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A8MLB5 (SYE_ALKOO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:Clos_0467
OrganismAlkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]
Taxonomic identifier350688 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length495 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 – 495495Glutamate--tRNA ligase HAMAP-Rule MF_00022
PRO_1000057190

Regions

Motif9 – 1911"HIGH" region HAMAP-Rule MF_00022
Motif257 – 2615"KMSKS" region HAMAP-Rule MF_00022

Sites

Binding site2601ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
A8MLB5 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 6C94413C6AC28043

FASTA49556,679
        10         20         30         40         50         60 
MSVRVRFAPS PTGFVHIGSL RTALYNYLFA KKSNGKYILR VEDTDQSRYV EGAIEGMLRS 

        70         80         90        100        110        120 
MAWAGVHHDE GVVFTGETLG QKGDFGPYIQ SERLEIYKKY MDILLEKGHA YYCFCSKERL 

       130        140        150        160        170        180 
DEVREKQKVE GLNAGYDGHC RNLSKEEIEE KLNAGQPYVI RLRLPENKDI QFHDIVRGDV 

       190        200        210        220        230        240 
VMNTADLDDQ VLMKSDGFPT YHFAVVVDDH LMEITHVIRG EEWLPSTPKH VYLYEAFGWE 

       250        260        270        280        290        300 
APQYVHLPNI LNADRKKLSK RQGDVAVEDF LKKGYLPEGL VNYIALVGWS PEDNNEIFSM 

       310        320        330        340        350        360 
EELEANFSLE RVSKSGGVFD VHKLNWVNGH YIRESSVERI TDLAIPHLIE AGYITESDAQ 

       370        380        390        400        410        420 
ERYEWLKDLV SVLQDRISYV AEIKEKAGIF FNAEIELKDE ESKELIQVEH LPQLLDVLKA 

       430        440        450        460        470        480 
KVEAAEVIDE EFGKSVFKEI QKETGIKGPN LFKPIRVVLT GEVHGPDLPL VMKVLGSKNI 

       490 
LDRIEYVYDL IQSMK 

« Hide

References

[1]"Complete genome of Alkaliphilus oremlandii OhILAs."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OhILAs.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000853 Genomic DNA. Translation: ABW18029.1.
RefSeqYP_001512025.1. NC_009922.1.

3D structure databases

ProteinModelPortalA8MLB5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING350688.Clos_0467.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW18029; ABW18029; Clos_0467.
GeneID5677003.
KEGGaoe:Clos_0467.
PATRIC20866035. VBIAlkOre124042_0486.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHOG000252720.
KOK09698.
OMALMLFGRD.
OrthoDBEOG6DRPF7.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycAORE350688:GHBG-485-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.
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.
ProtoNetSearch...

Entry information

Entry nameSYE_ALKOO
AccessionPrimary (citable) accession number: A8MLB5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 4, 2007
Last modified: February 19, 2014
This is version 44 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