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A3MY85 (MURE_ACTP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:APL_0013
OrganismActinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]
Taxonomic identifier416269 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus ›

Protein attributes

Sequence length500 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 – 500500UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012333

Regions

Nucleotide binding123 – 1297ATP Potential
Region43 – 453UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region165 – 1662UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region423 – 4264Meso-diaminopimelate binding By similarity
Motif423 – 4264Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site261UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site281UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1641UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1921UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1981UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site2001UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3991Meso-diaminopimelate By similarity
Binding site4741Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4781Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2321N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MY85 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: D65A0C4EC9E4784A

FASTA50054,629
        10         20         30         40         50         60 
MKRLLPFLTE LDAWVTELKP LKQMTLDSRQ VDEGDLFVAL KGHQVDGRRF IQKAIEQGAA 

        70         80         90        100        110        120 
LVLAEADEGQ DEIELDAKFA KYNLDRTACK VVLVPNLARI LSEIAGAFYA NPSEKLTLVG 

       130        140        150        160        170        180 
VTGTNGKTTS AQLLAQWHNL LGGKSAVMGT IGNGLYGKVQ EAANTTGSAI EVQRNLADFV 

       190        200        210        220        230        240 
EMGADFCAME VSSHGLAQYR AEALSYDLAV FTNLSRDHLD YHKTMEEYAQ AKFRLFSELD 

       250        260        270        280        290        300 
TKAQVLNADD EVGREWLAKL PDAVAVSTDA SFSSEHKFVK ATDVSFSLQG VKIAFESSWG 

       310        320        330        340        350        360 
NGELNSRLIG AFNVNNLLTA LAGLLVLGHD LPKLIETAPL LQGVAGRMEC VVSQKNPQNR 

       370        380        390        400        410        420 
PLVLVDYAHT PDALEKALQA ARLHTEGELY CIFGCGGDRD AGKRPMMAAI AEELADKVIA 

       430        440        450        460        470        480 
TDDNPRTEDN AKIMADILNG FVQVEKVQVI HDREQAIKTA IEQANEKDVI LIAGKGHEDY 

       490        500 
QIIGTTKHHF SDQETAAKYL

« Hide

References

[1]"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)."
Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E.
J. Bacteriol. 190:1495-1496(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: L20.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000569 Genomic DNA. Translation: ABN73121.1.
RefSeqYP_001052726.1. NC_009053.1.

3D structure databases

ProteinModelPortalA3MY85.
SMRA3MY85. Positions 12-500.
ModBaseSearch...

Protein-protein interaction databases

STRING416269.APL_0013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN73121; ABN73121; APL_0013.
GeneID4849091.
KEGGapl:APL_0013.
PATRIC20744802. VBIActPle94089_0015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycAPLE416269:GHV7-13-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.90.190.20. 1 hit.
HAMAPMF_00208. MurE.
InterProIPR004101. 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. Mur_ligase_C. 1 hit.
SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_ACTP2
AccessionPrimary (citable) accession number: A3MY85
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: May 29, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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