CAZyme Information: MGYG000001615_05069

Basic Information

• Species: Eisenbergiella sp900548905
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900548905
• CAZyme ID: MGYG000001615_05069
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
386	MGYG000001615_60|CGC2	41628	6.8474

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001615	6842156	MAG	China	Asia

• Gene Location: Start: 21062; End: 22222 Strand: +

Full Sequence      

MKKHIIHSLVAAAVLLLAGTGMGAKAAPAKTDTGNLVVGYYTNWSSDKGYTPADIPANKL
THLNYAFAKIDPAVNTIAMANPEKDIKNFEQLRALKKKNPALKTLISVGGWDYSTYFSTI
AATEESRNQFASGCLTFMLTHGFDGIDLDWEYPVSGGPAGNMNSPEDKQNFTLLLSAIRN
QLNAQSLRDGKKYYLTIAGAANSSYLNKIEPLQVAGLVDYIFVMAYDMHGPWDTYSDLGA
PLYNPAEESPQYKNSVQNGIQAYLNAGVAAGKLVLGMPFYGYLYEGTAAEREGRYSTFSK
ARALGYDAIKRTYLNNPAFSSFFHEGAMVPYLYGNGAFLSYENPRSITAKAAFAGNAGLA
GVGIWELSHDSGGELLESARAGLAGA

Enzyme Prediction     

EC	3.2.1.14	3.2.1.17	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	37	373	7.2e-78	0.9391891891891891

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	1.41e-118	37	370	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	7.84e-111	37	370	2	334	Glyco_18 domain.
COG3325	ChiA	2.46e-96	19	385	19	438	Chitinase, GH18 family [Carbohydrate transport and metabolism].
pfam00704	Glyco_hydro_18	8.01e-93	37	370	2	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	6.91e-85	37	367	1	338	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QNL43287.1	9.98e-145	13	385	9	378
QCI60723.1	1.32e-133	1	379	1	381
BCK83697.1	4.74e-127	38	379	1	341
QUO36603.1	3.60e-120	15	380	16	373
QEY33675.1	9.08e-120	36	379	170	509

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ITX_A	2.02e-84	37	383	14	419	ChainA, Glycosyl Hydrolase [Niallia circulans]
6KST_A	2.00e-78	37	370	9	357	Crystalstructure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KST_B Crystal structure of the catalytic domain of chitinase ChiL from Chitiniphilus shinanonensis (CsChiL) [Chitiniphilus shinanonensis],6KXL_A Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXL_B Crystal structure of the catalytic domain of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
6KXM_A	1.12e-77	37	370	9	357	Crystalstructure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXM_B Crystal structure of D157N mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
6KXN_A	2.48e-76	37	370	9	357	Crystalstructure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis],6KXN_B Crystal structure of W50A mutant of Chitiniphilus shinanonensis chitinase ChiL (CsChiL) complexed with N,N'-diacetylchitobiose [Chitiniphilus shinanonensis]
6BT9_A	7.56e-70	37	370	39	448	ChitinaseChiA74 from Bacillus thuringiensis [Bacillus thuringiensis],6BT9_B Chitinase ChiA74 from Bacillus thuringiensis [Bacillus thuringiensis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.06e-80	37	383	46	451	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P32470	5.66e-48	1	383	5	398	Chitinase 1 OS=Aphanocladium album OX=12942 GN=CHI1 PE=1 SV=2
Q92222	9.38e-47	33	385	2	362	Endochitinase B OS=Emericella nidulans OX=162425 GN=chiB PE=1 SV=3
G5EAZ3	9.38e-47	33	385	2	362	Endochitinase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chiB PE=1 SV=1
P48827	1.15e-46	40	373	43	386	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 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
0.000465	0.995436	0.003342	0.000297	0.000235	0.000187

TMHMM  Annotations     

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