UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase

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Q9WY79 (MURE_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase
EC=6.3.2.37
EC=6.3.2.7

Alternative name(s):
D-lysine-adding enzyme
L-lysine-adding enzyme
UDP-MurNAc-L-Ala-D-Glu:LD-Lys ligase
UDP-MurNAc-tripeptide synthetase
UDP-N-acetylmuramyl-tripeptide synthetase

Gene names

Name:	murE
Ordered Locus Names:	TM_0237

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the addition of both L- and D-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use meso-diaminopimelate as the amino acid substrate in vitro, although much less efficiently. Ref.2
Catalytic activity	ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysine. HAMAP MF_00208 ATP + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate + D-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-D-lysine.
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
Miscellaneous	The peptidoglycan of T.maritima was shown to contain approximate amounts of both enantiomers of lysine and no diaminopimelate. HAMAP MF_00208
Sequence similarities	Belongs to the MurCDEF family. MurE subfamily.
Biophysicochemical properties	Kinetic parameters: The catalytic efficiency for the L-lysine adding activity is 4-fold and 10-fold higher than that for the D-lysine and meso-diaminopimelate adding activity, respectively. K_M=0.45 mM for UDP-N-acetylmuramoyl-L-Ala-D-Glu Ref.2 K_M=2.8 mM for L-lysine (at pH 9.4) K_M=0.65 mM for L-lysine (at pH 8) K_M=1.7 mM for D-lysine (at pH 9.4) K_M=1.0 mM for D-lysine (at pH 8) K_M=4.8 mM for meso-diaminopimelate (at pH 9.4) K_M=27 mM for L-ornithine (at pH 9.4) K_M=3.6 mM for ATP pH dependence: Optimum pH is 9.4 for the L-lysine adding activity. Temperature dependence: Optimum temperature is 68 degrees Celsius for the L-lysine adding activity.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity Inferred from electronic annotation. Source: EC tetrahydrofolylpolyglutamate synthase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 490

490

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase HAMAP MF_00208

PRO_0000101962

Regions

Nucleotide binding

110 – 116

ATP Potential

Region

152 – 153

UDP-MurNAc-L-Ala-D-Glu binding By similarity

Sites

Binding site

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

179

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

185

UDP-MurNAc-L-Ala-D-Glu By similarity

Binding site

187

UDP-MurNAc-L-Ala-D-Glu By similarity

Amino acid modifications

Modified residue

219

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WY79 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 21A6FBE388D741A9
Show »

FASTA

490

54,740

        10         20         30         40         50         60 
MNISTIVSNL KDLILEVRAP YDLEITGVSN HSSKVKKGDL FICRRGEKFD SHEIIPEVME 

        70         80         90        100        110        120 
KGAVAVVVER EIDLDFPYIQ VFDSRYFEAK VASLFFEDPW KDVLTFGVTG TNGKTTTTMM 

       130        140        150        160        170        180 
IYHMLTSLGE RGSVLTTAVK RILGNSYYDD ITTPDAITIL SAMKENREGG GKFFALEVSS 

       190        200        210        220        230        240 
HALVQQRVEG VRFDVGIFTN ISRDHLDFHG TFENYLKAKL HLFDLLKDDG VAVLNESLAD 

       250        260        270        280        290        300 
AFNRKSRKIT FGTSKNADYR LGNIEVSWEG TQFVLETPDG LLKVFTRAIG DFNAYNAAAA 

       310        320        330        340        350        360 
IAALHQLGYD PKDLASSLET FTGVEGRFEV VRGAKKIGLN VVVDFAHSPD ALEKLLKNVR 

       370        380        390        400        410        420 
KISQGRVIVV FGAGGNSDRG KRPMMSEVAS KLADVVILTT DDPRGEDPEQ IMEDLIKGID 

       430        440        450        460        470        480 
KRKPYLVLFD RREAIETALT IANRGDSVVI AGRGHERYQI IDEEKKVPFQ DREVVEEIIR 

       490 
DKLKGRKYAQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity." Boniface A., Bouhss A., Mengin-Lecreulx D., Blanot D. J. Biol. Chem. 281:15680-15686(2006) [PubMed: 16595662] [Abstract] Cited for: FUNCTION, CHARACTERIZATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000512 Genomic DNA. Translation: AAD35328.1.
PIR	G72402.
RefSeq	NP_228051.1. NC_000853.1.
3D structure databases
ProteinModelPortal	Q9WY79.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	897137.
GenomeReviews	Gene locus TM_0237 in contig AE000512_GR.
KEGG	tma:TM0237.
NMPDR	fig\|243274.1.peg.235.
PATRIC	23935349. VBITheMar51294_0240.
TIGR	TM_0237.
Phylogenomic databases
HOGENOM	HBG602753.
OMA	HTTPEST.
PhylomeDB	Q9WY79.
ProtClustDB	CLSK875045.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-16146. TMAR243274:TM_0237-MONOMER.
Family and domain databases
HAMAP	MF_00208. MurE. [Tree]
InterPro	IPR018109. Folylpolyglutamate_synth_CS. IPR004101. Mur_ligase_C. IPR013221. Mur_ligase_cen. IPR000713. Mur_ligase_N. IPR005761. UDP-N-AcMur-Glu-dNH2Pim_ligase. [Graphical view]
Gene3D	G3DSA:3.90.190.20. Mur_ligase_C. 1 hit. G3DSA:3.40.1190.10. Mur_ligase_cen. 1 hit.
KO	K01928.
Pfam	PF01225. Mur_ligase. 1 hit. PF02875. Mur_ligase_C. 1 hit. PF08245. Mur_ligase_M. 1 hit. [Graphical view]
SUPFAM	SSF53244. Mur_ligase_C. 1 hit. SSF53623. Mur_ligase_cen. 1 hit.
TIGRFAMs	TIGR01085. MurE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURE_THEMA

Accession

Primary (citable) accession number: Q9WY79

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents