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Reviewed, UniProtKB/Swiss-Prot Q748D2 (MURE_GEOSL)

Last modified February 9, 2010. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase
Gene names
Name: murE
Ordered Locus Names: GSU3074
OrganismGeobacter sulfurreducens [Complete proteome] [HAMAP]
Taxonomic identifier35554 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length509 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 – 509509UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000012354

Regions

Nucleotide binding110 – 1167ATP Potential
Region152 – 1532UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region409 – 4124Meso-diaminopimelate binding By similarity
Motif409 – 4124Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1791UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1871UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3851Meso-diaminopimelate By similarity
Binding site4761Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4801Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2191N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q748D2-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9D0A9448D1BAACED

FASTA50954,778
        10         20         30         40         50         60 
MRLEDLARVV DPIAVRGDLT REINGLYCDS RQVRSGGLFF ALKGVASDGH DFIASARERG 

        70         80         90        100        110        120 
AVAVVLEDET RAPCGMEWIR VGDARLAMSR MAALFYGQPT DGVPVVGITG TNGKTTTTYL 

       130        140        150        160        170        180 
VEAIMSRAGI PAAVLGTISY RFGSKLVPAP HTTPESVELQ ATIRDLVDEG AKAVVMEVSS 

       190        200        210        220        230        240 
HALEQRRVDS CRFDVAVFTN LTRDHLDYHR DMESYFGSKA RLFTELVAPD GVKPRRAAAI 

       250        260        270        280        290        300 
NRDDSYGARL VETAVAPVIS YGLAADAAVR AENVVFSVDG IAGTLVTPFG TAPFHSHLLG 

       310        320        330        340        350        360 
RFNLYNILAA VAAGVGLGLS LDVILGGIEG DVRVPGRLER VHNERGVTVL VDYAHTGDAL 

       370        380        390        400        410        420 
ENVLKTVSEL ATGRIITVFG CGGDRDRGKR PVMAEISGRY SHLTIVTSDN PRTEEPAAII 

       430        440        450        460        470        480 
KEVLTGIIPM GLREYDAREL NRGFVEKGFT SLVSRHDAIR LAATVAVAGD IVLLAGKGHE 

       490        500 
DYQIIGTEKF HFDDREEAIA AFRSSDSGE 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017180 Genomic DNA. Translation: AAR36465.1.
RefSeqNP_954115.1.

3D structure databases

HSSPHSSP built from PDB template 1E8C based on UniProtKB P22188.
SMRQ748D2. Positions 16-504.
ModBaseSearch...

Genome annotation databases

GeneID2686302.
GenomeReviewsGene locus GSU3074 in contig AE017180_GR.
KEGGgsu:GSU3074.
NMPDRfig|243231.1.peg.3053.
TIGRGSU3074.

Phylogenomic databases

HOGENOMHBG602753.
OMAEHLDFHG.

Enzyme and pathway databases

BioCycGSUL243231:GSU_3074-MONOMER.
BRENDA6.3.2.13. 276898.

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.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_GEOSL
AccessionPrimary (citable) accession number: Q748D2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents