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CAZyme Information: MGYG000000022_02471
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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 | Faecalibacterium prausnitzii_C | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_C | |||||||||||
| CAZyme ID | MGYG000000022_02471 | |||||||||||
| CAZy Family | GH73 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 47133; End: 48509 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GH73 | 255 | 387 | 2.7e-16 | 0.9609375 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd06583 | PGRP | 4.06e-13 | 53 | 187 | 1 | 123 | 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 | 8.22e-12 | 52 | 174 | 1 | 123 | Ami_2 domain. |
| COG5632 | CwlA | 1.37e-11 | 50 | 213 | 20 | 177 | N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis]. |
| pfam01510 | Amidase_2 | 1.05e-10 | 53 | 187 | 1 | 119 | 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. |
| pfam01832 | Glucosaminidase | 2.96e-09 | 255 | 333 | 1 | 81 | Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AUV61531.1 | 0.0 | 1 | 458 | 1 | 458 |
| ATP01236.1 | 1.80e-194 | 172 | 458 | 1 | 287 |
| QIA44356.1 | 1.80e-194 | 172 | 458 | 1 | 287 |
| AFB75852.1 | 3.21e-104 | 39 | 452 | 18 | 449 |
| ADY57245.1 | 1.53e-85 | 220 | 452 | 263 | 494 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3HMB_A | 2.54e-14 | 53 | 198 | 25 | 153 | 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 | 8.76e-14 | 57 | 198 | 29 | 153 | 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 |
|---|---|---|---|---|---|---|
| O51481 | 1.47e-20 | 244 | 353 | 61 | 168 | Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1 |
| P54450 | 1.14e-14 | 57 | 203 | 26 | 156 | N-acetylmuramoyl-L-alanine amidase CwlH OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlH PE=1 SV=1 |
| P39800 | 1.89e-12 | 57 | 215 | 26 | 160 | N-acetylmuramoyl-L-alanine amidase XlyA OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyA PE=1 SV=1 |
| P36550 | 7.25e-06 | 35 | 339 | 8 | 319 | N-acetylmuramoyl-L-alanine amidase CwlL OS=Bacillus licheniformis OX=1402 GN=cwlL 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 |
|---|---|---|---|---|---|
| 1.000060 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |