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P65478 (MURE_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 56. 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:Mb2182c
OrganismMycobacterium bovis [Complete proteome] [HAMAP]
Taxonomic identifier1765 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length535 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 – 535535UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101914

Regions

Nucleotide binding153 – 1597ATP Potential
Region195 – 1962UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region448 – 4514Meso-diaminopimelate binding By similarity
Motif448 – 4514Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site671UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site2221UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site2301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site4241Meso-diaminopimelate By similarity
Binding site5021Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site5061Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2621N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P65478 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 4EB7D79C6374817E

FASTA53555,341
        10         20         30         40         50         60 
MSSLARGISR RRTEVATQVE AAPTGLRPNA VVGVRLAALA DQVGAALAEG PAQRAVTEDR 

        70         80         90        100        110        120 
TVTGVTLRAQ DVSPGDLFAA LTGSTTHGAR HVGDAIARGA VAVLTDPAGV AEIAGRAAVP 

       130        140        150        160        170        180 
VLVHPAPRGV LGGLAATVYG HPSERLTVIG ITGTSGKTTT TYLVEAGLRA AGRVAGLIGT 

       190        200        210        220        230        240 
IGIRVGGADL PSALTTPEAP TLQAMLAAMV ERGVDTVVME VSSHALALGR VDGTRFAVGA 

       250        260        270        280        290        300 
FTNLSRDHLD FHPSMADYFE AKASLFDPDS ALRARTAVVC IDDDAGRAMA ARAADAITVS 

       310        320        330        340        350        360 
AADRPAHWRA TDVAPTDAGG QQFTAIDPAG VGHHIGIRLP GRYNVANCLV ALAILDTVGV 

       370        380        390        400        410        420 
SPEQAVPGLR EIRVPGRLEQ IDRGQGFLAL VDYAHKPEAL RSVLTTLAHP DRRLAVVFGA 

       430        440        450        460        470        480 
GGDRDPGKRA PMGRIAAQLA DLVVVTDDNP RDEDPTAIRR EILAGAAEVG GDAQVVEIAD 

       490        500        510        520        530 
RRDAIRHAVA WARPGDVVLI AGKGHETGQR GGGRVRPFDD RVELAAALEA LERRA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248341 Genomic DNA. Translation: CAD97035.1.
RefSeqNP_855831.1. NC_002945.3.

3D structure databases

ProteinModelPortalP65478.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000015657; EBMYCP00000015492; EBMYCG00000015653.
GeneID1091262.
GenomeReviewsGene locus Mb2182c in contig BX248333_GR.
KEGGmbo:Mb2182c.
PATRIC18006504. VBIMycBov88188_2398.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000015779.
HOGENOMHBG602753.
OMAHTTPEST.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycMBOV233413:MB2182C-MONOMER.

Family and domain databases

HAMAPMF_00208. MurE.
[Tree]
InterProIPR004101. 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.
KOK01928.
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_MYCBO
AccessionPrimary (citable) accession number: P65478
Secondary accession number(s): O06219
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 56 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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