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Q5N1B8 (SYE_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:syc1712_c
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length481 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 – 481481Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000119676

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif248 – 2525"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding981Zinc By similarity
Metal binding1001Zinc By similarity
Metal binding1251Zinc By similarity
Metal binding1271Zinc By similarity
Binding site2511ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5N1B8 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 82AC99209A06D033

FASTA48153,200
        10         20         30         40         50         60 
MSVRVRIAPS PTGNLHIGTA RTAVFNWLFA RRHQGQFILR IEDTDLERSR SEYTDNILTG 

        70         80         90        100        110        120 
LQWLGLNWDE GPFYQTQRLD LYKAAVQQLL DSGKAYRCYC TEAELEALRE SQRARNEAPR 

       130        140        150        160        170        180 
YDNRHRDLTP EQEAAFQAEG REAVIRFRID DDREIAWTDL VRDRVVWKGS DLGGDMVIAR 

       190        200        210        220        230        240 
RSPAGTIGQP LYNLAVVVDD IDMTISHVIR GEDHIANTAK QILLYEALGA AVPEFAHTPL 

       250        260        270        280        290        300 
ILNKEGRKLS KRDGVTSISD FQNLGYLPEA IANYMTLLGW SPVEGMDERF SLAEAATVFD 

       310        320        330        340        350        360 
FDRVNKAGAK FDWDKLNWLN SQVIKEKSAS ELVALLQPFW SKAGVDTAAY PAAWLEELAT 

       370        380        390        400        410        420 
LLGPSLVTLT DIVGQSQLFF SQGIELQEDA IAQLGQAGSK AVLQQILEAL PSEALTLEVA 

       430        440        450        460        470        480 
KGLIDQAVKA AGVKKGIGMR SLRAALMGSM QGPDLLTSWV LLHQAGQAQP RLQAAIAAAQ 


G 

« Hide

References

[1]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008231 Genomic DNA. Translation: BAD79902.1.
RefSeqYP_172422.1. NC_006576.1.

3D structure databases

ProteinModelPortalQ5N1B8.
SMRQ5N1B8. Positions 2-480.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269084.syc1712_c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD79902; BAD79902; syc1712_c.
GeneID3198551.
KEGGsyc:syc1712_c.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252722.
KOK01885.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSELO269084:GCDQ-1758-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_SYNP6
AccessionPrimary (citable) accession number: Q5N1B8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: February 1, 2005
Last modified: February 19, 2014
This is version 63 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