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Q11PQ4 (SYE_CYTH3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:CHU_3373
OrganismCytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469) [Complete proteome] [HAMAP]
Taxonomic identifier269798 [NCBI]
Taxonomic lineageBacteriaBacteroidetesCytophagiaCytophagalesCytophagaceaeCytophaga

Protein attributes

Sequence length517 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 – 517517Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000330966

Regions

Motif14 – 2411"HIGH" region HAMAP-Rule MF_00022
Motif266 – 2705"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2691ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11PQ4 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: DC98D665678A2C4D

FASTA51758,622
        10         20         30         40         50         60 
MSDTNKQVRV RFAPSPTGPL HIGGVRTALY NYLFARKMGG KMLLRIEDTD QNRFVPGAEA 

        70         80         90        100        110        120 
YIQEALAWVG IVIDEGAGVG GPHAPYKQSE RKPMYREYAE KLIAEGNAYY AFDTSEELEA 

       130        140        150        160        170        180 
MKERLKAAKV ASPSYNMVTR MQMNNSLTLP EDEVKRRLDA GDEYVIRLKV PRKEEIRLND 

       190        200        210        220        230        240 
MIRGWVVVHS STIDDKVLLK SDGMPTYHLA NIVDDHLMEI THVIRGEEWL PSAPLHVLLY 

       250        260        270        280        290        300 
RFLGWEDTMP QFAHLPLLLK PDGNGKLSKR DADAGGFPIF PLDWKDPASG DTWIGFKQQG 

       310        320        330        340        350        360 
YLQEATTNFL AFLGWNPGTQ QELFTMDELI EAFTVERIGK SGTKFDINKA KWYNQQYMRQ 

       370        380        390        400        410        420 
LPDETLTRLL KEEADKHQAK YDAAKLPLIA QMLKERLTFA KDYWIEGQFF FEAPETFDEK 

       430        440        450        460        470        480 
VASTKWNAEA VTVISAYKEA LAAYTGEFNA ENVKHVLHEV LEKADVKIGK IMQALRLALT 

       490        500        510 
GAGAGPDLMQ FIEIVGKEEA IKRMQFALIT LSEKVNS 

« Hide

References

[1]"Genome sequence of the cellulolytic gliding bacterium Cytophaga hutchinsonii."
Xie G., Bruce D.C., Challacombe J.F., Chertkov O., Detter J.C., Gilna P., Han C.S., Lucas S., Misra M., Myers G.L., Richardson P., Tapia R., Thayer N., Thompson L.S., Brettin T.S., Henrissat B., Wilson D.B., McBride M.J.
Appl. Environ. Microbiol. 73:3536-3546(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33406 / NCIMB 9469.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000383 Genomic DNA. Translation: ABG60609.1.
RefSeqYP_679952.1. NC_008255.1.

3D structure databases

ProteinModelPortalQ11PQ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269798.CHU_3373.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG60609; ABG60609; CHU_3373.
GeneID4187162.
KEGGchu:CHU_3373.
PATRIC21597625. VBICytHut34013_3357.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCHUT269798:GJ83-3369-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_CYTH3
AccessionPrimary (citable) accession number: Q11PQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: August 22, 2006
Last modified: February 19, 2014
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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries