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Q7VDB2 (SYE_PROMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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
Ordered Locus Names:Pro_0471
OrganismProchlorococcus marinus (strain SARG / CCMP1375 / SS120) [Reference proteome] [HAMAP]
Taxonomic identifier167539 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length476 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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference 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

Molecule processing

Chain1 – 476476Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119624

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VDB2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 0FDDFD8035A9F910

FASTA47654,477
        10         20         30         40         50         60 
MKVRVRLAPS PTGSLHIGTA RTALFNWLFA QRNKGSFLIR IEDTDKERSK DEFTSNILEG 

        70         80         90        100        110        120 
LQWLGLKWDE APIIQSKRIH EHKEAIKSLI NKGLAYRCFA TEEELQTMRD AQINSGEAPR 

       130        140        150        160        170        180 
YDNRHRKLTK EQEQKFIKDG RSAVIRFRIE DEESVHWNDM VRGPIHWNSK DLGGDMVISR 

       190        200        210        220        230        240 
RAPANEIGDP LYNLVVVLDD AAMEITHVIR GEDHIANTAK QLLLYKALGF KEPSFAHTPL 

       250        260        270        280        290        300 
ILNKDGRKLS KRDGVTSISD FKTMGYTSQA MTNYMTLLGW SPPEGMGEKF TLKESSSVFD 

       310        320        330        340        350        360 
FDRVNNAGAK FDWDKLQWLN SQEIHNWSNE KLLDSLIPLW TKEGWNLSSK DWGLKLVHLI 

       370        380        390        400        410        420 
KPSLILINDG IEESRVFFEE PLLKKDAIQQ LEIPRAKEAL KFICRKLEET PWHGKENEIA 

       430        440        450        460        470 
IELITSCSKS LDIKKGIIMK SLRAALLGTL QGPDLITSWG LLAMMENDQA RIKRCL 

« Hide

References

[1]"Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a nearly minimal oxyphototrophic genome."
Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M., Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J., Tandeau de Marsac N., Weissenbach J. expand/collapse author list , Wincker P., Wolf Y.I., Hess W.R.
Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SARG / CCMP1375 / SS120.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017126 Genomic DNA. Translation: AAP99516.1.
RefSeqNP_874864.1. NC_005042.1.

3D structure databases

ProteinModelPortalQ7VDB2.
SMRQ7VDB2. Positions 2-476.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167539.Pro0471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP99516; AAP99516; Pro_0471.
GeneID1461853.
KEGGpma:Pro_0471.
PATRIC23027567. VBIProMar8617_0484.

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPMAR167539:GJN2-487-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_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.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_PROMA
AccessionPrimary (citable) accession number: Q7VDB2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries