes; UP000007753; Chromosome 1.
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:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
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; 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;
DR   PRODOM; D4YXS2.
DR   SWISS-2DPAGE; D4YXS2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000313|EMBL:BAI95154.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000313|EMBL:BAI95154.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN        3    306       tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}.
FT   MOTIF         9     19       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   MOTIF       240    244       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   BINDING     243    243       ATP. {ECO:0000256|HAMAP-Rule:MF_00022}.
SQ   SEQUENCE   443 AA;  49290 MW;  A51AFFBFB196C172 CRC64;
     MTVITRFAPS PTGNLHVGNI RAALHNWLWA RKSGGRFLLR LDDTDLERSR PEYAQAIKAD
     LRWLGLHWDG EERQSDRFAL YEERFEALKA SGHVYPAYET AQELDLRRKI LLGRGLPPVY
     DRAALSLIPD QIAAYKAEGR QPHWRFKLDH GQPIGWTDLI RGEQRFDPKL LSDPVIRRAD
     GSWLYMLPSV IDDIAMGVTH VLRGEDHVSN TATQIQMFAA LGASLPAFAH EALLTGSEGK
     LSKRLGSLGV AHFREIGLEP AAIASLLARL GSSMPVEPFA DMQPLIDSFD FAHFGRAPAR
     FDEAELATLN QKIVHLLPYA AVADRLPQGM DEAAWDAIRP NLETVSDAAD WWRIVTGPID
     APVPAEEDRD FLALAHDILT ETAFDGAVWR TLTEALKAET GRKGKALFLP LRRALTGMDH
     GPDMGRMLPL IGRDEALSRL KSS
//

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