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CAZyme Information: MGYG000000919_03379

You are here: Home > Sequence: MGYG000000919_03379

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 Niameybacter sp900551325
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Cellulosilyticaceae; Niameybacter; Niameybacter sp900551325
CAZyme ID MGYG000000919_03379
CAZy Family GH18
CAZyme Description Chitinase A1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
339 MGYG000000919_28|CGC1 37969.02 4.7256
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000919 4175004 MAG China Asia
Gene Location Start: 20053;  End: 21072  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000919_03379.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 3 328 2.7e-71 0.9527027027027027

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 2.01e-100 21 323 22 322
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 1.23e-88 4 323 1 334
Glyco_18 domain.
pfam00704 Glyco_hydro_18 1.75e-82 4 323 1 307
Glycosyl hydrolases family 18.
COG3325 ChiA 1.05e-74 51 333 117 433
Chitinase, GH18 family [Carbohydrate transport and metabolism].
cd02872 GH18_chitolectin_chitotriosidase 7.62e-71 54 323 64 341
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
BCJ95062.1 1.45e-150 4 337 3 337
AVM42081.1 6.19e-142 5 339 12 348
BCJ97222.1 9.43e-142 4 337 3 337
QOV20718.1 3.44e-141 4 337 3 337
SYX83526.1 6.00e-134 5 334 8 341

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6INX_A 2.26e-125 7 328 9 334
Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5GZU_A 5.20e-81 21 323 46 377
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 7.65e-80 21 323 297 628
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]
1ITX_A 4.70e-68 33 336 94 419
ChainA, Glycosyl Hydrolase [Niallia circulans]
6BT9_A 3.90e-66 50 323 147 448
ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P20533 9.00e-65 33 336 126 451
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
A6N6J0 3.64e-48 49 324 111 391
Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
P48827 1.32e-45 49 324 110 384
Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
P11797 7.58e-44 14 323 33 408
Chitinase B OS=Serratia marcescens OX=615 GN=chiB PE=1 SV=1
Q13231 1.17e-43 42 324 71 364
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 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
1.000089 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000919_03379.