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Reviewed, UniProtKB/Swiss-Prot Q4QLG3 (MURE_HAEI8)

Last modified February 9, 2010. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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):
    UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase
    Meso-diaminopimelate-adding enzyme
    Meso-A2pm-adding enzyme
    UDP-N-acetylmuramyl-tripeptide synthetase
    UDP-MurNAc-tripeptide synthetase
Gene names
Name: murE
Ordered Locus Names: NTHI1300
OrganismHaemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]
Taxonomic identifier281310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length488 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 – 488488UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_1000012356

Regions

Nucleotide binding113 – 1197ATP Potential
Region41 – 433UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region410 – 4134Meso-diaminopimelate binding By similarity
Motif410 – 4134Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site241UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site261UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1541UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1821UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1901UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3861Meso-diaminopimelate By similarity
Binding site4611Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4651Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2221N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4QLG3-1 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 01690E772AB7D99C

FASTA48853,643
        10         20         30         40         50         60 
MKKLTALFNL PELKNDIELH NMVLDSRKVK AGDLFVAIKG HQVDGNQFID SALHSGASAV 

        70         80         90        100        110        120 
VSETELSSEH LTVAFIRNVP VVKYYQLARH LSSLADVFYD SPSKNLTLVG VTGTNGKTTI 

       130        140        150        160        170        180 
SQLLAQWAEL LGHRAAVMGT IGNGLLGQIV EAKNTTGSAV EIQSSLSTFK HAGADFTSIE 

       190        200        210        220        230        240 
VSSHGLAQHR VEALHFKAAI FTNLTRDHLD YHQSMENYAA AKKRLFTELD TQIKVINADD 

       250        260        270        280        290        300 
EIGYQWLTEL PDAIAVSMNA DFKVGSHQWM KAINIHYHFK GADITFESSW GNGVLHSPLI 

       310        320        330        340        350        360 
GAFNVSNLLL VMTTLLSFGY PLENLLATAK SLKGVCGRME MIQYPNKPIV IVDYAHTPDA 

       370        380        390        400        410        420 
LEKALIAARE HCQGELWCIF GCGGDRDRGK RPLMAQVAEQ FAEKIIVTKD NPRTEPQSQI 

       430        440        450        460        470        480 
EADIVAGFKN MEKVGIIPDR AQAIQFAIES AVENDVILIA GKGHEHYQII GSEVVHFSDQ 


EIALDFLK 

« Hide

References

[1]"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20."
Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr.
J. Bacteriol. 187:4627-4636(2005) [PubMed: 15968074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000057 Genomic DNA. Translation: AAX88134.1.
RefSeqYP_248794.1.

3D structure databases

HSSPHSSP built from PDB template 1E8C based on UniProtKB P22188.
SMRQ4QLG3. Positions 15-487.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4QLG3.

Genome annotation databases

GeneID3430562.
GenomeReviewsGene locus NTHI1300 in contig CP000057_GR.
KEGGhit:NTHI1300.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHBG602753.
OMAHTPDGIE.
PhylomeDBQ4QLG3.

Enzyme and pathway databases

BioCycHINF281310:NTHI1300-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.
PfamPF01225. Mur_ligase. 1 hit.
PF02875. Mur_ligase_C. 1 hit.
PF08245. Mur_ligase_M. 1 hit.
[Graphical view]
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_HAEI8
AccessionPrimary (citable) accession number: Q4QLG3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2005
Last modified: February 9, 2010
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents