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B1WYU1 (SYE_CYAA5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. 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:cce_1758
OrganismCyanothece sp. (strain ATCC 51142) [Complete proteome] [HAMAP]
Taxonomic identifier43989 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length484 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

Cofactor

Binds 1 zinc ion per subunit By similarity. 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
Metal-binding
Nucleotide-binding
Zinc
   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

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000090069

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif250 – 2545"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B1WYU1 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 119C779725BFFF5B

FASTA48455,281
        10         20         30         40         50         60 
MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA HHHQGQFILR VEDTDRERSR AEYTENIKSG 

        70         80         90        100        110        120 
LAWLGLTWDE GPFFQTQRLD LYRQGIQTLL DKGFAYRCYC TPEELEQMRE AQKAQNQAPR 

       130        140        150        160        170        180 
YDNRHRHLTE EQRQGLEAQG RKPVIRFIID DDREIVWHDL IRGKMTWKGS DLGGDMVIAR 

       190        200        210        220        230        240 
IADNPDQPFG QPLYNLAVVV DDMDMKITHV IRGEDHIANT AKQILLYEAL GATVPEFAHT 

       250        260        270        280        290        300 
PLILNQEGRK LSKRDGVTSI DDFRKMGFLP QALANYMTLL GWTPPDSTQE IFTLTEAAQQ 

       310        320        330        340        350        360 
FSLERVNKAG AKFDWDKLDW INSQYVHKMS GEELVDLLVP YWQEAGYPIN IDSDRPWLEK 

       370        380        390        400        410        420 
MATLIGPSLT RLSDAAKESV LLFGGRVDYS EEAIAQMKQD GVKDVLQAVV EKIQESSQLT 

       430        440        450        460        470        480 
EDEAKDTIKQ VTKTFKVKKG LVMRSLRAGL MGELHGPDLI QSWLLLHEKG WDKTRLTHGL 


SLVE 

« Hide

References

[1]"The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium important in the marine nitrogen cycle."
Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.
Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51142.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000806 Genomic DNA. Translation: ACB51108.1.
RefSeqYP_001803174.1. NC_010546.1.

3D structure databases

ProteinModelPortalB1WYU1.
SMRB1WYU1. Positions 2-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING43989.cce_1758.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB51108; ACB51108; cce_1758.
GeneID6168807.
KEGGcyt:cce_1758.
PATRIC21541973. VBICyaSp130209_1816.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycCSP43989:GKC8-1786-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_CYAA5
AccessionPrimary (citable) accession number: B1WYU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
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

SIMILARITY comments

Index of protein domains and families

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries