Summary: Bacteriophage peptidoglycan hydrolase
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| 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 | ||||||||
|
|||||||||
| Amidase_2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
crystal structure of the c-terminal peptidoglycan-binding domain of human peptidoglycan recognition protein ialpha |
|||||||||
| Identifiers | |||||||||
| Symbol | Amidase_2 | ||||||||
| Pfam | PF01510 | ||||||||
| InterPro | IPR002502 | ||||||||
| SCOP | 1lba | ||||||||
| SUPERFAMILY | 1lba | ||||||||
| OPM superfamily | 438 | ||||||||
| OPM protein | 1sk4 | ||||||||
|
|||||||||
| Amidase_3 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
structure of the catalytic domain of cwlv, n-acetylmuramoyl-l-alanine amidase from bacillus(paenibacillus) polymyxa var.colistinus |
|||||||||
| Identifiers | |||||||||
| Symbol | Amidase_3 | ||||||||
| Pfam | PF01520 | ||||||||
| Pfam clan | CL0035 | ||||||||
| InterPro | IPR002508 | ||||||||
| SCOP | 1jwq | ||||||||
| SUPERFAMILY | 1jwq | ||||||||
|
|||||||||
| Amidase_5 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Amidase_5 | ||||||||
| Pfam | PF05382 | ||||||||
| Pfam clan | CL0125 | ||||||||
| InterPro | IPR008044 | ||||||||
|
|||||||||
| Amidase02_C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Amidase02_C | ||||||||
| Pfam | PF12123 | ||||||||
| InterPro | IPR021976 | ||||||||
|
|||||||||
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.
| This hydrolase article is a stub. You can help Wikipedia by expanding it. |
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
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.
Bacteriophage peptidoglycan hydrolase Provide feedback
At least one of the members of this family, the Pal protein from the pneumococcal bacteriophage Dp-1 O03979 has been shown to be a N-acetylmuramoyl-L-alanine amidase [1]. According to the known modular structure of this and other peptidoglycan hydrolases from the pneumococcal system, the active site should reside at the N-terminal domain whereas the C-terminal domain binds to the choline residues of the cell wall teichoic acids [2,3]. This family appears to be related to PF00877.
Literature references
-
Garcia P, Mendez E, Garcia E, Ronda C, Lopez R; , J Bacteriol 1984;159:793-796.: Biochemical characterization of a murein hydrolase induced by bacteriophage Dp-1 in Streptococcus pneumoniae: comparative study between bacteriophage-associated lysin and the host amidase. PUBMED:6146601 EPMC:6146601
-
Sheehan MM, Garcia JL, Lopez R, Garcia P; , Mol Microbiol 1997;25:717-725.: The lytic enzyme of the pneumococcal phage Dp-1: a chimeric lysin of intergeneric origin. PUBMED:9379901 EPMC:9379901
-
Garcia E, Garcia JL, Garcia P, Arraras A, Sanchez-Puelles JM, Lopez R; , Proc Natl Acad Sci U S A 1988;85:914-918.: Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. PUBMED:3422470 EPMC:3422470
External database links
| PANDIT: | PF05382 |
| Pseudofam: | PF05382 |
| SYSTERS: | Amidase_5 |
This tab holds annotation information from the InterPro database.
InterPro entry IPR008044
This entry is represented by Bacteriophage SFi21, lysin (Cell wall hydrolase; EC). At least one of proteins in this entry, the Pal protein from the pneumococcal bacteriophage Dp-1 (SWISSPROT) has been shown to be an N-acetylmuramoyl-L-alanine amidase [PUBMED:6146601]. According to the known modular structure of this and other peptidoglycan hydrolases from the pneumococcal system, the active site should reside within this domain while a C-terminal domain binds to the choline residues of the cell wall teichoic acids [PUBMED:9379901, PUBMED:3422470].
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Pfam Clan
This family is a member of clan Peptidase_CA (CL0125), which contains the following 60 members:
Acetyltransf_2 Amidase_5 Amidase_6 CHAP DUF1175 DUF1287 DUF1460 DUF2272 DUF3335 DUF553 DUF830 EDR1 Guanylate_cyc_2 LRAT NLPC_P60 OTU Peptidase_C1 Peptidase_C10 Peptidase_C12 Peptidase_C16 Peptidase_C1_2 Peptidase_C2 Peptidase_C21 Peptidase_C23 Peptidase_C27 Peptidase_C28 Peptidase_C31 Peptidase_C32 Peptidase_C33 Peptidase_C34 Peptidase_C36 Peptidase_C39 Peptidase_C39_2 Peptidase_C42 Peptidase_C47 Peptidase_C48 Peptidase_C5 Peptidase_C54 Peptidase_C58 Peptidase_C6 Peptidase_C65 Peptidase_C7 Peptidase_C70 Peptidase_C71 Peptidase_C78 Peptidase_C8 Peptidase_C9 Peptidase_C93 Peptidase_C98 Phytochelatin Rad4 Transglut_core Transglut_core2 Transglut_core3 Transglut_i_TM Transpep_BrtH UCH UCH_1 Viral_protease YopJAlignments
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...
View options
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 (8) |
Full (235) |
Representative proteomes | NCBI (361) |
Meta (31) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (13) |
RP35 (19) |
RP55 (26) |
RP75 (32) |
|||||
| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
Download options
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 (8) |
Full (235) |
Representative proteomes | NCBI (361) |
Meta (31) |
||||
|---|---|---|---|---|---|---|---|---|
| RP15 (13) |
RP35 (19) |
RP55 (26) |
RP75 (32) |
|||||
| 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_6845 (Pfam7.8) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Studholme DJ, Garcia E |
| Number in seed: | 8 |
| Number in full: | 235 |
| Average length of the domain: | 134.80 aa |
| Average identity of full alignment: | 28 % |
| Average coverage of the sequence by the domain: | 32.91 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
| Model details: |
|
||||||||||||
| Model length: | 145 | ||||||||||||
| Family (HMM) version: | 8 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.

Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence