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B3PN19 (SYE_MYCA5) 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:MARTH_orf641
OrganismMycoplasma arthritidis (strain 158L3-1) [Complete proteome] [HAMAP]
Taxonomic identifier243272 [NCBI]
Taxonomic lineageBacteriaTenericutesMollicutesMycoplasmataceaeMycoplasma

Protein attributes

Sequence length464 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 – 464464Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090090

Regions

Motif11 – 2111"HIGH" region HAMAP-Rule MF_00022
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2561ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3PN19 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 151CEA98284D39AE

FASTA46453,707
        10         20         30         40         50         60 
MNKTIRTRYA PSPTGYLHIG GARTALFCYL FAKHSNGDFI FRLEDTDVER NVEGGEASQL 

        70         80         90        100        110        120 
NNLAWLGIVP DESPLKPNPK YGKYRQSEKL AIYQAYIDEL IKQGLAYKAY DSSEELAKQH 

       130        140        150        160        170        180 
EEQEKAGVAS FRYDPTWLKL SESEIKRRDE AKEYSIRLKL PKNKNYSWDD LVRGPISVNS 

       190        200        210        220        230        240 
DDIGDFVIMK SDGYPTYNFA VVVDDHQMDI THVLRGEEHI TNTPKQLAIY EAFGWDNPVF 

       250        260        270        280        290        300 
GHLTIITNME GKKLSKRDKS LKQFIEDYKN EGYCPEAIFN FLALLGWTSG DKTEIMSHDE 

       310        320        330        340        350        360 
LIKKFDYNRL SKSPSKFDIV KMEWFSKQYM KKLPNEVIIE KINSPKDAQW NNLFVETYKQ 

       370        380        390        400        410        420 
QAATISEIKE NLKIYLFPKE KLELQIDNDL VVKTFFAHLK AKDFTIENIQ AAIDETKNAL 

       430        440        450        460 
NVKGKDLFMP IRITATYEEH GPELAKAIYL FGKDLVYKRL TKWS 

« Hide

References

[1]"Genome of Mycoplasma arthritidis."
Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H., Loraine A.E.
Infect. Immun. 76:4000-4008(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 158L3-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001047 Genomic DNA. Translation: ACF07421.1.
RefSeqYP_002000125.1. NC_011025.1.

3D structure databases

ProteinModelPortalB3PN19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243272.MARTH_orf641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF07421; ACF07421; MARTH_orf641.
GeneID6418126.
KEGGmat:MARTH_orf641.
PATRIC20004069. VBIMycArt31993_0460.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMART243272:GHIZ-483-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_MYCA5
AccessionPrimary (citable) accession number: B3PN19
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 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