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 | |||||||||
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| Identifiers | |||||||||
| EC number | 3.5.1.28 | ||||||||
| CAS number | 9013-25-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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| Amidase_2 | |||||||||
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crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha |
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| Identifiers | |||||||||
| Symbol | Amidase_2 | ||||||||
| Pfam | PF01510 | ||||||||
| InterPro | IPR002502 | ||||||||
| SCOP | 1lba | ||||||||
| SUPERFAMILY | 1lba | ||||||||
| OPM superfamily | 438 | ||||||||
| OPM protein | 1sk4 | ||||||||
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| Amidase_3 | |||||||||
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structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus |
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| Identifiers | |||||||||
| Symbol | Amidase_3 | ||||||||
| Pfam | PF01520 | ||||||||
| Pfam clan | CL0035 | ||||||||
| InterPro | IPR002508 | ||||||||
| SCOP | 1jwq | ||||||||
| SUPERFAMILY | 1jwq | ||||||||
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| Amidase_5 | |||||||||
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| Identifiers | |||||||||
| Symbol | Amidase_5 | ||||||||
| Pfam | PF05382 | ||||||||
| Pfam clan | CL0125 | ||||||||
| InterPro | IPR008044 | ||||||||
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| Amidase02_C | |||||||||
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| Identifiers | |||||||||
| Symbol | Amidase02_C | ||||||||
| Pfam | PF12123 | ||||||||
| InterPro | IPR021976 | ||||||||
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In enzymology, a N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) 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.
[edit] See also
[edit] References
- 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): 213â22. 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): 7231â8. PMID 809432.
- Herbold DR, Glaser L (1975). "Bacillus subtilis N-acetylmuramic acid L-alanine amidase". J. Biol. Chem. 250 (5): 1676â82. 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): 1171â8. 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.
Literature references
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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
| Similarity to PfamA using HHSearch: | SpoIIP |
External database links
| PANDIT: | PF01520 |
| Pseudofam: | PF01520 |
| SCOP: | 1jwq |
| SYSTERS: | Amidase_3 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR002508
The cell wall envelope of Gram-positive bacteria is a macromolecular, exoskeletal organelle that is assembled and turned over at designated sites. The cell wall also functions as a surface organelle that allows Gram-positive pathogens to interact with their environment, in particular the tissues of the infected host. All of these functions require that surface proteins and enzymes be properly targeted to the cell wall envelope. Two basic mechanisms, cell wall sorting and targeting, have been identified. Cell well sorting is the covalent attachment of surface proteins to the peptidoglycan via a C-terminal sorting signal that contains a consensus LPXTG sequence. More than 100 proteins that possess cell wall-sorting signals, including the M proteins of Streptococcus pyogenes, protein A of Staphylococcus aureus, and several internalins of Listeria monocytogenes, have been identified. Cell wall targeting involves the noncovalent attachment of proteins to the cell surface via specialised binding domains. Several of these wall-binding domains appear to interact with secondary wall polymers that are associated with the peptidoglycan, for example teichoic acids and polysaccharides. Proteins that are targeted to the cell surface include muralytic enzymes such as autolysins, lysostaphin, and phage lytic enzymes. Other examples for targeted proteins are the surface S-layer proteins of bacilli and clostridia, as well as virulence factors required for the pathogenesis of L. monocytogenes (internalin B) and Streptococcus pneumoniae (PspA) infections [PUBMED:10066836].
Autolysin EC hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain bacterial cell wall glycopeptides.
Gene Ontology
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) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Peptidase_MH (CL0035), which contains the following 12 members:
Amidase_3 AstE_AspA DUF2172 DUF2817 Nicastrin Peptidase_M14 Peptidase_M17 Peptidase_M18 Peptidase_M20 Peptidase_M28 Peptidase_M42 SpoIIPAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (103) |
Full (7380) |
Representative proteomes | NCBI (5592) |
Meta (1358) |
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| RP15 (519) |
RP35 (1014) |
RP55 (1265) |
RP75 (1463) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (103) |
Full (7380) |
Representative proteomes | NCBI (5592) |
Meta (1358) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (519) |
RP35 (1014) |
RP55 (1265) |
RP75 (1463) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_888 (release 4.0) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A |
| Number in seed: | 103 |
| Number in full: | 7380 |
| Average length of the domain: | 194.90 aa |
| Average identity of full alignment: | 29 % |
| Average coverage of the sequence by the domain: | 50.10 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 175 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Structures
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 11 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 seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence