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CAZyme Information: MGYG000003335_01494

You are here: Home > Sequence: MGYG000003335_01494

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 GCA-900066135 sp900543575
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; GCA-900066135; GCA-900066135 sp900543575
CAZyme ID MGYG000003335_01494
CAZy Family GH18
CAZyme Description Chitinase A1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
335 MGYG000003335_163|CGC2 37821.94 5.2836
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003335 3295822 MAG China Asia
Gene Location Start: 33966;  End: 34973  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003335_01494.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 14 322 1.2e-54 0.8614864864864865

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 3.22e-80 22 320 26 322
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.
smart00636 Glyco_18 3.49e-69 3 315 1 329
Glyco_18 domain.
COG3325 ChiA 1.45e-63 22 331 65 434
Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704 Glyco_hydro_18 2.07e-61 3 315 1 302
Glycosyl hydrolases family 18.
cd02872 GH18_chitolectin_chitotriosidase 6.34e-54 23 315 29 336
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANS77385.1 7.04e-105 3 329 13 345
QDM46973.1 5.29e-104 4 326 8 336
ANY73914.1 6.00e-100 4 326 6 334
ALS30085.1 1.04e-98 6 329 10 339
AVV56031.1 1.14e-98 6 334 8 342

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6INX_A 3.65e-95 4 326 7 335
Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A 5.95e-60 18 334 533 882
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]
5GZT_B 1.68e-59 18 334 784 1133
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]
6BT9_A 1.00e-50 48 320 147 448
ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
1ITX_A 1.36e-47 46 329 110 415
ChainA, Glycosyl Hydrolase [Niallia circulans]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P20533 4.12e-45 46 329 142 447
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9D7Q1 1.18e-26 15 315 44 356
Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
Q11174 1.97e-26 23 315 83 394
Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
P36362 1.84e-25 7 332 42 384
Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
Q95M17 1.01e-24 23 315 52 360
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 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
1.000061 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003335_01494.