CAZyme Information: MGYG000003993_01410

Basic Information

• Species: Alistipes sp900550925
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900550925
• CAZyme ID: MGYG000003993_01410
• CAZy Family: GH18
• CAZyme Description: Chitinase A1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
339	MGYG000003993_7|CGC2	37429.73	6.0373

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003993	1895769	MAG	United Kingdom	Europe

• Gene Location: Start: 65642; End: 66661 Strand: +

Full Sequence      

MKQHNVLIAISLLLALCGCNKTTPVDKADRIVAAYVTAGSESIPDPACLTHINYAFGHVA
ETFDSVCIANPDRLRQIVELKKIKPSLKITLSLGGWGSGRFSEMAADDSLRHAFVADCRH
IVDQYGLDGIDLDWEYPTSSVAGISSSPDDTENFTKLVSELRQTLGEDKLLTVASPANAR
YIDFAAISDMIDLVNIMTYDMAKPPYHHSAFADSPMSNGESCIRAVKRHLKAGVPADKLV
LGIPFYGHGRAPLPDYINYDKIVELQKVASQKWDNKAKMPYLADEAGEMICCYDDPKSIA
VKSKWLLKRGLRGAMYWQYDGDDSQGTLRNAVYNSIMEQ

Enzyme Prediction     

No EC number prediction in MGYG000003993_01410.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	45	334	3.3e-67	0.8817567567567568

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	6.27e-89	49	322	26	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.
pfam00704	Glyco_hydro_18	1.64e-71	32	322	2	307	Glycosyl hydrolases family 18.
smart00636	Glyco_18	1.49e-70	45	322	22	334	Glyco_18 domain.
cd02872	GH18_chitolectin_chitotriosidase	3.85e-66	45	327	24	346	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	4.46e-51	20	332	29	432	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ADV45176.1	9.31e-124	1	339	1	342
QIK56154.1	3.93e-123	3	339	2	348
QIK61506.1	3.19e-122	3	339	2	348
ATP56025.1	3.69e-122	5	339	9	342
SCD19272.1	1.78e-120	26	337	31	342

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6TSB_AAA	5.08e-52	31	317	37	332	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6T9M_AAA	8.03e-52	31	317	56	351	ChainAAA, Peroxiredoxin [Clostridioides difficile 630]
6INX_A	2.64e-49	49	336	27	342	Structuralinsights into a novel glycoside hydrolase family 18 N-acetylglucosaminidase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
3QOK_A	5.95e-47	49	329	54	410	ChainA, Putative chitinase II [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
4NZC_A	7.32e-47	45	324	30	385	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P20533	1.54e-43	18	332	93	447	Chitinase A1 OS=Niallia circulans OX=1397 GN=chiA1 PE=1 SV=1
P36362	6.61e-36	39	326	43	379	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
Q13231	1.00e-31	45	326	47	367	Chitotriosidase-1 OS=Homo sapiens OX=9606 GN=CHIT1 PE=1 SV=1
Q9W092	3.22e-31	29	329	40	396	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
Q95M17	7.36e-31	45	330	47	373	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA 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	0.000056	0.999994	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003993_01410.