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Q8FNT5 (MURE_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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:CE2058
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length526 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 – 526526UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase HAMAP MF_00208
PRO_0000101889

Regions

Nucleotide binding136 – 1427ATP Potential
Region178 – 1792UDP-MurNAc-L-Ala-D-Glu binding By similarity
Region432 – 4354Meso-diaminopimelate binding By similarity
Motif432 – 4354Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site481UDP-MurNAc-L-Ala-D-Glu; via carbonyl oxygen By similarity
Binding site501UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site2051UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site2131UDP-MurNAc-L-Ala-D-Glu By similarity
Binding site4081Meso-diaminopimelate By similarity
Binding site4901Meso-diaminopimelate; via carbonyl oxygen By similarity
Binding site4941Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue2451N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FNT5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 7C7C2B82CB11F577

FASTA52655,720
        10         20         30         40         50         60 
MCADTPHHPT PVHTEEAMAI TLGELARTIG GELFNAPDQD LEIHNIGLDS STLAKKAPIF 

        70         80         90        100        110        120 
AAVPGSRKHG AEFADTDRAA GALAVLTDRD GATILDRKGD TRPRLIVDDV REVLGVASSS 

       130        140        150        160        170        180 
VYGDPSRDLV LIGVTGTSGK TTTSYLLERG LMEAGYKVGL IGTTGTRIDG EPVPTKLTTP 

       190        200        210        220        230        240 
EAPTLQKLFY RMRQHGVTHV VMEVSSHALS LGRVSGSHFN VAAFTNLSQD HLDFHDTMEE 

       250        260        270        280        290        300 
YFDAKALFFR AGSPLAADHQ VVCIDDEWGT RMAEVAGNAQ TVATTGKRAD FTAGLVTVKE 

       310        320        330        340        350        360 
TGEQSFTVTV PDHGEVPVTL ALPGAFNVAN ATLALAAAVR AGVDPVAFAR GMAQVAVPGR 

       370        380        390        400        410        420 
MERIDEGQDF LAVVDYAHKP AAVAAVLDTL RTQIDGRLGV VIGAGGDRDA TKRAPMGELS 

       430        440        450        460        470        480 
ARRADLVIVT DDNPRSEVPA TIRAAVMEGA RRGAAEADHE VEVREIGDRA EAIRALIEWA 

       490        500        510        520 
GPGDGIVVAG KGHEVGQLIA GVTHHFDDRE QVREALRHTQ SDGEGK

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000035 Genomic DNA. Translation: BAC18868.1.
RefSeqNP_738668.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FNT5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1032069.
GenomeReviewsGene locus CE2058 in contig BA000035_GR.
KEGGcef:CE2058.
NMPDRfig|196164.1.peg.2058.
PATRIC21490251. VBICorEff9312_2040.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG602753.
OMAHTTPEST.
PhylomeDBQ8FNT5.
ProtClustDBPRK00139.

Enzyme and pathway databases

BioCycCEFF196164:CE2058-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_COREF
AccessionPrimary (citable) accession number: Q8FNT5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 63 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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