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Q31N55 (MURE_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 56. 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:Synpcc7942_1484
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus ›

Protein attributes

Sequence length497 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 – 497497UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP-Rule MF_00208
PRO_1000012398

Regions

Nucleotide binding119 – 1257ATP Potential
Region161 – 1622UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region414 – 4174Meso-diaminopimelate binding By similarity
Motif414 – 4174Meso-diaminopimelate recognition motif HAMAP-Rule MF_00208

Sites

Binding site331UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1881UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1941UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site1961UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site3901Meso-diaminopimelate By similarity
Binding site4651Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4691Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2281N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31N55 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 31F9BC731A0E73DB

FASTA49752,665
        10         20         30         40         50         60 
MNLRSLLAST PTQVLQPQHA ALDLAITGLQ TDSRRCQPGD LFLGMPGTQV DGGQFWPEAI 

        70         80         90        100        110        120 
AAGAVAVIVT PTALAQRPLS ANPEACLILS DQMPVTAGAI AAAFYNQPAQ TLKLIGVTGT 

       130        140        150        160        170        180 
NGKTTTTHLV EHFLNAADTK TALLGTLYNR WPGYSEVAQH TTPFATDLQA QLATAVDAGC 

       190        200        210        220        230        240 
QAAVMEVSSH ALDQGRVNGC GFDVAVFTNL TQDHLDYHGT MEAYFAAKAR LFAPPYLRGK 

       250        260        270        280        290        300 
AVINADDAYG QRLITMTPPG QCLTYSVVGT ADFCTTDLQY GPTGVEGTIK TPDGAFPFRS 

       310        320        330        340        350        360 
PLVGQFNLAN LLGAIAAGWT LGLPIETMLA VVPDFVGVPG RMERVVGQDS DPTVIVDYAH 

       370        380        390        400        410        420 
TPDSLENLLK AARPFIQGEL ICVFGCGGDR DRTKRPLMGE IAARLADRVI ITSDNPRTED 

       430        440        450        460        470        480 
PRQILADIVA GIPAASPVVV EADRAAAIRQ AILSAQPGDG VLLAGKGHED YQILGTTKIH 

       490 
FDDREQARLA LAERQSA

« Hide

References

[1]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000100 Genomic DNA. Translation: ABB57514.1.
RefSeqYP_400501.1. NC_007604.1.

3D structure databases

ProteinModelPortalQ31N55.
ModBaseSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_1484.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB57514; ABB57514; Synpcc7942_1484.
GeneID3773656.
KEGGsyf:Synpcc7942_1484.
PATRIC23788327. VBISynElo51371_1689.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHOG000268118.
KOK01928.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycSYNEL:SYNPCC7942_1484-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_SYNE7
AccessionPrimary (citable) accession number: Q31N55
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 6, 2005
Last modified: May 29, 2013
This is version 56 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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