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Q2P5M8 (SYE_XANOM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:XOO1394
OrganismXanthomonas oryzae pv. oryzae (strain MAFF 311018) [Complete proteome] [HAMAP]
Taxonomic identifier342109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length467 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 – 467467Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000237421

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif237 – 2415"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2401ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2P5M8 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 083DB8ACD9431ADF

FASTA46751,649
        10         20         30         40         50         60 
MACRTRFAPS PTGYLHIGGA RTALYCWLEA RRRGGQFVLR IEDTDRQRST QAAIDAILEA 

        70         80         90        100        110        120 
MQWLGLGYDE GPIYQTQRVA RYQEVAEQLL AQGKAYYAYE TREELDAMRE AAMAKQEKPR 

       130        140        150        160        170        180 
YDGAAREQNL PYRDDPNRVI RFKNPIGGTV VFDDLIKGRI EIANSELDDM VIFRPDGLPT 

       190        200        210        220        230        240 
YNFAVVVDDW DMGITEVIRG DDHINNTPRQ INIYAALGAP VPKFAHMPMI LDEQGTKLSK 

       250        260        270        280        290        300 
RTGAADVMQY KDAGYLPHAL INYLARLGWS HGDQELFTPQ ELLDLFDVKD VNSKAARLDM 

       310        320        330        340        350        360 
AKLGWVNQHY LKTDDPASIA PQLEYQLAKL GVDLAAGPAA ADVVVALRER VHTLKEMAEK 

       370        380        390        400        410        420 
AVVWYQPLET YDAAAVMKHL KLGAEVPLGK ARELLAAVDQ WSVDSVSAAL HDAAAALELG 

       430        440        450        460 
MGKVAQPLRV AITGTQVSPD ISQTVYLAGR EGALKRIDAA LTKIGAA 

« Hide

References

[1]"Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of large numbers of effector genes and insertion sequences to its race diversity."
Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.
Jpn. Agric. Res. Q. 39:275-287(2005)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF 311018.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008229 Genomic DNA. Translation: BAE68149.1.
RefSeqYP_450423.1. NC_007705.1.

3D structure databases

ProteinModelPortalQ2P5M8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING342109.XOO_1394.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE68149; BAE68149; BAE68149.
GeneID3857156.
KEGGxom:XOO_1394.
PATRIC24112292. VBIXanOry49434_1577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
KOK01885.
OMARANQGKF.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycXORY342109:GIX9-1418-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_XANOM
AccessionPrimary (citable) accession number: Q2P5M8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 55 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