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Reviewed, UniProtKB/Swiss-Prot Q83F28 (MURE_COXBU)

Last modified July 22, 2008. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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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):
    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: CBU_0123
OrganismCoxiella burnetii [Complete proteome] [HAMAP]
Taxonomic identifier777 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella

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Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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.

Pathway

Cell wall biosynthesis; peptidoglycan biosynthesis.

Subcellular location

CytoplasmBy similarity.

Post-translational modification

Carbamoylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP By similarity.

Sequence similarities

Belongs to the murCDEF family. MurE subfamily.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 489489UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

Regions

Nucleotide binding113 – 1197ATP Potential
Region155 – 1562UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region412 – 4154Meso-diaminopimelate binding By similarity
Motif412 – 4154Meso-diaminopimelate recognition motif

Sites

Binding site301UDP-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 site3881Meso-diaminopimelate By similarity
Binding site4631Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4671Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2221N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q83F28-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6AC4716157215B22

FASTA48953,828
        10         20         30         40         50         60 
MNGKYLSQLL DAKNKALTAD VLIKALQTDS RKIQPGDLFI AYPGLQVDGR DYIKEALDKK 

        70         80         90        100        110        120 
AAAVFYEANQ YNPSIQTKVP LIPFENLQHR IGEIAARFYD DPSCEMEIIG ITGTNGKTSC 

       130        140        150        160        170        180 
AQFIAQALQS QGIRCGVIGT LGYGFLGSLH KTSHTTPEPI QLQQAFAEMR KQGAKAIAME 

       190        200        210        220        230        240 
VSSHALHQRR VEGVQFDIAV FTQLSRDHLD YHGDMENYAR AKELLFQQPG LHTGVVNCDD 

       250        260        270        280        290        300 
ALGKRIIAHY RHQLTLVGYS ANGVKDDRVS SVIASAIQPL AQGFSVEVQT PWGEGTFTTP 

       310        320        330        340        350        360 
LFGRFNISNL LAVLSVLCLC EIPFDKALLE LSQLRNVPGR MQVVDSQRQP QIIVDYAHTP 

       370        380        390        400        410        420 
DALEKALTAL REHCQGRLIC VFGCGGDRDR GKRPQMAAVA EQHADQIILT NDNPRTESPL 

       430        440        450        460        470        480 
TIIQDIQAGF KNKNAVLVKL DRAEAIRYAV QMAAVNDIVL IAGKGHETTQ TIADQVLPFN 


DVEEAKKAL

« Hide

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Cross-references

Sequence databases

AE016828 Genomic DNA. Translation: AAO89687.1.
RefSeqNP_819173.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1207994.
GenomeReviewsGene locus CBU_0123 in contig AE016828_GR.
KEGGcbu:CBU_0123.
NMPDRfig|227377.1.peg.117.
TIGRCBU_0123.

Phylogenomic databases

HOGENOMQ83F28.

Enzyme and pathway databases

BioCycCBUR227377:CBU_0123-MON.

Family and domain databases

HAMAPMF_00208.
[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.
ProDomQ83F28.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameMURE_COXBU
AccessionPrimary (citable) accession number: Q83F28
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: July 22, 2008
This is version 39 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)

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Relevant documents

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names

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