CAZyme Information: MGYG000002468_02977

Basic Information

• Species: Enterococcus caccae
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus; Enterococcus caccae
• CAZyme ID: MGYG000002468_02977
• CAZy Family: GH18
• CAZyme Description: Chitinase D

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
349	MGYG000002468_21|CGC1	38344.44	6.0326

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002468	3531321	Isolate	United States	North America

• Gene Location: Start: 25056; End: 26105 Strand: +

Full Sequence      

MKFKQFIPAFLLVSGIVFGSLLTPLPAHASDSASEMVSVANKKVLVGYWHNWASKGRDGY
KQGTSANISLADVNKAYNVVPVSFMKSDGVNRIPTFAPYNKTDAAFRQDVALLNSQGRAV
LLALGGADAHIQLKAGDEQAFADEIIRQVETYGFDGLDIDLEQSAITAGDNQTVIPTALK
KVKEHYKTQGKNFLITMAPEFPYLKPGGAYEKYITSLDGYYDYIAPQLYNQGGDGVWVDE
IMTWIPQSNDALKYEFLYYMSDSMIHGTRTFLKIPNNKLVLGLPANVDGAGSGYVSDPNA
VYKALDQLAKDGNPIKGLMTWSANWDIGTNVNGVSYNNEFATRYARILQ

Enzyme Prediction     

EC	3.2.1.14

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	42	286	5.3e-29	0.6621621621621622

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3469	Chi1	2.40e-172	15	348	3	329	Chitinase [Carbohydrate transport and metabolism].
cd02871	GH18_chitinase_D-like	2.23e-102	43	345	1	310	GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
pfam00704	Glyco_hydro_18	1.48e-16	44	326	1	307	Glycosyl hydrolases family 18.
cd00598	GH18_chitinase-like	3.47e-12	45	230	1	177	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
cd02877	GH18_hevamine_XipI_class_III	1.97e-11	45	337	3	275	This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALS35954.1	4.07e-245	1	349	1	349
ALS01709.1	3.28e-235	1	349	1	349
QDJ05233.1	5.37e-204	1	349	1	348
QOG32850.1	7.63e-204	1	349	1	348
AZV95926.1	2.18e-203	1	349	1	348

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4AXN_A	9.65e-145	27	349	9	328	Hallmarksof processive and non-processive glycoside hydrolases revealed from computational and crystallographic studies of the Serratia marcescens chitinases [Serratia marcescens],4AXN_B Hallmarks of processive and non-processive glycoside hydrolases revealed from computational and crystallographic studies of the Serratia marcescens chitinases [Serratia marcescens]
3IAN_A	6.34e-139	43	348	5	310	ChainA, Chitinase [Lactococcus lactis subsp. lactis]
4W5Z_A	2.66e-124	37	348	25	338	Highresolution crystal structure of catalytic domain of Chitinase 60 from psychrophilic bacteria Moritella marina. [Moritella marina]
4HMC_A	9.41e-122	37	348	3	316	Crystalstructure of cold-adapted chitinase from Moritella marina [Moritella marina],4HMD_A Crystal structure of cold-adapted chitinase from Moritella marina with a reaction intermediate - oxazolinium ion (NGO) [Moritella marina],4HME_A Crystal structure of cold-adapted chitinase from Moritella marina with a reaction product - NAG2 [Moritella marina]
4MB3_A	2.67e-121	37	348	3	316	Crystalstructure of E153Q mutant of cold-adapted chitinase from Moritella marina [Moritella marina],4MB4_A Crystal structure of E153Q mutant of cold-adapted chitinase from Moritella complex with Nag4 [Moritella marina],4MB5_A Crystal structure of E153Q mutant of cold-adapted chitinase from Moritella complex with Nag5 [Moritella marina]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q838S2	2.94e-202	1	349	1	348	Chitinase OS=Enterococcus faecalis (strain ATCC 700802 / V583) OX=226185 GN=EF_0361 PE=1 SV=1
P27050	6.13e-36	30	330	177	500	Chitinase D OS=Niallia circulans OX=1397 GN=chiD PE=1 SV=4
E9F7R6	3.00e-24	11	333	9	343	Endochitinase 4 OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=chi4 PE=3 SV=1
A5FB63	4.70e-21	29	345	1129	1481	Chitinase ChiA OS=Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101) OX=376686 GN=chiA PE=1 SV=1
Q8NJQ5	6.83e-20	25	326	12	327	Endochitinase 37 OS=Trichoderma harzianum OX=5544 GN=chit37 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
0.000577	0.998388	0.000238	0.000299	0.000261	0.000224

TMHMM  Annotations     

start	end
7	29