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Q9PPP0 (SYE_UREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 75. 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:UU599
OrganismUreaplasma parvum serovar 3 (strain ATCC 700970) [Complete proteome] [HAMAP]
Taxonomic identifier273119 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeUreaplasma

Protein attributes

Sequence length482 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
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 – 482482Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119690

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PPP0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3977C1BCFA31C16C

FASTA48255,909
        10         20         30         40         50         60 
MKIRTRYAPS PTGYLHIGGA RTALFNYLLA KAYGGDFIIR IEDTDIERNV EGGINSQLDF 

        70         80         90        100        110        120 
LAWMGIIPDE SIRNPKAFGP YIQSEKLKHY EKLALDLVDQ KKAYFCFCSK EQLDADRELA 

       130        140        150        160        170        180 
EKSHQTPKYK RHCLNLDKKT IESNLLQNKE YTIRLKINEN MEYSWDDLIR GKISIPGSAL 

       190        200        210        220        230        240 
TDPVILKSNK IAMYNFAVVI DDYEMQISHV IRGEEHISNT PYQLAIAQAL NYDITKIKYG 

       250        260        270        280        290        300 
HLSIIVDETG KKLSKRNLSL KQFVSDYEKD GYWPHAITNF VALLGWSPKN NDEIMSLETM 

       310        320        330        340        350        360 
IKNFDINNLS KSPAFFDINK MNWFSTQYFN NITQEEFINF IKKHSLTKEL VLNDYTFINK 

       370        380        390        400        410        420 
CLLFKSHIIN LKQLIDLVIE QFNCDKKVLA SDVDYIKKNQ LITVVRVFYE QLIINDEFNE 

       430        440        450        460        470        480 
EFIKEIIKKV QIITNNKGAN LYMPIRIATT FSSHGPELAK TICYLGREKV LKNLINILKI 


LD 

« Hide

References

[1]"The complete sequence of the mucosal pathogen Ureaplasma urealyticum."
Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y., Cassell G.H.
Nature 407:757-762(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700970.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF222894 Genomic DNA. Translation: AAF31013.1.
RefSeqNP_078438.1. NC_002162.1.

3D structure databases

ProteinModelPortalQ9PPP0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273119.UU599.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF31013; AAF31013; UU599.
GeneID876116.
KEGGuur:UU599.
PATRIC20534835. VBIUrePar45146_0622.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycUPAR273119:GHVP-640-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_UREPA
AccessionPrimary (citable) accession number: Q9PPP0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 75 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