UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase

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Q8XJ99 (MURE_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. 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--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:	CPE1862

Organism

Clostridium perfringens [Complete proteome] [HAMAP]

Taxonomic identifier

1502 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

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
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-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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 – 484

484

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

PRO_0000101887

Regions

Nucleotide binding

110 – 116

ATP Potential

Region

152 – 153

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

Region

405 – 408

Meso-diaminopimelate binding By similarity

Motif

405 – 408

Meso-diaminopimelate recognition motif HAMAP MF_00208

Sites

Binding site

179

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

Binding site

187

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

Binding site

381

Meso-diaminopimelate By similarity

Binding site

455

Meso-diaminopimelate; via carbonyl oxygen By similarity

Binding site

459

Meso-diaminopimelate By similarity

Amino acid modifications

Modified residue

219

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8XJ99 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: CDB169DF3B903EB2
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FASTA

484

54,471

        10         20         30         40         50         60 
MILKSLLKGL DYEVIKGNEE SKVQNIRYDN RKIEQGDAFV CVKGFKVDGH SFIGDAIKKG 

        70         80         90        100        110        120 
AKTLIVQEDV SVQEDITIIK VRDTRKALAI MSSNYFGNPK DKLKIIGITG TNGKTTSAFI 

       130        140        150        160        170        180 
IKSILEKAGF MTGLIGTIAN YIGNKKVDAV RTTPESYELH ELFKNMVDAG VEYCVMEVSS 

       190        200        210        220        230        240 
HSLELDRVYG IQFEEGIFTN LTRDHLDFHK TFENYYNAKF KLFERSNHSI INLDDPYGAN 

       250        260        270        280        290        300 
IVKDIEERGV KTKVSTFSIE KESDFKAFEI KSHSNGSEFK VNLEGIEEFS INIPGEYNIY 

       310        320        330        340        350        360 
NSLGCIICAY NLNIPMDKIK EGLSDVVIPG RCELVAKEKN LPYSIIIDYA HTPDGLENIL 

       370        380        390        400        410        420 
STVKAFTKNR MISVFGCGGD RDKVKRPQMG KIGCELSDIA IITSDNPRSE EPMDIINDIV 

       430        440        450        460        470        480 
KPLNYDNFVI EVNRKEAIRK AMNMALEGDV IVIAGKGHET YQILKDETIH FDEREVVYDI 


LEGK

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References

[1]	"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater." Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H. Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed: 11792842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 13 / Type A.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000016 Genomic DNA. Translation: BAB81568.1.
RefSeq	NP_562778.1. NC_003366.1.
3D structure databases
ProteinModelPortal	Q8XJ99.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	990171.
GenomeReviews	Gene locus CPE1862 in contig BA000016_GR.
KEGG	cpe:CPE1862.
NMPDR	fig\|195102.1.peg.1925.
PATRIC	19497679. VBICloPer59675_1935.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG602753.
OMA	IGTIANY.
PhylomeDB	Q8XJ99.
ProtClustDB	PRK00139.
Enzyme and pathway databases
BioCyc	CPER195102:CPE1862-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_CLOPE

Accession

Primary (citable) accession number: Q8XJ99

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	March 1, 2002
Last modified:	January 25, 2012
This is version 67 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

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents