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Q8A455 (SYE_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 64. 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:BT_2748
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

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
Reference 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_0000119509

Regions

Motif12 – 2211"HIGH" region HAMAP MF_00022_B
Motif260 – 2645"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2631ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A455 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B81EB682A53E8157

FASTA50457,734
        10         20         30         40         50         60 
MAERKVRVRF APSPTGALHI GGVRTALYNY LFARQHGGDL IFRIEDTDSN RFVPGAEEYI 

        70         80         90        100        110        120 
LESFKWLGIH FDEGVSFGGE HGPYRQSERR EIYKKYVQIL LDNDKAYIAF DTPEELDAKR 

       130        140        150        160        170        180 
AEIANFQYDA STRGMMRNSL TMSKEEVDAL IAEGKQYVVR FKIEPNEDVH VNDLIRGEVV 

       190        200        210        220        230        240 
INSSILDDKV LYKSADELPT YHLANIVDDH LMEVSHVIRG EEWLPSAPLH VLLYRAFGWE 

       250        260        270        280        290        300 
DTMPEFAHLP LLLKPEGNGK LSKRDGDRLG FPVFPLEWRP ESGEVSSGYR ESGYLPEAVI 

       310        320        330        340        350        360 
NFLALLGWNP GNDQEVMSMD EMIKLFDIHR CSKSGAKFDY KKGIWFNHQY IQLKPNEEIA 

       370        380        390        400        410        420 
ELFLPVLKEH GVEAPFEKVV TVVGMMKDRV SFIKELWDVC SFFFVAPAEY DEKTVKKRWK 

       430        440        450        460        470        480 
EDSAKCMTEL AEVIAGIEDF SIEGQEKVVM DWIAEKGYHT GNIMNAFRLT LVGEGKGPHM 

       490        500 
FDISWVLGKE ETLARMKRAV EVLK 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO77854.1.
RefSeqNP_811660.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A455.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1072222.
GenomeReviewsGene locus BT_2748 in contig AE015928_GR.
KEGGbth:BT_2748.
NMPDRfig|226186.1.peg.2747.
PATRIC21060455. VBIBacThe70966_2795.

Phylogenomic databases

HOGENOMHBG628189.
OMAIEWFNLD.
PhylomeDBQ8A455.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycBTHE226186:BT_2748-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_BACTN
AccessionPrimary (citable) accession number: Q8A455
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 64 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