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Q7U581 (SYE_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 53. 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:SYNW1826
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechococcus

Protein attributes

Sequence length477 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 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 – 477477Glutamate--tRNA ligase HAMAP MF_00022_B
PRO_0000119678

Regions

Motif8 – 1811"HIGH" region HAMAP MF_00022_B
Motif247 – 2515"KMSKS" region HAMAP MF_00022_B

Sites

Binding site2501ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7U581 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 152F9000D56D5E29

FASTA47753,329
        10         20         30         40         50         60 
MVRVRLAPSP TGTLHIGTAR TAVFNWLYAR RQQGSFLLRI EDTDKERSKP EYTQNILEGL 

        70         80         90        100        110        120 
RWLGIDWDEE PLIQSEQVQQ HRAAIETLLQ KGLAYRCYAN EAELDAMREA QKASNQAPRY 

       130        140        150        160        170        180 
DNRHRNLTPE QEAAFQSEGR EAVIRFRIDD NAEIRWNDMV RGAMSWRGAD LGGDMVVARR 

       190        200        210        220        230        240 
APADQIGDPL YNLVVVVDDA AMAISHVIRG EDHIANTAKQ LLLYEALDLP APTFAHAPLI 

       250        260        270        280        290        300 
LNAEGRKLSK RDGVTSINDF RTMGYTAEAI ANYMTLLGWS VPEGMEERFT LPEAAAVFSF 

       310        320        330        340        350        360 
DRVNKAGARF DWDKLNWLNG QVLHALPAQQ LLDDLRPLWA EQGWTLPDDS SWGLELCELL 

       370        380        390        400        410        420 
GPSLTLLKEG VEQATPFFKC PDLEDDGVRQ LEADGARTAV AQLLQILEAE PWDGKDTDRA 

       430        440        450        460        470 
KQLLADAAKG AGVKKGVVMK SLRAALLGRL QGPDLITTWC LLARIGEDLP RLQRCLA 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed: 12917641] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569694 Genomic DNA. Translation: CAE08341.1.
RefSeqNP_897917.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U581.
SMRQ7U581. Positions 2-476.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7U581.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1731239.
GenomeReviewsGene locus SYNW1826 in contig BX548020_GR.
KEGGsyw:SYNW1826.
PATRIC23835335. VBISynSp27240_1960.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0008.
HOGENOMHBG628189.
OMADKETAND.
PhylomeDBQ7U581.
ProtClustDBPRK01406.

Enzyme and pathway databases

BioCycSSP84588:SYNW1826OR0662-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_SYNPX
AccessionPrimary (citable) accession number: Q7U581
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 53 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