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Q8YWF0 (MURE_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 65. 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:all1663
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Nostocales › Nostocaceae › Nostoc

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 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 – 496496UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101861

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 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
Q8YWF0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: C5ED7B9D786A5B90

FASTA49653,474
        10         20         30         40         50         60 
MKLRELLATV DSVENLPPVL ADAEVKGIKT NSHACGAGDL FIGMPGTRVD GGEFWPSAIA 

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

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

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

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

       310        320        330        340        350        360 
VGQYNLENLL AAVGAVLHLG LNLQLIANAI PEFPGVPGRM ERVQINPDQD ISVIVDYAHT 

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

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

       490 
DDREHARAAL TEREKL

« Hide

References

[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed: 11759840] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000019 Genomic DNA. Translation: BAB78029.1.
PIRAI2013.
RefSeqNP_485703.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YWF0.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8YWF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1105255.
GenomeReviewsGene locus all1663 in contig BA000019_GR.
KEGGana:all1663.
NMPDRfig|103690.1.peg.1970.
PATRIC22773372. VBINosSp37423_2165.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0769.
HOGENOMHBG602753.
OMAHTTPEST.
PhylomeDBQ8YWF0.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycNSP103690:ALL1663-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_NOSS1
AccessionPrimary (citable) accession number: Q8YWF0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: January 25, 2012
This is version 65 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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