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A4W6I8 (MURE_ENT38) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 37. 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:Ent638_0631
OrganismEnterobacter sp. (strain 638) [Complete proteome] [HAMAP]
Taxonomic identifier399742 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter

Protein attributes

Sequence length495 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 – 495495UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000058587

Regions

Nucleotide binding116 – 1227ATP Potential
Region44 – 463UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region158 – 1592UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region414 – 4174Meso-diaminopimelate binding By similarity
Motif414 – 4174Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site271UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site291UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1571UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1931UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3901Meso-diaminopimelate By similarity
Binding site4651Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4691Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2251N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A4W6I8 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: B3306168CE6F0FE9

FASTA49553,275
        10         20         30         40         50         60 
MADRNLRDLL APWVQNVPAR ALREMVLDSR VAASGDLFVA VVGHQADGRR YIPQAIAQGV 

        70         80         90        100        110        120 
AAIIAEAKDD ATDGEIREMH GVPVIYLSQL NERLSALAGR FYHEPSDQLR LVGVTGTNGK 

       130        140        150        160        170        180 
TTTTQLMAQW AQLLGETGAV MGTVGNGLLG KVNPTENTTG SAVDVQHVLS GLAGQGATFA 

       190        200        210        220        230        240 
AMEVSSHGLV QHRVSALKFA ASVFTNLSRD HLDYHGDMEN YEAAKWLLYS THHCGQAIIN 

       250        260        270        280        290        300 
ADDEVGRRWL AKLPDAVAVS MEDHINPNCH GRWLKATDVD YHDSGATIRF ASSWGEGEIE 

       310        320        330        340        350        360 
SRLMGAFNVS NLLLALATLL ALDYPLSELV NTGARLQPVC GRMEVFTAPG KPTVVVDYAH 

       370        380        390        400        410        420 
TPDALEKALQ AARLHCTGKL WCVFGCGGDR DKGKRPLMGA IAEQFADIPV VTDDNPRTEE 

       430        440        450        460        470        480 
PRAIINDILA GMMDAGHARV VEGRAEAVTN AIMQAKENDV VLLAGKGHED YQIVGAHRLD 

       490 
YSDRVTAARL LGALA

« Hide

References

[1]"Complete sequence of chromosome of Enterobacter sp. 638."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 638.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000653 Genomic DNA. Translation: ABP59318.1.
RefSeqYP_001175369.1. NC_009436.1.

3D structure databases

ProteinModelPortalA4W6I8.
SMRA4W6I8. Positions 3-495.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4W6I8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5113670.
GenomeReviewsGene locus Ent638_0631 in contig CP000653_GR.
KEGGent:Ent638_0631.
NMPDRfig|399742.4.peg.685.
PATRIC20410808. VBIEntSp101211_0761.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHBG602753.
OMAGALAYVD.
PhylomeDBA4W6I8.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycESP42895:ENT638_0631-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_ENT38
AccessionPrimary (citable) accession number: A4W6I8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 29, 2007
Last modified: January 25, 2012
This is version 37 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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