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228  structures 5869  species 4  interactions 11334  sequences 289  architectures

Family: Amidase_2 (PF01510)

Summary: N-acetylmuramoyl-L-alanine amidase

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This is the Wikipedia entry entitled "N-acetylmuramoyl-L-alanine amidase". More...

N-acetylmuramoyl-L-alanine amidase Edit Wikipedia article

N-acetylmuramoyl-L-alanine amidase
EC number
CAS number 9013-25-6
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
PDB 1sk4 EBI.jpg
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
Symbol Amidase_2
Pfam PF01510
InterPro IPR002502
SCOP 1lba
OPM superfamily 438
OPM protein 1sk4
PDB 1jwq EBI.jpg
structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus
Symbol Amidase_3
Pfam PF01520
Pfam clan CL0035
InterPro IPR002508
SCOP 1jwq
Symbol Amidase_5
Pfam PF05382
Pfam clan CL0125
InterPro IPR008044
Symbol Amidase02_C
Pfam PF12123
InterPro IPR021976

In enzymology, a N-acetylmuramoyl-L-alanine amidase (EC is an enzyme that catalyzes a chemical reaction that cleaves the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is peptidoglycan amidohydrolase. Other names in common use include acetylmuramyl-L-alanine amidase, N-acetylmuramyl-L-alanine amidase, N-acylmuramyl-L-alanine amidase, acetylmuramoyl-alanine amidase, N-acetylmuramic acid L-alanine amidase, acetylmuramyl-alanine amidase, N-acetylmuramylalanine amidase, N-acetylmuramoyl-L-alanine amidase type I, and N-acetylmuramoyl-L-alanine amidase type II. This enzyme participates in peptidoglycan biosynthesis. Autolysins and some phage lysins are examples of N-acetylmuramoyl-L-alanine amidases.

See also


  • Campbell JN; Dierickx, L; Coyette, J; Leyh-Bouille, M; Guinand, M; Campbell, JN (1969). "An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-l-alanine amidase active on bacterial wall peptidoglycans". Biochemistry. 8 (1): 213–22. doi:10.1021/bi00829a031. PMID 5777325. 
  • Herbold DR, Glaser L (1975). "Interaction of N-acetylmuramic acid L-alanine amidase with cell wall polymers". J. Biol. Chem. 250 (18): 7231–8. PMID 809432. 
  • Herbold DR, Glaser L (1975). "Bacillus subtilis N-acetylmuramic acid L-alanine amidase". J. Biol. Chem. 250 (5): 1676–82. PMID 803507. 
  • Ward JB, Curtis CA, Taylor C, Buxton RS (1982). "Purification and characterization of two phage PBSX-induced lytic enzymes of Bacillus subtilis 168: an N-acetylmuramoyl-L-alanine amidase and an N-acetylmuramidase". J. Gen. Microbiol. 128 (6): 1171–8. doi:10.1099/00221287-128-6-1171. PMID 6126517. 

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

N-acetylmuramoyl-L-alanine amidase Provide feedback

This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC: This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.

Literature references

  1. Potvin C, Leclerc D, Tremblay G, Asselin A, Bellemare G; , Mol Gen Genet 1988;214:241-248.: Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli. PUBMED:3070348 EPMC:3070348

  2. Wang X, Wilkinson BJ, Jayaswal RK; , Gene 1991;102:105-109.: Sequence analysis of a Staphylococcus aureus gene encoding a peptidoglycan hydrolase activity. PUBMED:1677905 EPMC:1677905

  3. Cheng X, Zhang X, Pflugrath JW, Studier FW; , Proc Natl Acad Sci U S A 1994;91:4034-4038.: The structure of bacteriophage T7 lysozyme, a zinc amidase and an inhibitor of T7 RNA polymerase. PUBMED:8171031 EPMC:8171031

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002502

Proteins containing this domain include zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The bacteriophage endolysins PLY118 and PLY500 cleave between L-Ala and D-Glu residues of Listeria cell-wall peptidoglycan and are therefore peptidases (MEROPS subfamily M15C) [PUBMED:8577256]. The structure is known for the Bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding [PUBMED:14506276, PUBMED:12845326, PUBMED:8171031, PUBMED:15223330, PUBMED:16556841, PUBMED:18304640, PUBMED:15140887, PUBMED:16103125, PUBMED:16428381].

Gene Ontology

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Domain organisation

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Seed source: Pfam-B_735 (release 4.0)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A
Number in seed: 623
Number in full: 11334
Average length of the domain: 137.30 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 43.38 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.1 21.1
Trusted cut-off 21.1 21.1
Noise cut-off 21.0 21.0
Model length: 126
Family (HMM) version: 25
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Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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There are 4 interactions for this family. More...

RNA_pol PG_binding_1 Amidase_2 RPOL_N


For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Amidase_2 domain has been found. There are 228 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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