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P0A636 (SYE_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--tRNA ligase
EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS
Gene names
Name:gltX
Synonyms:gltS
Ordered Locus Names:Rv2992c, MT3070
ORF Names:MTV012.06c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Subcellular location

Cytoplasm By similarity.

Miscellaneous

Was identified as a high-confidence drug target. HAMAP-Rule MF_00022

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119610

Regions

Motif13 – 2311"HIGH" region HAMAP-Rule MF_00022
Motif257 – 2615"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2601ATP By similarity

Secondary structure

1 .................................................................................... 490
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A636 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: DE4EA5D5C7B9AD7E

FASTA49053,864
        10         20         30         40         50         60 
MTATETVRVR FCPSPTGTPH VGLVRTALFN WAYARHTGGT FVFRIEDTDA QRDSEESYLA 

        70         80         90        100        110        120 
LLDALRWLGL DWDEGPEVGG PYGPYRQSQR AEIYRDVLAR LLAAGEAYHA FSTPEEVEAR 

       130        140        150        160        170        180 
HVAAGRNPKL GYDNFDRHLT DAQRAAYLAE GRQPVVRLRM PDDDLAWNDL VRGPVTFAAG 

       190        200        210        220        230        240 
SVPDFALTRA SGDPLYTLVN PCDDALMKIT HVLRGEDLLP STPRQLALHQ ALIRIGVAER 

       250        260        270        280        290        300 
IPKFAHLPTV LGEGTKKLSK RDPQSNLFAH RDRGFIPEGL LNYLALLGWS IADDHDLFGL 

       310        320        330        340        350        360 
DEMVAAFDVA DVNSSPARFD QKKADALNAE HIRMLDVGDF TVRLRDHLDT HGHHIALDEA 

       370        380        390        400        410        420 
AFAAAAELVQ TRIVVLGDAW ELLKFFNDDQ YVIDPKAAAK ELGPDGAAVL DAALAALTSV 

       430        440        450        460        470        480 
TDWTAPLIEA ALKDALIEGL ALKPRKAFSP IRVAATGTTV SPPLFESLEL LGRDRSMQRL 

       490 
RAARQLVGHA

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842581 Genomic DNA. Translation: CAE55534.1.
AE000516 Genomic DNA. Translation: AAK47399.1.
AL123456 Genomic DNA. Translation: CCP45797.1.
PIRC70854.
RefSeqNP_337585.1. NC_002755.2.
YP_006516448.1. NC_018143.1.
YP_177915.1. NC_000962.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JA2X-ray1.65A1-490[»]
3PNVX-ray1.95A/B1-490[»]
3PNYX-ray1.70A/B1-490[»]
ProteinModelPortalP0A636.
SMRP0A636. Positions 1-485.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv2992c.

Proteomic databases

PaxDbP0A636.
PRIDEP0A636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK47399; AAK47399; MT3070.
GeneID13317791.
887850.
925203.
KEGGmtc:MT3070.
mtu:Rv2992c.
mtv:RVBD_2992c.
PATRIC18128518. VBIMycTub22151_3357.

Organism-specific databases

TubercuListRv2992c.

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAYESMELL.
ProtClustDBPRK01406.

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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A636.

Entry information

Entry nameSYE_MYCTU
AccessionPrimary (citable) accession number: P0A636
Secondary accession number(s): L0TE59, O53241
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents