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B0S0W2 (SYE_FINM2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:FMG_0414
OrganismFinegoldia magna (strain ATCC 29328) (Peptostreptococcus magnus) [Complete proteome] [HAMAP]
Taxonomic identifier334413 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiales Family XI. Incertae SedisFinegoldia

Protein attributes

Sequence length489 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 – 489489Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_0000367674

Regions

Motif10 – 2011"HIGH" region HAMAP-Rule MF_00022
Motif261 – 2655"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2641ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0S0W2 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 9FA480FE08A462D0

FASTA48956,324
        10         20         30         40         50         60 
MSEVRVRFAP SPTGFLHIGG LRTALYNYLY AKRNNGKFLL RIEDTDRTRY VEGAIENLLE 

        70         80         90        100        110        120 
QLKWAGLDPD EGVVLDDEGN VTEVGECGPY IQSDRVKQGL YQKYIDELIE KGYAYYCFCS 

       130        140        150        160        170        180 
KERLDQVKAQ QKADGLMPKY DGLCRGISIE DAKKRIANGE EYVIRLKLPE NKEITFNDAI 

       190        200        210        220        230        240 
KGKITFNTND MDDQVLIKSD GFPTYHFAVV VDDHLMGITH IVRGDEWISS TAKHVYLYQC 

       250        260        270        280        290        300 
FGWDVPEFVH LPVVLNKSGK KLSKRNDDVA VKDFRKKGYL PEAIDNYLAL VGWSSEDNQE 

       310        320        330        340        350        360 
IMSMEELKHK FDFNRVSKSG GVFDTEKLNW INRHYIKEIE NEKLASMLKP YLVEDGVISE 

       370        380        390        400        410        420 
DYPEYKLIEI ASLFKEELDY MAEITEKVEF LFKDYEMDDD AKEFLNYEKL DELMNALKEE 

       430        440        450        460        470        480 
IESVDEIEKE FASGVMKKVQ KKTGIKGKDL WMTTRAVVTG NVHGPDLDSI MVVLGKQEVL 


DRINKALNR 

« Hide

References

[1]"Complete genome sequence of Finegoldia magna, an anaerobic opportunistic pathogen."
Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K., Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.
DNA Res. 15:39-47(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29328.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008971 Genomic DNA. Translation: BAG07832.1.
RefSeqYP_001691722.1. NC_010376.1.

3D structure databases

ProteinModelPortalB0S0W2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING334413.FMG_0414.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG07832; BAG07832; FMG_0414.
GeneID6019878.
KEGGfma:FMG_0414.
PATRIC21886439. VBIFinMag33027_0619.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMAAFRCFCT.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycFMAG334413:GJ6M-432-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_FINM2
AccessionPrimary (citable) accession number: B0S0W2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 41 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