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P59419 (MURE_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. 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:bbp_203
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length508 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.

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 – 508508UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101875

Regions

Nucleotide binding121 – 1277ATP Potential
Region163 – 1642UDP-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 site331UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1621UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1961UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1981UDP-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 residue2301N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P59419 [UniParc].

Last modified March 28, 2003. Version 1.
Checksum: B69747808687D18F

FASTA50858,577
        10         20         30         40         50         60 
MTILIKNNNL QQLLSSWIKL SYSYTISGIQ SDSRLVKPGY LFCVLKKKNI NETNKHMIHA 

        70         80         90        100        110        120 
IKNGAKIILY DTKQKFKNGT LKKIINHVPI IYFFKLSKNL PQILKKYYHF ENNFTLIGIT 

       130        140        150        160        170        180 
GTNGKSTTTH IVSQWANLLN VKIGIMGTLG HGINNNLKKT DNTTESSANI HQFLYHMLKQ 

       190        200        210        220        230        240 
NIKTFAIEIS SHGIVQHRIE QLPFKIAILT NITPEHLDYH RTMDNYINAK KAFFFKYNIN 

       250        260        270        280        290        300 
TLIINADDLI AKTWIKKLNH KNVITITTKD QNFNSISPKK WIHANKIIQK QNCTNIHFNS 

       310        320        330        340        350        360 
SWGHGILNST LIGHFNVINI LLALATLLEL NYPITDLVKV CKYIKTISGR MEHIHIVNKP 

       370        380        390        400        410        420 
KVIIDYAHNT NGLKNLLSTL KEIFNKKKIW CIFGCGGDRD KTKRPYMGSI AEKMSDQVIL 

       430        440        450        460        470        480 
TNDNPRNEHP LKIIKNILSG CKFKNKIRII PNREHAIKFA VNNADKEDII VVAGKGHEKY 

       490        500 
QIINNKYYHF SDHKIIKKLL NKKNYDFN 

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016826 Genomic DNA. Translation: AAO26935.1.
RefSeqNP_777830.1. NC_004545.1.

3D structure databases

ProteinModelPortalP59419.
ModBaseSearch...

Protein-protein interaction databases

STRING224915.bbp203.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26935; AAO26935; bbp_203.
GeneID1058584.
KEGGbab:bbp203.
PATRIC21245181. VBIBucAph80364_0197.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
KOK01928.
OMARPLMGEA.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-203-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.
IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase.
[Graphical view]
PfamPF02875. 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_BUCBP
AccessionPrimary (citable) accession number: P59419
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: May 1, 2013
This is version 84 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