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B0JY53 (SYE_MICAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:MAE_52690
OrganismMicrocystis aeruginosa (strain NIES-843) [Complete proteome] [HAMAP]
Taxonomic identifier449447 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesMicrocystis

Protein attributes

Sequence length480 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_B

Catalytic activity

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B

Subunit structure

Monomer By similarity. HAMAP MF_00022_B

Subcellular location

Cytoplasm By similarity HAMAP MF_00022_B.

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 480480Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_1000074325

Regions

Motif9 – 1911"HIGH" region HAMAP MF_00022_B
Motif250 – 2545"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2531ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B0JY53 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 0A7A5D456C43761D

FASTA48054,663
        10         20         30         40         50         60 
MTVRVRIAPS PTGNLHIGTA RTAVFNWLFA RHHRGKFILR VEDTDLERSR PEYTENIQAG 

        70         80         90        100        110        120 
LQWLGLNWDE GPFFQTQRLN YYRQAIQTLL DRGLAYRCYC TPEELEKMRE EQKARNLAPR 

       130        140        150        160        170        180 
YDNRHRYLTP EQQAQFEQAG RKAVIRFIID DDQEIIWQDL IREKVIWKGS DLGGDMVIAR 

       190        200        210        220        230        240 
TSENGEENFG QPLYNLAVVV DDIDMEITHV IRGEDHIANT AKQILLYEAL GAKVPEFAHS 

       250        260        270        280        290        300 
PLILNQEGRK LSKRDGVTSI DDFRKLGFLP QALVNYMTLL GWTPPDSTEE IFTLEAAAEV 

       310        320        330        340        350        360 
FSLERVNKAG AKFDWTKLDW INSQYLHRLT GEELVPLLLP YWQEAGYNFA AETDRAWLIG 

       370        380        390        400        410        420 
LATLIGPSLT RLSDAVAESR LLLTPLANYN QEALSQLQLE GVKDIIKDIL AAITPDLTGE 

       430        440        450        460        470        480 
VAKGIVETTT KAHRVKKGLV MKSLRAALMG ELHGPDLMQS WLLLNQKGWD ISRLQQAVNS 

« Hide

References

[1]"Complete genomic structure of the bloom-forming toxic cyanobacterium Microcystis aeruginosa NIES-843."
Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M., Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A., Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M. expand/collapse author list , Nakazaki N., Nakayama S., Yamada M., Tabata S., Watanabe M.M.
DNA Res. 14:247-256(2007) [PubMed: 18192279] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NIES-843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009552 Genomic DNA. Translation: BAG05091.1.
RefSeqYP_001660283.1. NC_010296.1.

3D structure databases

ProteinModelPortalB0JY53.
SMRB0JY53. Positions 2-478.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0JY53.

Proteomic databases

PRIDEB0JY53.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5866106.
GenomeReviewsGene locus MAE_52690 in contig AP009552_GR.
KEGGmar:MAE_52690.
PATRIC22634997. VBIMicAer59304_4802.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628189.
OMAIEWFNLD.
PhylomeDBB0JY53.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycMAER449447:MAE_52690-MONOMER.

Family and domain databases

HAMAPMF_00022_B. Glu_tRNA_synth_B.
[Tree]
InterProIPR008925. aa-tRNA-synth_I_codon-bd.
IPR020751. aa-tRNA-synth_I_codon-bd_sub2.
IPR001412. aa-tRNA-synth_I_CS.
IPR004527. Glu-tRNA-synth_Ib_bac/mito.
IPR000924. Glu/Gln-tRNA-synth_Ib.
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]
Gene3DG3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KOK01885.
PANTHERPTHR10119. Glu_tRNA-synt_1c. 1 hit.
PTHR10119:SF1. PTHR10119:SF1. 1 hit.
PfamPF00749. tRNA-synt_1c. 1 hit.
[Graphical view]
PRINTSPR00987. TRNASYNTHGLU.
SUPFAMSSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMsTIGR00464. GltX_bact. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYE_MICAN
AccessionPrimary (citable) accession number: B0JY53
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 18, 2008
Last modified: January 25, 2012
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families