Summary: N-acetylmuramoyl-L-alanine amidase
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N-acetylmuramoyl-L-alanine amidase Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / QuickGO|
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha
|SCOPe||1lba / SUPFAM|
structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus
|SCOPe||1jwq / SUPFAM|
In enzymology, a N-acetylmuramoyl-L-alanine amidase (EC 22.214.171.124) 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.
- 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): 213â€“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): 7231â€“8. PMID 809432.
- Herbold DR, Glaser L (1975). "Bacillus subtilis N-acetylmuramic acid L-alanine amidase". J. Biol. Chem. 250 (5): 1676â€“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): 1171â€“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 enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
Kuroda A, Sugimoto Y, Funahashi T, Sekiguchi J; , Mol Gen Genet 1992;234:129-137.: Genetic structure, isolation and characterization of a Bacillus licheniformis cell wall hydrolase. PUBMED:1495475 EPMC:1495475
Internal database links
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002508
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination.
In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division [ PUBMED:16855223 ]. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins [ PUBMED:18266855 ].
The amidase catalytic module is fused to another functional module (cell wall binding module) either at the N or C terminus, which is responsible for high affinity binding of the protein to the cell wall [ PUBMED:23927005 ].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||N-acetylmuramoyl-L-alanine amidase activity (GO:0008745)|
|Biological process||peptidoglycan catabolic process (GO:0009253)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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This clan contains peptidases belonging to MEROPS clan MH, MC and MF. We also include Nicastrin that is part of the gamma secretase complex and not known to be a peptidase.
The clan contains the following 17 members:Amidase_3 AstE_AspA DUF2817 DUF4910 FGase Gamma_PGA_hydro Glycolytic Ncstrn_small Nicastrin Peptidase_M14 Peptidase_M17 Peptidase_M18 Peptidase_M20 Peptidase_M28 Peptidase_M42 Peptidase_M99 SpoIIP
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Seed source:||Pfam-B_888 (release 4.0)|
|Number in seed:||62|
|Number in full:||13527|
|Average length of the domain:||192.40 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||50.90 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||21|
|Download:||download the raw HMM for this family|
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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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_3 domain has been found. There are 27 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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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.
|Protein||Predicted structure||External Information|
|I6Y4D2||View 3D Structure||Click here|
|L7N653||View 3D Structure||Click here|
|P26365||View 3D Structure||Click here|
|P36548||View 3D Structure||Click here|
|P63883||View 3D Structure||Click here|
|Q2FXU3||View 3D Structure||Click here|
|Q2FYD8||View 3D Structure||Click here|