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CAZyme Information: MGYG000003684_05523

You are here: Home > Sequence: MGYG000003684_05523

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 Eisenbergiella massiliensis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella massiliensis
CAZyme ID MGYG000003684_05523
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
401 MGYG000003684_38|CGC1 42933.35 5.6534
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003684 6691925 Isolate China Asia
Gene Location Start: 43370;  End: 44575  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003684_05523.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 205 350 1.8e-22 0.9609375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 1.83e-37 2 176 1 172
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) 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. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. 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. 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. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
COG1705 FlgJ 2.72e-37 181 360 30 194
Flagellum-specific peptidoglycan hydrolase FlgJ [Cell wall/membrane/envelope biogenesis, Cell motility].
pfam01520 Amidase_3 8.77e-26 6 175 7 172
N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
NF038016 sporang_Gsm 6.12e-22 184 354 150 312
sporangiospore maturation cell wall hydrolase GsmA. The peptidoglycan-hydrolyzing enzyme GsmA occurs in some sporangia-forming members of the Actinobacteria, such as Actinoplanes missouriensis, and is required for proper separation of spores. GsmA proteins have one or two SH3 domains N-terminal to the hydrolase domain.
PRK06347 PRK06347 5.40e-21 195 354 151 303
1,4-beta-N-acetylmuramoylhydrolase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QBF75599.1 1.58e-60 192 390 1 198
ADB89215.1 5.97e-56 182 354 198 372
CBL18646.1 8.91e-54 192 354 201 365
AMP42248.1 5.70e-52 190 361 207 381
QQQ98955.1 1.28e-51 186 369 205 389

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3VWO_A 3.82e-09 195 345 2 143
Crystalstructure of peptidoglycan hydrolase mutant from Sphingomonas sp. A1 [Sphingomonas sp. A1]
2ZYC_A 4.50e-09 195 345 3 144
ChainA, Peptidoglycan hydrolase FlgJ [Sphingomonas sp. A1]
3QAY_A 5.34e-09 1 158 2 154
ChainA, Endolysin [Clostridium virus phiCD27],3QAY_B Chain B, Endolysin [Clostridium virus phiCD27],3QAY_C Chain C, Endolysin [Clostridium virus phiCD27],3QAY_D Chain D, Endolysin [Clostridium virus phiCD27]
3K3T_A 2.81e-08 195 345 3 144
E185Amutant of peptidoglycan hydrolase from Sphingomonas sp. A1 [Sphingomonas sp. A1]
5T1Q_A 8.05e-08 196 361 62 218
ChainA, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_B Chain B, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_C Chain C, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325],5T1Q_D Chain D, N-acetylmuramoyl-L-alanine amidase domain-containing protein SAOUHSC_02979 [Staphylococcus aureus subsp. aureus NCTC 8325]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P58698 2.05e-18 1 163 1 158
Uncharacterized protein CPE1502 OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=CPE1502 PE=4 SV=1
O32083 9.83e-15 214 357 68 201
Exo-glucosaminidase LytG OS=Bacillus subtilis (strain 168) OX=224308 GN=lytG PE=1 SV=1
P18020 1.02e-14 1 163 1 158
Uncharacterized 38.4 kDa protein OS=Clostridium perfringens OX=1502 PE=4 SV=1
P0C2T5 5.53e-08 181 357 49 217
Probable N-acetylmuramidase OS=Lactococcus lactis subsp. cremoris OX=1359 GN=acmA PE=3 SV=1
Q9CIT4 5.55e-08 181 357 49 217
Probable N-acetylmuramidase OS=Lactococcus lactis subsp. lactis (strain IL1403) OX=272623 GN=acmA 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
1.000078 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003684_05523.