Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4FQ04 (SYE_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Psyc_2057
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [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_0000237392

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
Q4FQ04 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: 7130F212DDE88F23

FASTA50957,379
        10         20         30         40         50         60 
MMQPSTSTNS NRPVRTRIAP SPTGFPHVGT AYIALFNLAF AKAHGGEFIL RIEDTDQTRS 

        70         80         90        100        110        120 
TEQSEKMILD ALRWVGLDWS EGPDVGGPHA PYRQSERSAI YKKHAEQLID SDHAFRCFCT 

       130        140        150        160        170        180 
SEELDTMRAE QMANGETPRY DGRCAHLATE KTEQLVKEGK PNVIRMRVPT EGVCQVQDML 

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

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

       310        320        330        340        350        360 
KFTLDEMIAS LDIQRVSLGG PIFDIEKLNW LNAEWLRALT PEELKNKILD WASNSDKLTA 

       370        380        390        400        410        420 
IAAAIQPRIE LLSDAVNWSG FYFQNLPDIN AESFTHKSLT AEQIIEMLQL ALWQLETLPT 

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

       490        500 
VDVLGGLGKK KLKKLEKQAA ELPDFLAAE 

« Hide

References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ19904.1.
RefSeqYP_265338.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FQ04.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_2057.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ19904; AAZ19904; Psyc_2057.
GeneID3516032.
KEGGpar:Psyc_2057.
PATRIC23059053. VBIPsyArc98534_2425.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPARC259536:GI3A-2108-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_PSYA2
AccessionPrimary (citable) accession number: Q4FQ04
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: August 30, 2005
Last modified: February 19, 2014
This is version 60 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