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D7CCB7 (D7CCB7_STRBB) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 26. Feed History...

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

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 ADI06636.1
Ordered Locus Names:SBI_03515 EMBL ADI06636.1
OrganismStreptomyces bingchenggensis (strain BCW-1) [Complete proteome] [HAMAP] EMBL ADI06636.1
Taxonomic identifier749414 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length486 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

Ontologies

Keywords
   Biological processProtein biosynthesis HAMAP-Rule MF_00022
   Cellular componentCytoplasm HAMAP-Rule MF_00022
   LigandATP-binding HAMAP-Rule MF_00022
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase HAMAP-Rule MF_00022 EMBL ADI06636.1
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglutamyl-tRNA aminoacylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Motif7 – 1711"HIGH" region By similarity HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region By similarity HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity HAMAP-Rule MF_00022

Sequences

Sequence LengthMass (Da)Tools
D7CCB7 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: 531FEC8977AD4A47

FASTA48653,642
        10         20         30         40         50         60 
MRVRFCPSPT GNPHVGLVRT ALFNWAFARH HGGTLVFRIE DTDAARDSEE SYQQLLDAMR 

        70         80         90        100        110        120 
WLGLDWDEGP EIGGPHAPYR QSQRMDLYRD VAERLQESGH AYRCYCTAEE LEERREEARK 

       130        140        150        160        170        180 
AGRPSGYDGK CRTLTAEQRA AYEAEGRSSI VRFRMPDEPI TFTDLVRGEL TFTPENVTDY 

       190        200        210        220        230        240 
GIVRANGAPL YTLVNPVDDA LMEITHVLRG EDLLSSTPRQ IALYRALAEI GVGGGTVPAF 

       250        260        270        280        290        300 
GHLPYVMGEG NKKLSKRDPQ ASLNLYRERG FLPEGLLNYL SLLGWSLAPD RDVFSMDELV 

       310        320        330        340        350        360 
AAFDIAQVNA NPARFDLKKA EAINADHIRQ LDVKAFIEAC GPWLKAPHAP WAPEAFDSAA 

       370        380        390        400        410        420 
FEALAPLAQT RLTVLSDITA NVDFLFLDEP VEDEASWTKA MKPGADALLA SVRTRLAEAE 

       430        440        450        460        470        480 
WDAETLKAAV LAAGEEHGLK LGKAQAPVRV AVTGRTVGLP LFESLEVLGR ERTLARVDAA 


LAKLTA 

« Hide

References

[1]"Genome sequence of the milbemycin-producing bacterium Streptomyces bingchenggensis."
Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L., Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X., Xiang W.S.
J. Bacteriol. 192:4526-4527(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BCW-1 EMBL ADI06636.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002047 Genomic DNA. Translation: ADI06636.1.
RefSeqYP_004961767.1. NC_016582.1.

3D structure databases

ProteinModelPortalD7CCB7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADI06636; ADI06636; SBI_03515.
GeneID11613976.
KEGGsbh:SBI_03515.
PATRIC43264892. VBIStrBin158249_3647.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.

Enzyme and pathway databases

BioCycSBIN749414:GHKA-3537-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.
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]
PANTHERPTHR10119. PTHR10119. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. SSF48163. 1 hit.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD7CCB7_STRBB
AccessionPrimary (citable) accession number: D7CCB7
Entry history
Integrated into UniProtKB/TrEMBL: August 10, 2010
Last sequence update: August 10, 2010
Last modified: February 19, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)