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D5DVR1 (D5DVR1_BACMQ) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase HAMAP-Rule MF_00022

EC=6.1.1.17 HAMAP-Rule MF_00022
Alternative name(s):
Glutamyl-tRNA synthetase HAMAP-Rule MF_00022
Gene names
Name:gltX HAMAP-Rule MF_00022 EMBL ADE67226.1
Ordered Locus Names:BMQ_0113 EMBL ADE67226.1
OrganismBacillus megaterium (strain ATCC 12872 / QMB1551) [Complete proteome] [HAMAP] EMBL ADE67226.1
Taxonomic identifier545693 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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) By similarity. HAMAP-Rule MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP-Rule MF_00022

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00022

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00022.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. HAMAP-Rule MF_00022 RuleBase RU003489

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif11 – 2111"HIGH" region By similarity HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region By similarity HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
D5DVR1 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 8CA5C5985F6CB3AF

FASTA48555,743
        10         20         30         40         50         60 
MSSEVRVRYA PSPTGHLHIG NARTALFNYL FARNQNGKFI IRIEDTDQKR NIEGGEESQL 

        70         80         90        100        110        120 
RYLKWLGIEW DESIDVGGEY GPYRQSERTE IYQKYTEELL EKGLAYHCYC TSEELEKERE 

       130        140        150        160        170        180 
EQQANSQMPR YSGKCRNLTA EQRAELEAEG REPSIRFRVP SNKEIKWNDI VKDEVSFESE 

       190        200        210        220        230        240 
GIGDFVIVKK DGTPTYNYAV AIDDYLMKMT HVLRGDDHIS NTPKQILVYE ALGWTPPVFG 

       250        260        270        280        290        300 
HMTLIVNENR RKLSKRDESI IQFIEQYKEL GYLPEALFNF ITMLGWSPVG EEEIFSKEQF 

       310        320        330        340        350        360 
IEIFDPARLS KSPALFDTSK LRWMNNQYMK QLDLDEVVAL SVPHLVKAGK VEETRDAETE 

       370        380        390        400        410        420 
QWVRDLVALY QEQMSFGAEI VELTEMFFKK EIDYSEEAKA VLAEEQVPEV LKAFAEEISS 

       430        440        450        460        470        480 
LEEFSADEIK AATKAVQKAT GQKGKKLFMP IRVATTGETH GPELPKAISL LGKETVLARL 


ESIYS 

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References

[1]"Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure."
Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12872 / QMB1551.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001983 Genomic DNA. Translation: ADE67226.1.
RefSeqYP_003560660.1. NC_014019.1.

3D structure databases

ProteinModelPortalD5DVR1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE67226; ADE67226; BMQ_0113.
GeneID8984551.
KEGGbmq:BMQ_0113.
PATRIC35476829. VBIBacMeg35839_0167.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000252720.
KOK09698.

Enzyme and pathway databases

BioCycBMEG545693:GHSY-113-MONOMER.

Family and domain databases

Gene3D1.10.10.350. 1 hit.
1.10.1160.10. 1 hit.
3.40.50.620. 2 hits.
HAMAPMF_00022_B. Glu_tRNA_synth_B.
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-ligase_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD5DVR1_BACMQ
AccessionPrimary (citable) accession number: D5DVR1
Entry history
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: May 29, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)