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A9W982 (SYE2_METEP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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 2

EC=6.1.1.17
Alternative name(s):
Glutamyl-tRNA synthetase 2
Short name=GluRS 2
Gene names
Name:gltX2
Ordered Locus Names:Mext_4753
OrganismMethylobacterium extorquens (strain PA1) [Complete proteome] [HAMAP]
Taxonomic identifier419610 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length449 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 MF_00022_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449Glutamate--tRNA ligase 2 HAMAP MF_00022_B
PRO_0000367709

Regions

Motif11 – 2111"HIGH" region HAMAP MF_00022_B
Motif242 – 2465"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2451ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A9W982 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8224A7CD69B79AA8

FASTA44948,704
        10         20         30         40         50         60 
MAASPLVRFA PSPTGFLHIG NARPALLNAL FARREGGRFL LRLDDTDRER STEEFATAAA 

        70         80         90        100        110        120 
EDLGWLGIEP DLFFRQSDRT ALYDTAAERL KAAGRLYPCY ETPEELDRRR KRQLGRGLPP 

       130        140        150        160        170        180 
IYDRAALSLT EAERAAFEAD GRQPHWRFKL DHRVVAWNDL VRGESHVDCA SLSDPVLVRA 

       190        200        210        220        230        240 
DGSYLYTLPS VVDDAEVGVT HVIRGEDHVT NTGVQVQLFE ALAAAVPAFG HHNLLTTADG 

       250        260        270        280        290        300 
EGLSKRLGHL SLRSLREAGY EPAAVRSLAV LTGSAEAVRP IASLDELAGL VDLAHLSRAP 

       310        320        330        340        350        360 
ARFDPAELDG MNARLVHDMP LEAVHERLAA LGVPAEAAEA FWLAVRANLG RVSDAAAWWQ 

       370        380        390        400        410        420 
VVNGPVTPVI AEPDFIARAA DLLPEAPFGP GTWKAWTDAV KAETGAKGRA LFMPLRLALT 

       430        440 
GLDHGPDLAA LLPLIGRERA VRRLAGETA 

« Hide

References

[1]"Complete sequence of Methylobacterium extorquens PA1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Marx C., Richardson P.
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000908 Genomic DNA. Translation: ABY33121.1.
RefSeqYP_001642192.1. NC_010172.1.

3D structure databases

ProteinModelPortalA9W982.
ModBaseSearch...

Protein-protein interaction databases

STRINGA9W982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5834557.
GenomeReviewsGene locus Mext_4753 in contig CP000908_GR.
KEGGmex:Mext_4753.
PATRIC22540215. VBIMetExt98426_4839.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMADQERIEW.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycMEXT419610:MEXT_4753-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE2_METEP
AccessionPrimary (citable) accession number: A9W982
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: January 25, 2012
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families