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Q8G4X3 (GLUQ_BIFLO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutamyl-Q tRNA(Asp) synthetase
Short name=Glu-Q-RSs
EC=6.1.1.-
Gene names
Name:gluQ
Ordered Locus Names:BL1251
OrganismBifidobacterium longum (strain NCC 2705)
Taxonomic identifier206672 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the tRNA-independent activation of glutamate in presence of ATP and the subsequent transfer of glutamate onto a tRNA(Asp). Glutamate is transferred on the 2-amino-5-(4,5-dihydroxy-2-cyclopenten-1-yl) moiety of the queuosine in the wobble position of the QUC anticodon By similarity. HAMAP MF_01428

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_01428

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. GluQ subfamily.

Ontologies

Keywords
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

aminoacyl-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 379379Glutamyl-Q tRNA(Asp) synthetase HAMAP MF_01428
PRO_0000208287

Regions

Region14 – 185Glutamate binding By similarity
Motif17 – 2711"HIGH" region HAMAP MF_01428
Motif300 – 3045"KMSKS" region HAMAP MF_01428

Sites

Metal binding1061Zinc By similarity
Metal binding1081Zinc By similarity
Metal binding1281Zinc By similarity
Metal binding1321Zinc By similarity
Binding site501Glutamate By similarity
Binding site2291Glutamate By similarity
Binding site2471Glutamate By similarity
Binding site3031ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8G4X3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: DEAC7D620B757C8B

FASTA37942,168
        10         20         30         40         50         60 
MVLNFIRGGP VTGRFAPTPS GRMHIGNVYA MLGAWLSARS RGDRMLMRIE DVDKPRVVAG 

        70         80         90        100        110        120 
ADQLMMDDLH WLGLDWDGEP MFQSQRTERY EYALECLRSQ GVLYPCFCSR ADIRAASAPN 

       130        140        150        160        170        180 
EGDGFMVYPG TCRRLLHDHP DEVRARLVRG DQHSIRIAMP ESAAGEKQRT VPDDSAALSG 

       190        200        210        220        230        240 
AVPPEQQGDA GIVDGVACFN DRVYSPQHYD LAREVGDSVI RRADGLFGYQ LVVVVDDLDM 

       250        260        270        280        290        300 
GVDDIVRGRD LLRSTALQMW IRQCLLAGGF EPECGNTEKP LAEHPEYAHL PLIDNAAGRR 

       310        320        330        340        350        360 
LAKRERSLDM GALRARNVTP EQIIGYCAWL LRLQPTPIPC KPADLLADFS WEPLRANHLD 

       370 
RALKPDDPTT PQWLAEALG

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References

[1]"The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract."
Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.
Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCC 2705.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014295 Genomic DNA. Translation: AAN25052.1.
RefSeqNP_696416.1. NC_004307.2.

3D structure databases

ProteinModelPortalQ8G4X3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1022750.
GenomeReviewsGene locus BL1251 in contig AE014295_GR.
KEGGblo:BL1251.
NMPDRfig|206672.1.peg.1183.
PATRIC21120200. VBIBifLon107831_1536.

Phylogenomic databases

HOGENOMHBG628189.
OMADAPSSYH.
PhylomeDBQ8G4X3.
ProtClustDBPRK05710.

Enzyme and pathway databases

BioCycBLON206672:BL1251-MONOMER.

Family and domain databases

HAMAPMF_01428. Glu_Q_tRNA_synth. Divergent sequence.
[Tree]
InterProIPR000924. Glu/Gln-tRNA-synth_Ib.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 2 hits.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLUQ_BIFLO
AccessionPrimary (citable) accession number: Q8G4X3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 61 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

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