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Q8DJI4 (MURE_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 80. 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:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

EC=6.3.2.13
Alternative name(s):
Meso-A2pm-adding enzyme
Meso-diaminopimelate-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase
Gene names
Name:murE
Ordered Locus Names:tlr1239
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan By similarity. HAMAP-Rule MF_00208

Catalytic activity

ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-heptanedioate. HAMAP-Rule MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP-Rule MF_00208

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00208.

Post-translational modification

Carbamoylation is probably crucial for Mg2+ binding and, consequently, for the gamma-phosphate positioning of ATP By similarity. HAMAP-Rule MF_00208

Sequence similarities

Belongs to the MurCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101959

Regions

Nucleotide binding113 – 1197ATP Potential
Region155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region409 – 4124Meso-diaminopimelate binding By similarity
Motif409 – 4124Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site321UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3851Meso-diaminopimelate By similarity
Binding site4601Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4641Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2221N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DJI4 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2F21F05584ECF07B

FASTA49753,933
        10         20         30         40         50         60 
MNLRELLTAA AITPGFEHPA LNQEVKSLRM NSWECEPGSL FIGMPGTRVE GGNFWPSALA 

        70         80         90        100        110        120 
AGAIAAVVSP QAKPREGEAC VIVVPDIERA CGRLAAAFYN YPSQHLSLLG VTGTNGKTTT 

       130        140        150        160        170        180 
THLVEHLLNR VGYPTALLGT LYSRWPGHCE VASHTTPFAV TLQEQLAAAV DAGCRFGVME 

       190        200        210        220        230        240 
VSSHALAQDR VWGCQFEVAA FTNLTQDHLD YHRDLEDYFA AKAKLFTADY LKGRAILNGD 

       250        260        270        280        290        300 
DPFGQRLAQQ LPRDRYWTYG LSKDADFRAE NLNYRSNGVT GAVHTPLGSG TLDSPLVGQF 

       310        320        330        340        350        360 
NVANVLAAIA MGAAVGLPLE AMLNALRDFP GVPGRMEQVR LDPEQDITVV VDYAHTPDSL 

       370        380        390        400        410        420 
ENLLRAARPF IPGKLICVFG CGGDRDRSKR PQMGAIAARL ADQVVVTSDN PRTENPQRIL 

       430        440        450        460        470        480 
DDILAGIPPE TAMIVEGDRR QAILQAILTA APGDGVIIAG KGHEDYQILG TEKVHFDDRE 

       490 
EARNALKERL KQPLQRG 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08791.1.
RefSeqNP_682029.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DJI4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tlr1239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08791; BAC08791; BAC08791.
GeneID1011779.
KEGGtel:tlr1239.
PATRIC23927810. VBITheElo119873_1303.

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAVDYAHTG.
OrthoDBEOG6PKFCR.
ProtClustDBPRK00139.

Enzyme and pathway databases

UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.40.1390.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR018109. Folylpolyglutamate_synth_CS.
IPR004101. Mur_ligase_C.
IPR013221. Mur_ligase_cen.
IPR000713. Mur_ligase_N.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
SUPFAMSSF53244. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
SSF63418. SSF63418. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_THEEB
AccessionPrimary (citable) accession number: Q8DJI4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 80 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

PATHWAY comments

Index of metabolic and biosynthesis pathways