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A3PMJ1 (SYE2_RHOS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:Rsph17029_2455
OrganismRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) [Complete proteome] [HAMAP]
Taxonomic identifier349101 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length441 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 – 441441Glutamate--tRNA ligase 2 HAMAP-Rule MF_00022
PRO_0000367748

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif239 – 2435"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2421ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PMJ1 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: EB0754DDC9C4812D

FASTA44149,077
        10         20         30         40         50         60 
MTTVTRFAPS PTGYIHVGNL RTALMNWAIA RKSGGTFILR LDDTDRERSK QEYSDGIMED 

        70         80         90        100        110        120 
LEWLGLTWDR LERQSDRLDR YAEAADELRR AGRFYECFES PTELDLKRKK LLNMGKPPVY 

       130        140        150        160        170        180 
DRAALKLSDE ERARLRAERG GYWRFLLDQE RIEWTDGILG PISIDAASVS DPVLIRADGQ 

       190        200        210        220        230        240 
VLYTFASSVD DIDMGVTFIV RGGDHVTNTA TQIQIMQALG GTPPSFAHHS LLTGAQGEAL 

       250        260        270        280        290        300 
SKRLGTLSLR DLRARGVEPM ALLSLMARLG SSQPVELFRT HEELLAGFDV STFGAAPTKF 

       310        320        330        340        350        360 
DAEDLFPLTR HYVQGLPFEA VRGRIAALGV PDDLAEPFWR VAKDNIGVLE DLGGWWTLFS 

       370        380        390        400        410        420 
EGAEPQIDPE DEDFIRQAMT LLPPPPYGPE SWAQFTAAVK EATGRKGKGL FMPLRKALTG 

       430        440 
QAHGPDMSEV MPLLQKVRAK G 

« Hide

References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P., Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17029 / ATH 2.4.9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000577 Genomic DNA. Translation: ABN77557.1.
RefSeqYP_001044329.1. NC_009049.1.

3D structure databases

ProteinModelPortalA3PMJ1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349101.Rsph17029_2455.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN77557; ABN77557; Rsph17029_2455.
GeneID4897091.
KEGGrsh:Rsph17029_2455.
PATRIC23172779. VBIRhoSph114483_2681.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252721.
KOK01885.
OMAAGRLYPC.
OrthoDBEOG6DRPF7.
ProtClustDBPRK12558.

Enzyme and pathway databases

BioCycRSPH349101:GHC8-2494-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 nameSYE2_RHOS1
AccessionPrimary (citable) accession number: A3PMJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 3, 2007
Last modified: February 19, 2014
This is version 53 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