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Q3B256 (SYE_PELLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:Plut_1721
OrganismPelodictyon luteolum (strain DSM 273) (Chlorobium luteolum (strain DSM 273)) [Complete proteome] [HAMAP]
Taxonomic identifier319225 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length504 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 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 – 504504Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000237384

Regions

Motif14 – 2411"HIGH" region HAMAP MF_00022_B
Motif261 – 2655"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2641ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3B256 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: CD840631064CD11B

FASTA50457,956
        10         20         30         40         50         60 
MHMVGKRVRT RFAPSPTGYL HVGGLRTALY NYLFAKKMNG DFIIRIEDTD QSRKVEGAQQ 

        70         80         90        100        110        120 
NLIKTLEWAG LVPDESPVHG GNFGPYLQSE RLELYAGYCR QLLEDGTAYY CFATSEELEE 

       130        140        150        160        170        180 
NRQLQMKQGL QPKYNRKWLP EDMGGSMPRS ESEKMLASGA PYVIRMKVPD YVSVWFEDII 

       190        200        210        220        230        240 
RGPIEFDSAT IDDQVLMKSD GFPTYHFASV IDDHLMEFTH IIRGEEWLPS MPKHLLLYEF 

       250        260        270        280        290        300 
FGWEPPKYAH LPLLLNPDRS KLSKRQGDVA VEDYIQKGYS QEAIINFIAL LGWNEGEGCE 

       310        320        330        340        350        360 
QEVYSMEQLI DRFSLERVGK AGSIFTIDKL NWLEKQYIKN RPAEKIIETI RPLLQEELSS 

       370        380        390        400        410        420 
KETMLDREVI TGDDYLRQVI ELMRERVGFE HEFVTFSSYF FFEPETWEEE AVKKRWTSDT 

       430        440        450        460        470        480 
PALLSEFLPT LEGLPEFTSD AIEAALKAFV EPKGLKAAVL IHPLRILASG VSFGPSLYHM 

       490        500 
LEVLGREAVL RRIRKGMECI TVPA 

« Hide

References

[1]"Complete sequence of Pelodictyon luteolum DSM 273."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 273.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000096 Genomic DNA. Translation: ABB24575.1.
RefSeqYP_375618.1. NC_007512.1.

3D structure databases

ProteinModelPortalQ3B256.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3B256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3745189.
GenomeReviewsGene locus Plut_1721 in contig CP000096_GR.
KEGGplt:Plut_1721.
NMPDRfig|319225.3.peg.1725.
PATRIC21381096. VBIChlLut1287_1805.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAMAHIPLI.
PhylomeDBQ3B256.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycPLUT319225:PLUT_1721-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 nameSYE_PELLD
AccessionPrimary (citable) accession number: Q3B256
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 22, 2005
Last modified: January 25, 2012
This is version 44 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