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CAZyme Information: MGYG000000837_01350

You are here: Home > Sequence: MGYG000000837_01350

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 Dysosmobacter sp900544105
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Dysosmobacter; Dysosmobacter sp900544105
CAZyme ID MGYG000000837_01350
CAZy Family GH25
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
539 59545.61 4.4708
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000837 2171635 MAG China Asia
Gene Location Start: 4940;  End: 6559  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000837_01350.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH25 339 526 5.4e-40 0.9943502824858758

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06414 GH25_LytC-like 9.05e-71 338 536 3 191
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 3.31e-28 337 534 1 185
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.
pfam01183 Glyco_hydro_25 5.91e-19 339 526 1 180
Glycosyl hydrolases family 25.
COG3757 Acm 1.95e-18 338 533 65 251
Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].
cd06415 GH25_Cpl1-like 2.49e-18 337 532 2 195
Cpl-1 lysin (also known as Cpl-9 lysozyme / muramidase) is a bacterial cell wall endolysin encoded by the pneumococcal bacteriophage Cp-1, which cleaves the glycosidic N-acetylmuramoyl-(beta1,4)-N-acetylglucosamine bonds of the pneumococcal glycan chain, thus acting as an enzymatic antimicrobial agent (an enzybiotic) against streptococcal infections. Cpl-1 belongs to the CP family of lysozymes (CPL lysozymes) which includes the Cpl-7 lysin. Cpl-1 has a glycosyl hydrolase family 25 (GH25) catalytic domain with an irregular (beta/alpha)5-beta3 barrel and a C-terminal cell wall-anchoring module formed by six similar choline-binding repeats (ChBr's). The ChBr's facilitate the anchoring of Cpl-1 to the choline-containing teichoic acid of the pneumococcal cell wall. Other members of this domain family have an N-terminal CHAP (cysteine, histidine-dependent amidohydrolases/peptidases) domain similar to that of the firmicute CHAP lysins and associated with endopeptidase activity. The Cpl-7 lysin is also included here as is LysB of Lactococcus phage, and the Mur lysin of Lactobacillus phage.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCI60549.1 3.68e-231 2 539 4 546
BCK85948.1 1.72e-230 8 539 9 550
QUO37824.1 3.58e-222 9 536 10 556
BAK99312.1 5.68e-193 4 537 3 542
QNL45744.1 1.18e-169 12 539 15 545

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1JFX_A 4.00e-06 338 533 7 200
Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P38536 1.48e-11 26 195 1682 1856
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P38535 8.19e-10 26 195 908 1082
Exoglucanase XynX OS=Acetivibrio thermocellus OX=1515 GN=xynX PE=3 SV=1
Q06852 2.16e-09 22 142 2141 2273
Cell surface glycoprotein 1 OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=olpB PE=3 SV=2
P38537 1.74e-08 9 195 19 207
Surface-layer 125 kDa protein OS=Lysinibacillus sphaericus OX=1421 PE=3 SV=1
Q06848 4.22e-08 30 146 290 412
Cellulosome-anchoring protein OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=ancA 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
0.000582 0.928269 0.070279 0.000356 0.000266 0.000223

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000837_01350.