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CAZyme Information: MGYG000003406_01168

You are here: Home > Sequence: MGYG000003406_01168

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 Veillonella sp009929605
Lineage Bacteria; Firmicutes_C; Negativicutes; Veillonellales; Veillonellaceae; Veillonella; Veillonella sp009929605
CAZyme ID MGYG000003406_01168
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
557 62459.43 7.1409
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003406 1742690 MAG United States North America
Gene Location Start: 2621;  End: 4294  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003406_01168.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 164 505 2.6e-28 0.7905405405405406

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02874 GH18_CFLE_spore_hydrolase 1.58e-49 147 511 22 313
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
COG3858 YaaH 4.47e-33 145 512 120 419
Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning].
smart00636 Glyco_18 2.62e-16 146 351 36 249
Glyco_18 domain.
pfam00704 Glyco_hydro_18 2.45e-15 201 392 80 289
Glycosyl hydrolases family 18.
cd02875 GH18_chitobiase 3.21e-12 204 509 91 340
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBU36194.1 1.20e-163 1 517 1 440
SNU97803.1 2.82e-163 1 517 1 440
QQB17876.1 2.82e-163 1 517 1 440
ACZ24646.1 2.82e-163 1 517 1 440
ARF99299.1 2.88e-163 1 517 1 440

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3CZ8_A 2.50e-13 190 344 76 230
ChainA, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168],3CZ8_B Chain B, Putative sporulation-specific glycosylase ydhD [Bacillus subtilis subsp. subtilis str. 168]
1WNO_A 8.02e-06 225 350 130 273
Crystalstructure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus],1WNO_B Crystal structure of a native chitinase from Aspergillus fumigatus YJ-407 [Aspergillus fumigatus]
1W9P_A 8.64e-06 225 350 168 311
Specificityand affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9P_B Specificity and affinity of natural product cyclopentapeptide inhibitors against Aspergillus fumigatus, human and bacterial chitinaseFra [Aspergillus fumigatus],1W9U_A Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9U_B Specificity and affnity of natural product cyclopentapeptide inhibitor Argadin against Aspergillus fumigatus chitinase [Aspergillus fumigatus],1W9V_A Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],1W9V_B Specificity and affinity of natural product cyclopentapeptide argifin against Aspergillus fumigatus [Aspergillus fumigatus],2A3A_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3A_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with theophylline [Aspergillus fumigatus],2A3B_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3B_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with caffeine [Aspergillus fumigatus],2A3C_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3C_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with pentoxifylline [Aspergillus fumigatus],2A3E_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2A3E_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with allosamidin [Aspergillus fumigatus],2IUZ_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],2IUZ_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with C2-dicaffeine [Aspergillus fumigatus],3CH9_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CH9_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dimethylguanylurea [Aspergillus fumigatus],3CHC_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHC_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with monopeptide [Aspergillus fumigatus],3CHD_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHD_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with dipeptide [Aspergillus fumigatus],3CHE_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHE_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tripeptide [Aspergillus fumigatus],3CHF_A Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus],3CHF_B Crystal structure of Aspergillus fumigatus chitinase B1 in complex with tetrapeptide [Aspergillus fumigatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O32258 1.17e-19 186 349 86 257
Uncharacterized glycosylase YvbX OS=Bacillus subtilis (strain 168) OX=224308 GN=yvbX PE=3 SV=1
O31682 9.23e-19 152 356 27 224
Putative glycosylase YkvQ OS=Bacillus subtilis (strain 168) OX=224308 GN=ykvQ PE=3 SV=1
O05495 2.73e-12 190 344 168 322
Putative sporulation-specific glycosylase YdhD OS=Bacillus subtilis (strain 168) OX=224308 GN=ydhD PE=1 SV=2
P37531 3.23e-08 191 380 173 367
Cortical fragment-lytic enzyme OS=Bacillus subtilis (strain 168) OX=224308 GN=sleL PE=1 SV=2

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
0.000421 0.997808 0.001117 0.000230 0.000209 0.000190

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003406_01168.