CAZyme Information: MGYG000002511_01976

Basic Information

• Species: Klebsiella variicola
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella; Klebsiella variicola
• CAZyme ID: MGYG000002511_01976
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
417		45661.74	5.4696

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002511	5624300	Isolate	Australia	Oceania

• Gene Location: Start: 216637; End: 217890 Strand: -

Full Sequence      

MKRLPLLAALPLLCASALSAQPLMSVGYFNGGGDVTAGPGGDIDKLDVRQITHLNYSFGL
IYNDEKDETNAALKDPAHLHEIWLSPKVQADLQKLPALRKQNPDLKVLLSVGGWGARGFS
GAAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPVNGAWGLVASQPADRDNFTALLKEL
RAAFGTGKLVTMAVGANAESPKSWVDVKAIAPSLDYINLMTYDMAYGTQYFNSNLYDSSH
WPTVAAADKYSADFVVNNYLAAGLKPSQMNLGIGFYGRVPKRAVEPGIDWTKADAQNNPV
TQPYFGPQEVALFASLGYDLSKDTYVKYNDIVGKLLNDPQKRFTEHWDDEAKVPWLSVQS
AEGKPLFALSYENPRSVAIKADYIKAKGLAGAMFWEYGADDQNQLARQLAESLGIKH

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	25	407	4e-73	0.9527027027027027

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	2.99e-100	25	400	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	5.61e-85	26	400	3	334	Glyco_18 domain.
cd02872	GH18_chitolectin_chitotriosidase	1.36e-74	52	401	29	342	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.
pfam00704	Glyco_hydro_18	1.39e-71	26	400	3	307	Glycosyl hydrolases family 18.
COG3325	ChiA	2.39e-61	19	416	34	439	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VTO22364.1	2.46e-310	1	417	1	417
ADC58998.1	2.46e-310	1	417	1	417
ART07585.1	2.46e-310	1	417	1	417
QTH74184.1	2.46e-310	1	417	1	417
QOV56843.1	2.46e-310	1	417	1	417

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QOK_A	2.92e-295	2	417	5	420	ChainA, Putative chitinase II [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
4LGX_A	2.68e-237	15	415	1	401	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
4NZC_A	2.84e-237	20	415	3	398	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]
4PTM_A	3.41e-237	20	415	3	398	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]
6HM1_A	4.33e-237	24	415	4	395	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	7.59e-46	15	413	36	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
Q9W092	6.59e-37	43	401	62	390	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
Q11174	3.03e-32	52	403	83	402	Probable endochitinase OS=Caenorhabditis elegans OX=6239 GN=cht-1 PE=1 SV=1
Q9D7Q1	1.78e-31	93	401	78	362	Chitotriosidase-1 OS=Mus musculus OX=10090 GN=Chit1 PE=1 SV=2
Q95M17	2.70e-31	44	416	44	390	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000303	0.999036	0.000178	0.000148	0.000144	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002511_01976.