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Q7V8U6 (MURE_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. 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:PMT_0230
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length507 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 – 507507UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101924

Regions

Nucleotide binding117 – 1237ATP Potential
Region159 – 1602UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region424 – 4274Meso-diaminopimelate binding By similarity
Motif424 – 4274Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site321UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1921UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1941UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site4001Meso-diaminopimelate By similarity
Binding site4751Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4791Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2261N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V8U6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D6983D88B5F1B7BC

FASTA50753,567
        10         20         30         40         50         60 
MTQMLHSLLR AVGLPVPEGL ANPSLAMVSC DSRSVAQGCL FLGLPGEQVD GGSFWRQALA 

        70         80         90        100        110        120 
AGAEAAVIGP AAAALQPPGP TDAVVVVPEP VAAWVGQLAA AFWQQPSSRF ALIGVTGTNG 

       130        140        150        160        170        180 
KTTTTHLIEH LSVAVGRSTA LFGTLVNRWP NYSVPATHTT AFADRLQAQL AQAVEAGAEL 

       190        200        210        220        230        240 
GVMEVSSHAL EQQRVAGCRF AGAVFTNLTQ DHLDYHCSME AYFEAKAQLF APPLLESGSA 

       250        260        270        280        290        300 
KAVVNIDSPW GARLAQRLGD TCWRSSLAEG VLQQADAELK MTELTMSSDG VQGRLISPCG 

       310        320        330        340        350        360 
EGWFDSPLMG RFNLMNLLQA VGVLLQQGLP LPLLLKAIAD FRGVPGRMER VLIPAADATQ 

       370        380        390        400        410        420 
VPTVLVDYAH TPDGLENALK ASRPFTSKNL CCVFGCGGDR DRGKRSQMAA IAARLADRVV 

       430        440        450        460        470        480 
VTSDNPRTED PQQILADVVA GIPEGTTCTV EVDRAVAIAL AIAEAAPGDV VLVAGKGHED 

       490        500 
YQILGTSKVH FDDREEAERA LKQRLDG 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE20405.1.
RefSeqNP_894063.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V8U6.
ModBaseSearch...

Protein-protein interaction databases

STRING74547.PMT0230.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20405; CAE20405; PMT_0230.
GeneID1727531.
KEGGpmt:PMT0230.
PATRIC23008191. VBIProMar135351_0256.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
KOK01928.
OMARPLMGEA.
ProtClustDBPRK00139.

Enzyme and pathway databases

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_PROMM
AccessionPrimary (citable) accession number: Q7V8U6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2003
Last modified: May 1, 2013
This is version 72 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