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CAZyme Information: MGYG000001597_00202

You are here: Home > Sequence: MGYG000001597_00202

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 UBA866 sp900543295
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; UBA866; UBA866 sp900543295
CAZyme ID MGYG000001597_00202
CAZy Family GH18
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
521 57390.12 4.2797
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001597 2473217 MAG China Asia
Gene Location Start: 18100;  End: 19665  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 29 396 9.8e-57 0.875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 3.11e-72 28 394 10 322
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.
pfam00704 Glyco_hydro_18 2.42e-52 41 394 23 307
Glycosyl hydrolases family 18.
smart00636 Glyco_18 9.57e-51 28 394 11 334
Glyco_18 domain.
cd02872 GH18_chitolectin_chitotriosidase 1.54e-48 33 270 20 239
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 9.75e-45 41 407 65 436
Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDK20229.1 1.82e-86 30 410 40 416
QGU14940.1 2.57e-86 30 410 40 416
AWS97253.1 5.24e-86 30 411 40 417
AST79672.1 1.04e-85 30 407 40 413
AUO64755.1 1.04e-85 30 408 40 414

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4NZC_A 1.50e-80 30 407 23 396
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 1.58e-80 30 407 20 393
Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A 1.73e-80 30 407 23 396
CrystalStructure of Chitinase D from Serratia proteamaculans in complex with N-acetyl glucosamine, a hydrolyzed product of hexasaccharide at 1.7 Angstrom resolution [Serratia proteamaculans 568]
4LGX_A 1.89e-80 30 407 26 399
Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
3QOK_A 3.96e-80 30 411 43 420
ChainA, Putative chitinase II [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P20533 8.31e-33 32 409 61 453
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P32470 5.64e-23 28 416 49 420
Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
Q13231 6.56e-22 37 389 47 358
Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q95M17 9.19e-22 34 389 44 360
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
Q9WTV1 9.61e-22 37 389 45 350
Chitinase-3-like protein 1 OS=Rattus norvegicus OX=10116 GN=Chi3l1 PE=2 SV=3

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
0.999280 0.000764 0.000001 0.000001 0.000000 0.000001

TMHMM  Annotations      download full data without filtering help

start end
498 515