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Q1Q845 (SYE_PSYCK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Pcryo_2381
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length509 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 – 509509Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000001943

Regions

Motif20 – 3011"HIGH" region HAMAP-Rule MF_00022
Motif261 – 2655"KMSKS" region HAMAP-Rule MF_00022

Sites

Metal binding1171Zinc By similarity
Metal binding1191Zinc By similarity
Metal binding1441Zinc By similarity
Metal binding1461Zinc By similarity
Binding site2641ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1Q845 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: C5D4C77FD311B544

FASTA50957,493
        10         20         30         40         50         60 
MMQPSTSTNS IRPVRTRIAP SPTGFPHVGT AYIALFNLAF AKAHGGEFIL RIEDTDQTRS 

        70         80         90        100        110        120 
TEQSEKMILD ALRWVGLDWA EGPDIGGPHA PYRQSERSDI YKKHAEQLIE NDHAFRCFCS 

       130        140        150        160        170        180 
SEELDAMRAE QMANGETPRY DGRCAHLAAE KTEQLVAEGK PHVIRMRVPT EGVCQVQDML 

       190        200        210        220        230        240 
RGTVEIPWTQ VDMQVLLKTD GMPTYHLANV VDDHLMDISH VMRGEEWLNS APKHQLLYEY 

       250        260        270        280        290        300 
FGWEMPVLCH MPLLRNPDKS KLSKRKNPTS ITYYRDAGVL PEALLNYLGR MGYSMPDEAE 

       310        320        330        340        350        360 
QFTLEEMIAS FDIQRVSLGG PIFDIEKLNW LNSEWLRALT PEELKNKILE WASNSDKLTA 

       370        380        390        400        410        420 
IAAAIQPRIE LLSDAVNWSG FYFQNLPDIN AESFTHKSLT PEQIMDMLQL SLWQLEVLPT 

       430        440        450        460        470        480 
WSEENIYATL KGLAAHLDIK MRDFMAPFFI AIAGSTSSTP VMNSMAIIGA DMTLTRLRHA 

       490        500 
VDVLGGLGKK KLKKLEKQAA ELPDFLAAE 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000323 Genomic DNA. Translation: ABE76158.1.
RefSeqYP_581642.1. NC_007969.1.

3D structure databases

ProteinModelPortalQ1Q845.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335284.Pcryo_2381.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE76158; ABE76158; Pcryo_2381.
GeneID4034355.
KEGGpcr:Pcryo_2381.
PATRIC23064415. VBIPsyCry128170_2514.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK01885.
OMAVTGQTHG.
OrthoDBEOG6DRPF7.

Enzyme and pathway databases

BioCycPCRY335284:GHE9-2431-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_PSYCK
AccessionPrimary (citable) accession number: Q1Q845
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: May 14, 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