(data stored in SCRATCH zone)

SWISSPROT: D6XV80_BACIE

ID   D6XV80_BACIE            Unreviewed;       484 AA.
AC   D6XV80;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 67.
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   OrderedLocusNames=Bsel_0089 {ECO:0000313|EMBL:ADH97638.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97638.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97638.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:
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: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; CP001791; ADH97638.1; -; Genomic_DNA.
DR   RefSeq; WP_013171068.1; NC_014219.1.
DR   STRING; 439292.Bsel_0089; -.
DR   EnsemblBacteria; ADH97638; ADH97638; Bsel_0089.
DR   KEGG; bse:Bsel_0089; -.
DR   eggNOG; ENOG4105C20; Bacteria.
DR   eggNOG; COG0008; LUCA.
DR   HOGENOM; HOG000252720; -.
DR   KO; K09698; -.
DR   OMA; AYYAFDT; -.
DR   OrthoDB; 1409413at2; -.
DR   BioCyc; BSEL439292:G1GLR-113-MONOMER; -.
DR   Proteomes; UP000000271; 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; 3.40.50.620; -; 1.
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; 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;
DR   PRODOM; D6XV80.
DR   SWISS-2DPAGE; D6XV80.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000313|EMBL:ADH97638.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037};
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:UP000000271}.
FT   DOMAIN        5    323       tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}.
FT   MOTIF        11     21       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   MOTIF       252    256       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   BINDING     255    255       ATP. {ECO:0000256|HAMAP-Rule:MF_00022}.
SQ   SEQUENCE   484 AA;  55080 MW;  195F35951F1FCCD7 CRC64;
     MSNDIRVRFA PSPTGHLHIG GARSALFNYL FARNQGGKFI VRIEDTDQAR NVETATEKLM
     ESMKWLGIDW DESVDVGGPH APYRSMERLD LYNRYVDQLL KEGKAFHCYM TEEELEAERE
     EQRKRGETPM YSGRDRHLTD EQKRAYEAEG KKPVVRFMVP KGQEIVVDDA VRGKVTFDSD
     GIGDFVIVRT DGIPTYNFAV TVDDHTMGIS HVIRGEEHLS NAPLQVMLYE ALGFETPTFA
     HASLILNEDR QKMSKRDESI IQFVEQYRDL GYMPEAIVNF IALLGWSPGG EQEIMTKNEL
     IEAFSLDRVV KAPAVFDTKK LSWMNNQYMK EADDDQVVWL AQPHLQKAGK LPEMMSDEQK
     QWAYDLIVLH KEKMDCGADI VPLTELFFQD EIEYDEDAKA ILGEEQVPEV LEAFLKNLDS
     LEEFEAAAIK KAMKDVQKST GHKGKKLFMP IRVAVSGQQH GPDLPQMIAL LGRTVVTTRL
     KGLL
//

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