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CAZyme Information: MGYG000004203_01271

You are here: Home > Sequence: MGYG000004203_01271

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_A; Clostridia; Lachnospirales; Lachnospiraceae; Acetatifactor;
CAZyme ID MGYG000004203_01271
CAZy Family GH18
CAZyme Description Chitinase A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
498 55311.86 3.9531
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004203 2860639 MAG United Kingdom Europe
Gene Location Start: 64221;  End: 65717  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 70 487 4.2e-60 0.956081081081081

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06548 GH18_chitinase 1.10e-67 72 481 1 322
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 1.55e-53 71 477 1 330
Glyco_18 domain.
COG3325 ChiA 4.12e-52 72 481 40 423
Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704 Glyco_hydro_18 6.77e-52 71 481 1 307
Glycosyl hydrolases family 18.
cd02872 GH18_chitolectin_chitotriosidase 3.70e-37 156 483 52 352
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
QUA53259.1 6.38e-103 72 495 33 402
QTE75743.1 7.17e-102 72 495 33 402
QTE71783.1 7.17e-102 72 495 33 402
QTE68039.1 1.43e-101 72 487 33 392
QUC67499.1 2.85e-101 72 495 33 402

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JM7_A 2.85e-29 152 483 53 352
Crystalstructure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A 3.43e-28 152 483 53 352
Crystalstructure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
6INX_A 1.43e-27 173 477 61 325
Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
6BT9_A 2.70e-27 70 481 37 448
ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]
6IGY_A 1.28e-26 62 495 8 376
Crystalstructure of Aspergillus niger chitinase B [Aspergillus niger]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P32823 4.23e-28 75 495 163 585
Chitinase A OS=Pseudoalteromonas piscicida OX=43662 GN=chiA PE=1 SV=1
Q95M17 5.01e-24 157 490 69 374
Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
P20533 1.67e-23 65 481 39 438
Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P36909 3.37e-23 57 482 227 595
Chitinase C OS=Streptomyces lividans OX=1916 GN=chiC PE=2 SV=1
C5P230 1.65e-22 63 486 31 388
Endochitinase 1 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CTS1 PE=3 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 1.000073 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004203_01271.