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Q3ME15 (MURE_ANAVT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Ava_1147
OrganismAnabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]
Taxonomic identifier240292 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeAnabaena

Protein attributes

Sequence length496 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 HAMAP-Rule MF_00208.

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 – 496496UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012335

Regions

Nucleotide binding116 – 1227ATP Potential
Region158 – 1592UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region413 – 4164Meso-diaminopimelate binding By similarity
Motif413 – 4164Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site321UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1851UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1911UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1931UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3891Meso-diaminopimelate By similarity
Binding site4641Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4681Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2251N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ME15 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: DCDF7907B96B79BA

FASTA49653,416
        10         20         30         40         50         60 
MKLRELLATV DSVENLPPVL ADTEVKGIKT NSHACGAGDL FIGMPGTRVD GGEFWPSAIA 

        70         80         90        100        110        120 
SGAIAAIVSP QAVEKNPPSD EAVVISSNNM TKACAAIAAA FYGYPGQKLK LVGVTGTNGK 

       130        140        150        160        170        180 
TTTTHLIEFF LTKAQLSTAL MGTLYTRWPG FEQTATHTTP FAVELQQQLA QAVNAGCEFG 

       190        200        210        220        230        240 
VMEVSSHALA QGRVLGCPFE VGVFSNLTQD HLDYHSDMED YFAAKALLFS PDYLKGRAII 

       250        260        270        280        290        300 
NADDTYGQRL IKALSPEKVW SYSVNDSSAD LWMSDLSYEP NGVTGTIHTP EGDVSFRSPL 

       310        320        330        340        350        360 
VGQYNLENLL ASVGAVLHLG LDLQLIANAI PEFPGVPGRM ERVQINPDQD ISVIVDYAHT 

       370        380        390        400        410        420 
PDSLENLLKA ARPFIPGRMI CVFGCGGDRD RTKRPKMGKI AAELADLAFV TSDNPRTEDP 

       430        440        450        460        470        480 
EKILDDILAG IPDTVQPTVI GDRAIAIRTA ILQAQPGDGV LLAGKGHEDY QILGTEKIHF 

       490 
DDREHARAAL TEREKL 

« Hide

References

[1]"Complete sequence of Anabaena variabilis ATCC 29413."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29413 / PCC 7937.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000117 Genomic DNA. Translation: ABA20771.1.
RefSeqYP_321666.1. NC_007413.1.

3D structure databases

ProteinModelPortalQ3ME15.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING240292.Ava_1147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA20771; ABA20771; Ava_1147.
GeneID3683401.
KEGGava:Ava_1147.
PATRIC35422808. VBIAnaVar43351_1967.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
OMAVDYAHTG.
OrthoDBEOG6PKFCR.

Enzyme and pathway databases

BioCycAVAR240292:GCY3-1159-MONOMER.
UniPathwayUPA00219.

Family and domain databases

Gene3D3.40.1190.10. 1 hit.
3.40.1390.10. 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. SSF53244. 1 hit.
SSF53623. SSF53623. 1 hit.
SSF63418. SSF63418. 1 hit.
TIGRFAMsTIGR01085. murE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMURE_ANAVT
AccessionPrimary (citable) accession number: Q3ME15
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 25, 2005
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways