CAZyme Information: MGYG000003604_01201

Basic Information

• Species: Alistipes sp900770585
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900770585
• CAZyme ID: MGYG000003604_01201
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
380		43392.39	5.8432

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003604	1572375	MAG	Fiji	Oceania

• Gene Location: Start: 1622; End: 2764 Strand: -

Full Sequence      

MRKLLNVLFAVVAMTLVACGDDDPIPEPTPTPKPDTEQEDELYPEVAGRVVVSYVTYYGS
KIPDVRYMTHINYAFAELVEDDNGVYQSFKLQGKESRFKQIVDLKKKKPSLKILLSFTHG
SSNSKYTKENPFGGFSDMAKSDVSRKKFAQDCLDFCKKWGIDGIDIDWEFPGISWNGEEK
YDREVDVENYTLMMKQLRETLGDKYLLTYAGYVFDAQGSAENKNWKYIDIKSVDPYVDWV
NIMTYNMTSQAHSALNNPKLWVDCKRAVKHYTEKGVAPSKLVLGVPFFGWGEVTWTYKKI
IGLDKTKYKFDNWDSASSVPYVTEIATGERLCAYDNPKSIGMKGDFARGSGLKGMMSWEY
DQDDAKLSLNEAMWQSVMKK

Enzyme Prediction     

No EC number prediction in MGYG000003604_01201.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	60	367	2e-61	0.8817567567567568

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	4.63e-81	51	363	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	6.42e-65	50	363	1	334	Glyco_18 domain.
pfam00704	Glyco_hydro_18	1.03e-62	50	363	1	307	Glycosyl hydrolases family 18.
cd02872	GH18_chitolectin_chitotriosidase	4.85e-51	69	364	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.
COG3325	ChiA	3.42e-45	57	370	55	430	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEC44030.1	5.76e-124	41	380	34	371
AGY54522.1	7.81e-123	45	380	42	376
QMI82040.1	6.37e-114	6	380	4	375
QBJ17256.1	1.28e-113	2	380	3	375
QPH57581.1	1.81e-113	6	380	4	375

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NZC_A	3.44e-34	64	364	30	384	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	3.73e-34	64	364	30	384	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	3.92e-34	64	364	33	387	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6HM1_A	4.92e-34	64	364	27	381	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
6F8N_A	1.63e-33	64	364	35	389	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	2.23e-26	100	371	144	446	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P48827	4.38e-23	99	363	110	383	Endochitinase 42 OS=Trichoderma harzianum OX=5544 GN=chit42 PE=1 SV=1
P36909	3.69e-22	68	365	270	596	Chitinase C OS=Streptomyces lividans OX=1916 GN=chiC PE=2 SV=1
A6N6J0	5.48e-22	68	363	65	390	Endochitinase 46 OS=Trichoderma harzianum OX=5544 GN=chit46 PE=1 SV=1
Q873X9	1.04e-21	65	363	66	389	Endochitinase B1 OS=Neosartorya fumigata OX=746128 GN=chiB1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000013	1.000051	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003604_01201.