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Q64ZL7 (MURE_BACFR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. 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:BF0310
OrganismBacteroides fragilis (strain YCH46) [Complete proteome] [HAMAP]
Taxonomic identifier295405 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length485 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 – 485485UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000012338

Regions

Nucleotide binding111 – 1177ATP Potential
Region153 – 1542UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region402 – 4054Meso-diaminopimelate binding By similarity
Motif402 – 4054Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1801UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3781Meso-diaminopimelate By similarity
Binding site4551Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4591Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2201N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q64ZL7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 3B3A3E3500581913

FASTA48553,195
        10         20         30         40         50         60 
MKLKEILTSI QPVKITGNQD IEITGVDIDS RQVESGHLFM AMHGTQTDGH AYIPAAVEKG 

        70         80         90        100        110        120 
ATAILCEELP VELAEGVTYI QVADSEDAVG KAATTFYGNP SSKLELVGVT GTNGKTTIAT 

       130        140        150        160        170        180 
LLYNTFRYFG YKVGLISTVC NYIDDEAIPT EHTTPDPITL NRLLGRMADE GCKYVFMEVS 

       190        200        210        220        230        240 
SHSIAQKRIS GLKFAGGIFT NLTRDHLDYH KTVENYLKAK KKFFDDMPKN SFSLTNLDDK 

       250        260        270        280        290        300 
NGLVMTQNTK SKVYTYSLRS LSDFKGRVLE SHFEGMLLDF NNHELAVQFI GKFNASNLLA 

       310        320        330        340        350        360 
VFGAAVLLGK KEEDVLVALS TLHPVAGRFD AIRSPQGYTA IVDYAHTPDA LVNVLNAIHG 

       370        380        390        400        410        420 
VLEGKGKVIT VVGAGGNRDK GKRPIMAKEA ARASDRVIIT SDNPRFEEPQ DIINDMLAGL 

       430        440        450        460        470        480 
DTEDKKKTLS IADRKEAIRT ACMLAEKGDV ILVAGKGHEN YQDIKGVKHH FDDKEVLKEI 


FSLTV

« Hide

References

[1]"Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions regulating cell surface adaptation."
Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., Kuhara S., Hattori M., Hayashi T., Ohnishi Y.
Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004) [PubMed: 15466707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YCH46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP006841 Genomic DNA. Translation: BAD47059.1.
RefSeqYP_097593.1. NC_006347.1.

3D structure databases

HSSPHSSP built from PDB template 1E8C based on UniProtKB P22188.
ProteinModelPortalQ64ZL7.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3081738.
GenomeReviewsGene locus BF0310 in contig AP006841_GR.
KEGGbfr:BF0310.
NMPDRfig|295405.3.peg.157.
PATRIC21046398. VBIBacFra17906_0333.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG602753.
OMAHTTPEST.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycBFRA295405:BF0310-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_BACFR
AccessionPrimary (citable) accession number: Q64ZL7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 55 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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