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Q7NPZ4 (MURE_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:CV_4348
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length493 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 – 493493UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101884

Regions

Nucleotide binding114 – 1207ATP Potential
Region156 – 1572UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region410 – 4134Meso-diaminopimelate binding By similarity
Motif410 – 4134Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1831UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1891UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3861Meso-diaminopimelate By similarity
Binding site4601Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4641Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2231N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NPZ4 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: C5CA8187D9F19E7D

FASTA49352,957
        10         20         30         40         50         60 
MKSRLTALPD WDPALLQQLG LPIKRVEADS RRVLPGDVFL ACRGEYADGR DFIPAALEKG 

        70         80         90        100        110        120 
AAAVLWDEAD GFAWKAEWQA PNLAVPNLRE RAGIVAAHVL GLPSRDLTVV GITGTNGKTS 

       130        140        150        160        170        180 
ISHWLAQAFS LLGQKAALIG TVGNGFYGHL TETTHTTPDP VTVQQKLAEY RRQGAHVVTM 

       190        200        210        220        230        240 
EVSSHGLDQF RVNGVEFATA VFTNLTRDHL DYHGSMEAYG ESKKKLFFWE GLKHAVINAD 

       250        260        270        280        290        300 
DAFGRQLAAG IDPKQTRVVT YGLEQGDVRP LALAATLEGL QLTVATPWGT VDVRTGLVGR 

       310        320        330        340        350        360 
FNAANLLACL ATLCVNGVSL QDAAAVMARI QPARGRMQSV GGAHEPLVVI DYAHTPDALE 

       370        380        390        400        410        420 
KALATLSEIR PAGGRLFCVF GCGGDRDPGK RPMMGAIAEK HADVAVLTSD NPRSEDPQAI 

       430        440        450        460        470        480 
IRDVLAGMDA ARAHVEADRE AAIHWAVAQA RVGDVVLVAG KGHEEYQDIA GVKRPFSDFR 

       490 
VAEEALTAWG KRP

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References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ62007.1.
RefSeqNP_904018.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NPZ4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2549599.
GenomeReviewsGene locus CV_4348 in contig AE016825_GR.
KEGGcvi:CV_4348.
NMPDRfig|243365.1.peg.4348.
PATRIC21443557. VBIChrVio67196_4268.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG602753.
OMAGALAYVD.
PhylomeDBQ7NPZ4.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCVIO243365:CV_4348-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_CHRVO
AccessionPrimary (citable) accession number: Q7NPZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: December 15, 2003
Last modified: January 25, 2012
This is version 68 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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