(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHP2_GEOS0

ID   A0A0F6BHP2_GEOS0        Unreviewed;       486 AA.
AC   A0A0F6BHP2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 26.
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=GY4MC1_0087 {ECO:0000313|EMBL:ADP72943.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72943.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72943.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72943.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00022};
CC       Note=Binds 1 zinc ion per subunit. {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}.
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DR   EMBL; CP002293; ADP72943.1; -; Genomic_DNA.
DR   RefSeq; WP_003247514.1; NC_014650.1.
DR   EnsemblBacteria; ADP72943; ADP72943; GY4MC1_0087.
DR   GeneID; 29237277; -.
DR   KEGG; gmc:GY4MC1_0087; -.
DR   KO; K09698; -.
DR   OMA; AYYAFDT; -.
DR   OrthoDB; 1409413at2; -.
DR   BioCyc; GSP581103:G1GOQ-114-MONOMER; -.
DR   Proteomes; UP000002034; 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:UniProtKB-UniRule.
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; A0A0F6BHP2.
DR   SWISS-2DPAGE; A0A0F6BHP2.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037, ECO:0000313|EMBL:ADP72943.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00022};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00022,
KW   ECO:0000256|RuleBase:RU363037};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00022};
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   Zinc {ECO:0000256|HAMAP-Rule:MF_00022}.
FT   DOMAIN        4    324       tRNA-synt_1c. {ECO:0000259|Pfam:PF00749}.
FT   MOTIF        11     21       "HIGH" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   MOTIF       253    257       "KMSKS" region. {ECO:0000256|HAMAP-Rule:
FT                                MF_00022}.
FT   METAL       108    108       Zinc. {ECO:0000256|HAMAP-Rule:MF_00022}.
FT   METAL       110    110       Zinc. {ECO:0000256|HAMAP-Rule:MF_00022}.
FT   METAL       136    136       Zinc. {ECO:0000256|HAMAP-Rule:MF_00022}.
FT   METAL       138    138       Zinc. {ECO:0000256|HAMAP-Rule:MF_00022}.
FT   BINDING     256    256       ATP. {ECO:0000256|HAMAP-Rule:MF_00022}.
SQ   SEQUENCE   486 AA;  56080 MW;  18047B9F668E009F CRC64;
     MSQEVRVRYA PSPTGHLHIG GARTALFNYL FARHHNGKFI VRIEDTDIER NVEGGEQSQL
     ENLKWLGIDY DESVDKDGGY GPYRQTERLD IYRKYVNELL EKGYAYKCFC TPEELEQERE
     AQRAAGIAAP QYSGKCRHLT KEQIAQLEAE GKPYTIRVKV PEGKVYEFED IVRGKVTFES
     KDIGDWVIMK ANGIPTYNFA VVIDDHLMKI THVFRGEEHL SNTPKQLMIY DYFGWEPPQF
     GHLTLIVNEN RKKLSKRDES IIQFVSQYKE LGYLPEALFN FFALLGWSPE GEEEIFSKEE
     LIRIFDVSRL SKSPSMFDTK KLTWMNNQYI KKLDLDRLVE ISLPHLIKAG RLPEQMSEEQ
     RQWARDLIAL YQEQMSYGAE IVQLSELFFK EDIEYNEEAK EVLSGEQVPD VLKAFLEEVK
     QLDPFTAENI KAAIKSVQKS TGQKGKKLFM PIRVAATGQT HGPELPVALQ LLGKEKVISR
     LEKVVH
//

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