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Reviewed, UniProtKB/Swiss-Prot A4XHE0 (SYE1_CALS8)

Last modified February 9, 2010. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA synthetase 1
    EC=6.1.1.17
Alternative name(s):
    Glutamate--tRNA ligase 1
      Short name=GluRS 1
Gene names
Name: gltX1
Ordered Locus Names: Csac_0706
OrganismCaldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903) [Complete proteome] [HAMAP]
Taxonomic identifier351627 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length485 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 MF_00022

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022

Subunit structure

Monomer By similarity. HAMAP MF_00022

Subcellular location

Cytoplasm By similarity HAMAP 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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Glutamyl-tRNA synthetase 1 HAMAP MF_00022
PRO_0000367631

Regions

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

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A4XHE0-1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: 6EA895CBB689A4CE

FASTA48556,746
        10         20         30         40         50         60 
MEVRTRFAPS PTGHLHIGGA RTALFNYLFA KRYGGKFILR IEDTDLERSS IESEKVIIES 

        70         80         90        100        110        120 
LRWLGIEWDE GVEVGGPYGP YRSTERVDIY KKYVDVLFEK GYAYYCYCTE EELEAQRQEL 

       130        140        150        160        170        180 
LSKGQMPRYL GKCRNLTEDQ KRRFEQEGRK PTVRFKVPEG VKIVVHDLVR GDVEFLSDDI 

       190        200        210        220        230        240 
GDFVIVKSDG IPTYNFAVVI DDHLMKISHV IRGEEHLSNT PRQILIYNAL GFELPQFAHV 

       250        260        270        280        290        300 
SLILGKDRTK MSKRHGSTWV EQYRDQGYLK EGLINFLALL GWSPPEDREI FDMEYLIENF 

       310        320        330        340        350        360 
SLERVSKNPA IFDIDKLNYI NSQHIKLKSL DELTQMCIPY FVEAGYIKED EAKSKFEWLK 

       370        380        390        400        410        420 
KIVKSVYEGL DYLSQIKDRV DIFFNNEVKI EEDEAKEVLK WDHVKDLINV FENKIRQMNE 

       430        440        450        460        470        480 
LTPEAIKLLF KEIQKETGYK GKNLFMPIRV ALTGKTHGPE LVEIIEIVGK ENILKRLEFF 


KTWYN 

« Hide

References

[1]"Genome sequence of the thermophilic hydrogen-producing bacterium Caldicellulosiruptor saccharolyticus DSM 8903."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000679 Genomic DNA. Translation: ABP66325.1.
RefSeqYP_001179516.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4XHE0.

Genome annotation databases

GeneID5087365.
GenomeReviewsGene locus Csac_0706 in contig CP000679_GR.
KEGGcsc:Csac_0706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMAYRCFTSE.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020752. aa-tRNA-synth_I_codon-bd_sub1.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ic_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ic.
IPR020061. Glu/Gln-tRNA-synth_Ic_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ic_cat-dom.
IPR020060. Glu/Gln-tRNA-synth_Ic_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:1.10.8.70. aa-tRNA-synth_I_codon-bd_sub1. 1 hit.
G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
TIGRFAMsTIGR00464. gltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE1_CALS8
AccessionPrimary (citable) accession number: A4XHE0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 29, 2007
Last modified: February 9, 2010
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents