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CAZyme Information: MGYG000000588_00717

You are here: Home > Sequence: MGYG000000588_00717

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
Lineage Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-313; UMGS75;
CAZyme ID MGYG000000588_00717
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
831 95991.42 4.5336
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000588 1739916 MAG Madagascar Africa
Gene Location Start: 9164;  End: 11659  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000588_00717.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 520 818 1.6e-52 0.8581081081081081

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
smart00636 Glyco_18 1.03e-53 508 816 4 334
Glyco_18 domain.
pfam00704 Glyco_hydro_18 2.73e-51 508 811 4 302
Glycosyl hydrolases family 18.
cd06548 GH18_chitinase 1.91e-49 568 811 86 317
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
cd02872 GH18_chitolectin_chitotriosidase 1.91e-40 527 827 31 360
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
COG3325 ChiA 4.08e-37 568 827 128 434
Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AUD65244.1 4.65e-92 322 831 157 742
AUD63190.1 7.81e-91 392 831 285 735
BCR35892.1 1.22e-85 392 831 281 724
VEU83132.1 4.92e-84 419 831 307 726
CCV65692.1 1.30e-82 178 831 64 728

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GZT_B 3.41e-35 456 818 243 630
CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
6INX_A 7.03e-33 516 830 18 343
Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A 4.56e-32 498 818 39 379
CrystalStructure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZU_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_A Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7],5GZV_B Crystal Structure of Chitinase ChiW from Paenibacillus sp. str. FPU-7 Reveals a Novel Type of Bacterial Cell-Surface-Expressed Multi-Modular Enzyme Machinery [Paenibacillus sp. FPU-7]
4NZC_A 4.04e-27 558 829 77 396
Crystalstructure of Chitinase D from Serratia proteamaculans at 1.45 Angstrom resolution [Serratia proteamaculans 568],4Q22_A Crystal structure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine at 1.93 Angstrom resolution [Serratia proteamaculans 568]
6HM1_A 4.17e-27 558 829 74 393
Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P48827 2.50e-25 566 821 121 391
Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
P0CB51 3.53e-25 554 816 109 383
Endochitinase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=CTS1 PE=1 SV=1
Q1E3R8 3.53e-25 554 816 109 383
Endochitinase 1 OS=Coccidioides immitis (strain RS) OX=246410 GN=CTS1 PE=3 SV=1
C5P230 8.55e-25 568 816 123 383
Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 SV=1
A6N6J0 4.02e-23 566 821 122 398
Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000072 0.000000 0.000000 0.000000

TMHMM  Annotations      download full data without filtering help

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