Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q39YM4 (MURE_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Gmet_0407
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter ›

Protein attributes

Sequence length511 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 HAMAP-Rule MF_00208.

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 – 511511UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012353

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-Rule 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
Q39YM4 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 8700F06EAB4E3E6B

FASTA51154,733
        10         20         30         40         50         60 
MRLEDLARVI NPSEAGGSLA LEIEGLYCDS RQVRSGGLFF ALRGVATDGH DYIVASRDRG 

        70         80         90        100        110        120 
AVAVVVEDPS RVPEGMTWLK VDDARLAMSR AAAAFYGNPT DGIPVVGITG TNGKTTTTYL 

       130        140        150        160        170        180 
VEAVMARAGI PVAVLGTISY RFGDKTIPAP HTTPESVDLQ RTIRDLVDRG AQGVVMEVSS 

       190        200        210        220        230        240 
HALEQRRVDG CRFDVGVFTN LTRDHLDYHR DMESYFESKA RLFTELLAAD DTKPRRAAVI 

       250        260        270        280        290        300 
NVDDPYGARL ASDAVAPVVS YGLSPSVMVR AEMVTFSVDG ISGTLVTPLG TIPFHSRLLG 

       310        320        330        340        350        360 
RFNLYNILAA VAAGVALGLS PDAIRGGIEG DVRVPGRLER VDNDHGITVL VDYAHTGDAL 

       370        380        390        400        410        420 
ENVLKTVAEI ATGRIITVFG CGGDRDRGKR PVMGEIAGRF SDLSIVTSDN PRTEDAGAII 

       430        440        450        460        470        480 
GEILGGIRSL GLREYGAEEL ITGFDAKGFA AVESRREAIR LAARVARPGD VLLLAGKGHE 

       490        500        510 
DYQIIGTMKH HFDDREEVAA AFRELSSKGQ G

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000148 Genomic DNA. Translation: ABB30650.1.
RefSeqYP_006719370.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39YM4.
ModBaseSearch...

Protein-protein interaction databases

STRING269799.Gmet_0407.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB30650; ABB30650; Gmet_0407.
GeneID3738162.
KEGGgme:Gmet_0407.
PATRIC21999962. VBIGeoMet55070_0428.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMARPLMGEA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycGMET269799:GHNY-409-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_GEOMG
AccessionPrimary (citable) accession number: Q39YM4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: May 1, 2013
This is version 60 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents