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B1AJP0 (SYE_UREP2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:UPA3_0639
OrganismUreaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736) [Complete proteome] [HAMAP]
Taxonomic identifier505682 [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_1000074340

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
B1AJP0 [UniParc].

Last modified April 8, 2008. 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]"Genome sequence of Ureaplasma parvum serovar 3."
Methe B.A., Glass J., Waites K., Shrivastava S.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27815 / 27 / NCTC 11736.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000942 Genomic DNA. Translation: ACA32816.1.
RefSeqYP_001752684.1. NC_010503.1.

3D structure databases

ProteinModelPortalB1AJP0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING505682.UPA3_0639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA32816; ACA32816; UPA3_0639.
GeneID6155412.
KEGGupa:UPA3_0639.
PATRIC20533505. VBIUrePar123156_0609.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycUPAR505682:GHAZ-643-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_UREP2
AccessionPrimary (citable) accession number: B1AJP0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 41 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