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Q87WY0 (MURE_PSESM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. 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:PSPTO_4413
OrganismPseudomonas syringae pv. tomato (strain DC3000) [Complete proteome] [HAMAP]
Taxonomic identifier223283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length487 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 – 487487UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_0000101928

Regions

Nucleotide binding108 – 1147ATP Potential
Region150 – 1512UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region402 – 4054Meso-diaminopimelate binding By similarity
Motif402 – 4054Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site231UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site251UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1771UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1831UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3781Meso-diaminopimelate By similarity
Binding site4531Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4571Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2171N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87WY0 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: FBF47A42D387E905

FASTA48752,197
        10         20         30         40         50         60 
MAFNLSKIFA HTDRDPLIRE LTLDSRNVRP GDLFLAVPGI KVDGRAHIAD ALKRGAAAVA 

        70         80         90        100        110        120 
YEVEGATVLP ITDVPLIPVK GLAAQLSDVA GRFYGDPSRS LNLVGVTGTN GKTSVTQLVA 

       130        140        150        160        170        180 
QALDALGQRC GIVGTLGTGF YGALQSGRHT TPDPIAVQAA LTDLRKAGAR AVAMEVSSHG 

       190        200        210        220        230        240 
LDQGRATALA FDVAVLTNLS RDHLDYHGTM EAYAAAKAKL FAWPNLNCRV INLDDDFGRE 

       250        260        270        280        290        300 
LAGLKQESRL ITYSQLDSSA YLYCRDAKFD DDGVRATLVT PQGEHFLRSS LLGRFNLSNV 

       310        320        330        340        350        360 
LAAVGALLGL DYALDEILKV LPKLEGPVGR MQRLGGADKP LVVVDYAHTP DALEKVLEAL 

       370        380        390        400        410        420 
RPHAKGRLLC LFGCGGDRDR GKRPLMAEVV ERLADGVWVT DDNPRSEAPT NIFDDIRPGF 

       430        440        450        460        470        480 
VTADKVRFIE GRGQAIAELI ASATVDDVVV LAGKGHEDYQ EIDGKRQPFS DLEEAATALA 


AWGPEND 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016853 Genomic DNA. Translation: AAO57862.1.
RefSeqNP_794167.1. NC_004578.1.

3D structure databases

ProteinModelPortalQ87WY0.
ModBaseSearch...

Protein-protein interaction databases

STRING223283.PSPTO_4413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO57862; AAO57862; PSPTO_4413.
GeneID1186094.
KEGGpst:PSPTO_4413.
PATRIC20000336. VBIPseSyr93040_4528.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAFEDYLAC.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycPSYR223283:GJIX-4478-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_PSESM
AccessionPrimary (citable) accession number: Q87WY0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 78 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