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CAZyme Information: MGYG000004748_01544

You are here: Home > Sequence: MGYG000004748_01544

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; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides;
CAZyme ID MGYG000004748_01544
CAZy Family GH18
CAZyme Description Chitinase A1
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
376 MGYG000004748_6|CGC1 41828.33 4.7339
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004748 4696076 MAG China Asia
Gene Location Start: 33420;  End: 34550  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004748_01544.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 60 365 2e-63 0.8716216216216216

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 2.62e-85 55 359 15 322
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 5.93e-68 51 359 8 307
Glycosyl hydrolases family 18.
smart00636 Glyco_18 1.06e-64 51 359 11 334
Glyco_18 domain.
cd02872 GH18_chitolectin_chitotriosidase 6.23e-61 62 364 24 346
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 2.51e-45 55 365 55 428
Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QBJ17256.1 6.80e-216 4 376 3 375
QPH57581.1 6.80e-216 4 376 3 375
QMI82040.1 3.93e-215 4 376 3 375
BBK88809.1 1.31e-213 4 376 3 375
QUT34454.1 1.31e-213 4 376 3 375

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4NZC_A 6.33e-38 62 361 30 385
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 6.57e-38 62 361 27 382
Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A 6.94e-38 62 361 30 385
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 7.32e-38 62 361 33 388
Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A 2.26e-37 62 361 35 390
Keyresidues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [Serratia proteamaculans 568],6F8N_B Key residues affecting transglycosylation activity in family 18 chitinases - Insights into donor and acceptor subsites [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
Q9W092 2.70e-31 62 366 66 396
Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
P20533 1.70e-28 51 361 55 440
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q95M17 4.67e-28 62 364 47 370
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
Q6RY07 3.09e-27 57 364 39 370
Acidic mammalian chitinase OS=Rattus norvegicus OX=10116 GN=Chia PE=2 SV=1
Q91XA9 7.88e-27 57 364 39 370
Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

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
0.000002 0.001158 0.998882 0.000000 0.000001 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004748_01544.