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Protein

Glutamate--tRNA ligase

Gene

gltX

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).UniRule annotation

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei255 – 2551ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-tRNA ligase activity Source: UniProtKB-HAMAP
  3. tRNA binding Source: InterPro

GO - Biological processi

  1. glutamyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--tRNA ligaseUniRule annotation (EC:6.1.1.17UniRule annotation)
Alternative name(s):
Glutamyl-tRNA synthetaseUniRule annotation
Short name:
GluRSUniRule annotation
Gene namesi
Name:gltXUniRule annotation
Ordered Locus Names:BCE_0087
OrganismiBacillus cereus (strain ATCC 10987)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002527 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 485485Glutamate--tRNA ligasePRO_0000119499Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi222523.BCE_0087.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi11 – 2111"HIGH" regionAdd
BLAST
Motifi252 – 2565"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiKLNWINS.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q73FB9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKQVRVRYA PSPTGHLHIG NARTALFNYL FARHQDGKFI IRIEDTDVKR
60 70 80 90 100
NVAGGEESQL KYLKWLGMDW DEGVDVGGEF GPYRQTERLD IYKKLYEDLL
110 120 130 140 150
ERGLAYKCYM TEEELEAERE GQIARGETPR YAGNHRDLTE AQVKEFEAEG
160 170 180 190 200
RIPSIRFRVP ADRDYTFKDI VKDEVAFHSN DFGDFVIVKK DGIPTYNFAV
210 220 230 240 250
AVDDHLMEIT HVLRGDDHIS NTPKQMMIYE AFGWDIPQFG HMTLIVNESR
260 270 280 290 300
KKLSKRDESI IQFIEQYKEL GYLPEAIFNF IALLGWSPVG EEEIFSQEEF
310 320 330 340 350
IKMFDAARLS KSPALFDSQK LKWMNNQYMK KQDLDTVVEL SLPHLVKAGR
360 370 380 390 400
IGETLSEQEQ AWIRDVIALY HEQMSFGAEI VELSEMFFKD HVDYEEEGQE
410 420 430 440 450
VLKGEQVPEV LRAFAGQVEA LEAMEPAAIK AAIKAVQKET GHKGKNLFMP
460 470 480
IRVATTGQTH GPELPNAIAL LGKEKVLXRL QKVIG
Length:485
Mass (Da):55,613
Last modified:July 5, 2004 - v1
Checksum:iBE6D96D48A9259BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS39023.1.
RefSeqiNP_976415.1. NC_003909.8.
WP_000415155.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS39023; AAS39023; BCE_0087.
KEGGibca:BCE_0087.
PATRICi18848998. VBIBacCer118379_0083.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS39023.1.
RefSeqiNP_976415.1. NC_003909.8.
WP_000415155.1. NC_003909.8.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi222523.BCE_0087.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS39023; AAS39023; BCE_0087.
KEGGibca:BCE_0087.
PATRICi18848998. VBIBacCer118379_0083.

Phylogenomic databases

eggNOGiCOG0008.
HOGENOMiHOG000252720.
KOiK09698.
OMAiKLNWINS.
OrthoDBiEOG6DRPF7.

Family and domain databases

Gene3Di1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPiMF_00022_B. Glu_tRNA_synth_B.
InterProiIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_bac/mito.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SUPFAMiSSF48163. SSF48163. 1 hit.
TIGRFAMsiTIGR00464. gltX_bact. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987.

Entry informationi

Entry nameiSYE_BACC1
AccessioniPrimary (citable) accession number: Q73FB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.