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Reviewed, UniProtKB/Swiss-Prot Q8Y5L9 (MURE_LISMO)

Last modified February 9, 2010. Version 54. 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:
    UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase
    EC=6.3.2.13
Alternative name(s):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase
Gene names
Name: murE
Ordered Locus Names: lmo2038
OrganismListeria monocytogenes [Complete proteome] [HAMAP]
Taxonomic identifier1639 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesListeriaceaeListeria

Protein attributes

Sequence length491 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 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 MF_00208

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00208

Subcellular location

Cytoplasm By similarity HAMAP MF_00208.

Post-translational modification

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

Sequence similarities

Belongs to the murCDEF family. MurE subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101911

Regions

Nucleotide binding108 – 1147ATP Potential
Region150 – 1512UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region407 – 4104Meso-diaminopimelate binding By similarity
Motif407 – 4104Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1491UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1771UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1831UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3831Meso-diaminopimelate By similarity
Binding site4581Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4621Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8Y5L9-1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 9B80F0F669CFEB95

FASTA49153,747
        10         20         30         40         50         60 
MKLNELMQAI PVFTGEVSET IEISHIAQDS RKVKPGTLFI CIDGEVVDGH KFASRAVELG 

        70         80         90        100        110        120 
AVAIIAEKQV DVSIPVIYVR DSKRAMAMLA DYFYGSPTQA LKLVGITGTN GKTTVSHLVE 

       130        140        150        160        170        180 
QIVRENGEQT GLIGTMYRKI GDQILETKNT TPDSLTLQET FRDMLLSGVS TAVMEVSSHA 

       190        200        210        220        230        240 
LVQGRVYGSD YDVAVFMNLS QDHLDYHHTM EEYANAKSLL FAQLGNSYHT SNPKIAVLNA 

       250        260        270        280        290        300 
DDAESVRMQK ATAAHIITFG IKQEADFQAS NIKITSHGST FDLGTPVGNF TLKIKMIGNF 

       310        320        330        340        350        360 
SVYNVLAAIA TSFALHIPME KAIKTVESIP GVKGRFELVH AGQEFPVIVD YAHTPDGLLN 

       370        380        390        400        410        420 
VLETIDEFAE KRVFVVVGCG GDRDKGKRPQ MAKIAVDYAT NPIFTSDNPR SENPRAIIED 

       430        440        450        460        470        480 
MIQGVPESDA YVVHENRRDA IRFAVNQAEA GDVILIAGKG HEDYQVVGDE VIDFDDRVEA 

       490 
RIAIEKKLGL A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591982 Genomic DNA. Translation: CAD00116.1.
PIRAF1329.
RefSeqNP_465562.1.

3D structure databases

SMRQ8Y5L9. Positions 2-486.
ModBaseSearch...

Genome annotation databases

GeneID987940.
KEGGlmo:lmo2038.

Organism-specific databases

ListiListLMO02038.
CMRSearch...

Phylogenomic databases

HOGENOMHBG602753.
OMAEHLDFHG.

Enzyme and pathway databases

BioCycLMON169963:LMO2038-MONOMER.
BRENDA6.3.2.13. 96770.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
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]
Gene3DG3DSA:3.90.190.20. Mur_ligase_C. 1 hit.
G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_LISMO
AccessionPrimary (citable) accession number: Q8Y5L9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: February 9, 2010
This is version 54 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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