Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1BDK8 (SYE_CHLPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Cpha266_0427
OrganismChlorobium phaeobacteroides (strain DSM 266) [Complete proteome] [HAMAP]
Taxonomic identifier290317 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupChlorobium

Protein attributes

Sequence length502 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 – 502502Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001887

Regions

Motif12 – 2211"HIGH" region HAMAP-Rule MF_00022
Motif259 – 2635"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2621ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A1BDK8 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: B7D14FC1D8C4D0E0

FASTA50257,876
        10         20         30         40         50         60 
MVAQRYRTRF APSPTGYLHV GGLRTALYNY LFVKKMKGDF VLRIEDTDRS RRVEGAQQNL 

        70         80         90        100        110        120 
LKTLEWAGIV PDESPELGGD FGPYIQSERL EIYKKYCDEL LEGKYAYYCF ATSEELEENR 

       130        140        150        160        170        180 
QLQLKQGLQP KYNRKWLPEE MGGSMPSSEI RKKMEQNAPY VIRMKVPDYV SVWFEDLIRG 

       190        200        210        220        230        240 
PVEFDSSTID DQVLMKSDGF PTYHFASVID DHLMEFTHII RGEEWLPSMP KHLLLYEFFG 

       250        260        270        280        290        300 
WEPPKFAHLP LLLNPDRSKL SKRQGDVAVE DYIRKGYSAE AIVNFVAMLG WNEGEGTEQE 

       310        320        330        340        350        360 
VYSLEQLVER FSLERVGKAG AIFNVDKLNW LEKQYIKSRS ADRIIAVIKP LLMAELEKRP 

       370        380        390        400        410        420 
TAMHESVITS DLYLEQVIEL MRERVGFEHE FVTFSPYFFF DPETYEEEGV RKRWTAETNT 

       430        440        450        460        470        480 
LLREFVTVLA SLDAFTAEAI ETELKAFVAP KGLKAAALIH PLRILCSGVS FGPSLYHMLE 

       490        500 
VLGKDAVIRR ISRGIETVVC LS 

« Hide

References

[1]"Complete sequence of Chlorobium phaeobacteroides DSM 266."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E., Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., Bryant D.A., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 266.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000492 Genomic DNA. Translation: ABL64485.1.
RefSeqYP_910909.1. NC_008639.1.

3D structure databases

ProteinModelPortalA1BDK8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290317.Cpha266_0427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL64485; ABL64485; Cpha266_0427.
GeneID4570981.
KEGGcph:Cpha266_0427.
PATRIC21388587. VBIChlPha122104_0480.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAWLPEEMG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycCPHA290317:GHX4-437-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_CHLPD
AccessionPrimary (citable) accession number: A1BDK8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: May 14, 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