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A1WC11 (MURE_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. 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:Ajs_3675
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length501 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 – 501501UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000058582

Regions

Nucleotide binding112 – 1187ATP Potential
Region161 – 1622UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region417 – 4204Meso-diaminopimelate binding By similarity
Motif417 – 4204Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site291UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1961UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3931Meso-diaminopimelate By similarity
Binding site4681Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4721Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2281N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1WC11 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: E83400474E25A732

FASTA50152,501
        10         20         30         40         50         60 
MNALHTLTTL QEAVDWLRQR VTGTLQTDSR LIQPGDGFIA WPGAATDGRA HVGDAVARGA 

        70         80         90        100        110        120 
AACLVECEGV EPFALAGDHI AALRGLKAAT GMIASEWFGH PTQRLQVLAV TGTNGKTSTA 

       130        140        150        160        170        180 
WWLADALNQL SKEELPALAG CALVGTLGMG VPPALQTTGM TTPDPVRLQR AFAQFAEAGH 

       190        200        210        220        230        240 
RACAIEASSI GLAEHRLDGT RIHVALFTNF TQDHLDYHPG MAAYWQAKRA LFDWPGLRAA 

       250        260        270        280        290        300 
VVNVDDPQGA ALHAELQGSD LDLWSISLQG PARLQAKHIV HTGAGLALTV AEGAHTEVLQ 

       310        320        330        340        350        360 
TQVIGLYNVS NLLGVIAGMR ALGVPLAQAL QACARLRPVP GRMEQLAAAG QPLVAVDYAH 

       370        380        390        400        410        420 
TPDALHQALA ALKPVAAQRG GRLWCVFGCG GNRDAGKRPL MGAVAQREAD EVIVTSDNPR 

       430        440        450        460        470        480 
GEEPQSIIHQ ILLGTIAGTS VRAEVDRAAA IAQALAEAGA NDVVLIAGKG HEDYQEAAGQ 

       490        500 
RVPFSDMAHA RAALARRGGV A

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000539 Genomic DNA. Translation: ABM43786.1.
RefSeqYP_987862.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1WC11.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1WC11.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4673617.
GenomeReviewsGene locus Ajs_3675 in contig CP000539_GR.
KEGGajs:Ajs_3675.
PATRIC20692747. VBIAciSp27161_3889.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHBG602753.
OMAAQAWHRL.
PhylomeDBA1WC11.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycASP232721:AJS_3675-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_ACISJ
AccessionPrimary (citable) accession number: A1WC11
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 39 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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