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Q0I1D8 (MURE_HAES1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. 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:HS_0353
OrganismHaemophilus somnus (strain 129Pt) (Histophilus somni (strain 129Pt)) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Histophilus ›

Protein attributes

Sequence length495 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 – 495495UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012359

Regions

Nucleotide binding117 – 1237ATP Potential
Region45 – 473UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region159 – 1602UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region418 – 4214Meso-diaminopimelate binding By similarity
Motif418 – 4214Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site281UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1581UDP-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 site3941Meso-diaminopimelate By similarity
Binding site4691Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4731Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2261N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I1D8 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 93B412FEA2CFAAA5

FASTA49554,656
        10         20         30         40         50         60 
MKKLTALWDI DEQLDSVHRD IELQEMILDS RLANTGCLFV AIKGHRVDGR EFIMQAIQNG 

        70         80         90        100        110        120 
ASAVLFETDL VEQHLTVSFE QNIPLIAYYE LSKHLSHIAD RFYSSPSQRL TLVGVTGTNG 

       130        140        150        160        170        180 
KTTIAQLLAQ WTQILGHTSA VMGTIGNGLF GQIKEASNTT GSAIEIQSSL DKFIRQGADF 

       190        200        210        220        230        240 
AAIEVSSHGL VQHRVEALTF RAGIFTNLSR DHLDYHHTME NYAQAKKRLF SELNCQHKIL 

       250        260        270        280        290        300 
NVDDEIGATW LIELSKDDPD VVAVSCRADY QPDTKNWLKA TALSFHSKGT TIEFASSWGN 

       310        320        330        340        350        360 
GILSSPLIGG FNVSNLLLVL ATLLSLGYDI GKLLATVRQL TGVCGRMEML SAKHKATVIV 

       370        380        390        400        410        420 
DYAHTPDALE NALQSAAVHC QGKLWCIFGC GGDRDRGKRP LMAAIAEKFA DSVIVTDDNP 

       430        440        450        460        470        480 
RTENPEQIMQ DILTGFQQSS AVQIIHQREQ AIKTALQSAV ENDVVLIAGK GHENYQIIGT 

       490 
TKYHFSDQEI VKKYF

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000436 Genomic DNA. Translation: ABI24631.1.
RefSeqYP_718563.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I1D8.
SMRQ0I1D8. Positions 19-495.
ModBaseSearch...

Protein-protein interaction databases

STRING205914.HS_0353.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI24631; ABI24631; HS_0353.
GeneID4239829.
KEGGhso:HS_0353.
PATRIC20280643. VBIHaeSom53361_0371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAHTMEEYA.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-370-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_HAES1
AccessionPrimary (citable) accession number: Q0I1D8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: May 1, 2013
This is version 58 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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