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Q0A6J7 (MURE_ALHEH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. 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:Mlg_2198
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Ectothiorhodospiraceae › Alkalilimnicola ›

Protein attributes

Sequence length498 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 – 498498UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000058584

Regions

Nucleotide binding120 – 1267ATP Potential
Region162 – 1632UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region416 – 4194Meso-diaminopimelate binding By similarity
Motif416 – 4194Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site291UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1891UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1951UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1971UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3921Meso-diaminopimelate By similarity
Binding site4661Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4701Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2291N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A6J7 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 47C311F5CA7964C6

FASTA49852,734
        10         20         30         40         50         60 
MMRLRTLLQP WLDLTDADDR PVGGLAVDSR DIEPGFVFVA LRGSRHHGLG YLGDALAAGA 

        70         80         90        100        110        120 
GAVLWEPAGD VAPEPDERTA AERAGVPLIA VPDLGRRLGP IAARLYGDPS ARMRVVGVTG 

       130        140        150        160        170        180 
TDGKTSVTQY LAQLLDREAH RCGLVGTLGS GFPDSLQPGT HTTPDAASVQ RTLARLHRQG 

       190        200        210        220        230        240 
AAQVAMEVSS HALDQHRVAG VRFHTAVLTN LGRDHLDYHG DLAGYAEAKS RLFGVPGLQW 

       250        260        270        280        290        300 
AVLNLDDAFG RQVHGALAGG TRALGYSLAG HPQAGVRGEG LVLEPQGLRL RLSTEWGEAP 

       310        320        330        340        350        360 
VQAPLLGAFN AANVLAVAAA ALSLGVALPV IVERLAGLRP VPGRMEPFTR PGRPSVIVDY 

       370        380        390        400        410        420 
AHTPAALRGA LAAVRAHYRG AVWLVFGCGG DRDRGKRPLM GEAAAELADR VVLTDDNPRR 

       430        440        450        460        470        480 
EDPDRIIDDI RQGAPGRDWP VLRDRAGAIR HAVERAGPED VVLVAGKGHE TVQQIGDRCL 

       490 
PFSDREAVVQ ALGEEEGA

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MLHE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000453 Genomic DNA. Translation: ABI57540.1.
RefSeqYP_743030.1. NC_008340.1.

3D structure databases

ProteinModelPortalQ0A6J7.
ModBaseSearch...

Protein-protein interaction databases

STRING187272.Mlg_2198.

Proteomic databases

PRIDEQ0A6J7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI57540; ABI57540; Mlg_2198.
GeneID4270977.
KEGGaeh:Mlg_2198.
PATRIC20863653. VBIAlkEhr114327_2195.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMARPLMGEA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycAEHR187272:GHAX-2254-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_ALHEH
AccessionPrimary (citable) accession number: Q0A6J7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: May 1, 2013
This is version 57 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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