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Q8A254 (MURE_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. 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:BT_3452
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length482 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 – 482482UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101867

Regions

Nucleotide binding111 – 1177ATP Potential
Region153 – 1542UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region402 – 4054Meso-diaminopimelate binding By similarity
Motif402 – 4054Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site301UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1801UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1861UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3781Meso-diaminopimelate By similarity
Binding site4551Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4591Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2201N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A254 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B9118A18DF56614B

FASTA48252,932
        10         20         30         40         50         60 
MLLNELLKAI QPVQVTGDSR IEITGVNIDS RLVEAGQLFM AMRGTQTDGH AYIPAAIQKG 

        70         80         90        100        110        120 
ATAILCEDIP EEPVAGITYI QVKDSEDAVG KIATTFYGNP TSQFELVGVT GTNGKTTIAT 

       130        140        150        160        170        180 
LLYNTFRYFG YKVGLISTVC NYIDDQPIPT EHTTPDPITL NRLLGQMADE GCKYVFMEVS 

       190        200        210        220        230        240 
SHSIAQKRIS GLKFAGGIFT NLTRDHLDYH KTVENYLKAK KKFFDDMPKN AFSLTNLDDK 

       250        260        270        280        290        300 
NGLVMTQNTR SKVYTYSLRS LSDFKGRVIE SHFEGMLLDF NNHELAVQFI GKFNASNLLA 

       310        320        330        340        350        360 
VFGAAVLLGK KEEDVLLALS TLHPVAGRFD AIRSPKGVTA IVDYAHTPDA LVNVLNAIHG 

       370        380        390        400        410        420 
VLEGKGKVIT VVGAGGNRDK GKRPIMAKEA AKASDRVIIT SDNPRFEEPQ EIINDMLAGL 

       430        440        450        460        470        480 
DAEDMKKTLS IADRKEAIRT ACMLAEKGDV ILVAGKGHEN YQEIKGVKHH FDDKEVLKEI 


FN 

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References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015928 Genomic DNA. Translation: AAO78558.1.
RefSeqNP_812364.1. NC_004663.1.

3D structure databases

ProteinModelPortalQ8A254.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1073969.
GenomeReviewsGene locus BT_3452 in contig AE015928_GR.
KEGGbth:BT_3452.
NMPDRfig|226186.1.peg.3451.
PATRIC21061917. VBIBacThe70966_3519.

Phylogenomic databases

HOGENOMHBG602753.
OMAHTTPEST.
PhylomeDBQ8A254.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycBTHE226186:BT_3452-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_BACTN
AccessionPrimary (citable) accession number: Q8A254
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 66 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