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CAZyme Information: MGYG000000012_00462
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Bacillus subtilis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus subtilis | |||||||||||
| CAZyme ID | MGYG000000012_00462 | |||||||||||
| CAZy Family | CBM50 | |||||||||||
| CAZyme Description | N-acetylmuramoyl-L-alanine amidase CwlA | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 424680; End: 425633 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG5632 | CwlA | 2.27e-71 | 3 | 177 | 2 | 188 | N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis]. |
| cd06583 | PGRP | 1.31e-26 | 24 | 143 | 1 | 125 | Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity. |
| smart00644 | Ami_2 | 1.47e-26 | 26 | 141 | 4 | 126 | Ami_2 domain. |
| pfam01510 | Amidase_2 | 4.87e-25 | 26 | 143 | 3 | 121 | N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. 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. |
| pfam01471 | PG_binding_1 | 2.29e-17 | 251 | 313 | 1 | 57 | Putative peptidoglycan binding domain. This domain is composed of three alpha helices. This domain is found at the N or C-terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QRZ94235.1 | 1.94e-220 | 1 | 317 | 1 | 317 |
| AFI27897.1 | 3.22e-219 | 1 | 317 | 1 | 317 |
| AUS13475.1 | 9.24e-219 | 1 | 317 | 1 | 317 |
| ASB60518.1 | 9.24e-219 | 1 | 317 | 1 | 317 |
| AUZ38201.1 | 2.65e-218 | 1 | 317 | 1 | 317 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2L47_A | 1.01e-61 | 5 | 165 | 3 | 159 | Solutionstructure of the PlyG catalytic domain [Bacillus phage Gamma] |
| 1YB0_A | 1.90e-60 | 5 | 165 | 3 | 159 | Structureof PlyL [Bacillus anthracis],1YB0_B Structure of PlyL [Bacillus anthracis],1YB0_C Structure of PlyL [Bacillus anthracis] |
| 2AR3_A | 1.57e-59 | 5 | 165 | 3 | 159 | ChainA, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_B Chain B, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_C Chain C, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis] |
| 3HMB_A | 1.18e-31 | 22 | 157 | 23 | 156 | ChainA, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_B Chain B, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_C Chain C, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis] |
| 3RDR_A | 6.83e-30 | 22 | 157 | 23 | 156 | Structureof the catalytic domain of XlyA [Bacillus subtilis] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O34391 | 3.28e-213 | 1 | 317 | 1 | 317 | N-acetylmuramoyl-L-alanine amidase XlyB OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyB PE=3 SV=1 |
| P24808 | 2.01e-129 | 1 | 317 | 1 | 271 | N-acetylmuramoyl-L-alanine amidase CwlA OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlA PE=1 SV=1 |
| P39800 | 1.10e-74 | 22 | 301 | 20 | 280 | N-acetylmuramoyl-L-alanine amidase XlyA OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyA PE=1 SV=1 |
| P54450 | 1.59e-62 | 22 | 317 | 20 | 249 | N-acetylmuramoyl-L-alanine amidase CwlH OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlH PE=1 SV=1 |
| P14892 | 3.61e-52 | 5 | 149 | 3 | 147 | N-acetylmuramoyl-L-alanine amidase CwlA OS=Bacillus sp. OX=1409 GN=cwlA PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000065 | 0.000004 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |