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CAZyme Information: MGYG000002396_00109

You are here: Home > Sequence: MGYG000002396_00109

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 Bifidobacterium bifidum
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium bifidum
CAZyme ID MGYG000002396_00109
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
863 92246.44 5.4325
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002396 2311342 Isolate South Korea Asia
Gene Location Start: 135046;  End: 137637  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002396_00109.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 193 379 6.7e-37 0.9943502824858758
CBM13 660 817 1.4e-26 0.6914893617021277
CBM13 516 654 3.5e-26 0.6648936170212766
CBM13 431 579 6.7e-23 0.7446808510638298

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 5.79e-69 190 388 1 190
The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599 GH25_muramidase 1.68e-28 192 388 2 186
Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
pfam14200 RicinB_lectin_2 2.46e-24 762 851 1 89
Ricin-type beta-trefoil lectin domain-like.
cd06523 GH25_PlyB-like 9.26e-24 192 387 2 176
PlyB is a bacteriophage endolysin that displays potent lytic activity toward Bacillus anthracis. PlyB has an N-terminal glycosyl hydrolase family 25 (GH25) catalytic domain and a C-terminal bacterial SH3-like domain, SH3b. Both domains are required for effective catalytic activity. Endolysins are produced by bacteriophages at the end of their life cycle and participate in lysing the bacterial cell in order to release the newly formed progeny. Endolysins (also referred to as endo-N-acetylmuramidases or peptidoglycan hydrolases) degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
pfam14200 RicinB_lectin_2 7.77e-23 601 699 1 89
Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AXM90834.1 0.0 1 834 1 834
ALE10489.1 0.0 1 832 1 836
VEG16747.1 0.0 1 832 1 836
ADP35190.1 0.0 1 832 1 836
QGM63437.1 0.0 1 834 1 838

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2WW5_A 1.16e-38 160 388 238 467
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae at 1.6 A resolution [Streptococcus pneumoniae R6],2WWD_A 3D-structure of the modular autolysin LytC from Streptococcus pneumoniae in complex with pneummococcal peptidoglycan fragment [Streptococcus pneumoniae R6]
2WWC_A 2.85e-38 160 388 238 467
3D-structureof the modular autolysin LytC from Streptococcus pneumoniae in complex with synthetic peptidoglycan ligand [Streptococcus pneumoniae R6]
4KRT_A 6.47e-11 193 444 23 253
X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRU_A 1.36e-10 193 400 23 219
X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
3HMC_A 4.47e-10 192 391 7 183
Endolysinfrom Bacillus anthracis [Bacillus anthracis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26836 5.82e-11 193 428 12 226
Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8X7H0 3.54e-06 193 412 70 271
Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P25310 7.37e-06 193 388 85 279
Lysozyme M1 OS=Streptomyces globisporus OX=1908 GN=acm PE=1 SV=1
P34020 8.70e-06 193 396 4 188
Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000329 0.998895 0.000223 0.000198 0.000182 0.000159

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002396_00109.