dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000608_01927

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Basic Information help

Species

Lineage

Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; UMGS1518;

CAZyme ID

MGYG000000608_01927

CAZy Family

GH18

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
436		49543.52	4.5546

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000608	2613041	MAG	Madagascar	Africa

Gene Location

Start: 941; End: 2251 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.14

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH18	66	271	4.9e-37	0.706081081081081

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00704	Glyco_hydro_18	2.08e-34	68	268	85	307	Glycosyl hydrolases family 18.
smart00636	Glyco_18	1.16e-31	67	268	87	334	Glyco_18 domain.
cd02872	GH18_chitolectin_chitotriosidase	1.21e-27	68	268	93	341	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.
cd06545	GH18_3CO4_chitinase	5.97e-25	60	279	72	251	The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.
cd06548	GH18_chitinase	4.21e-24	68	268	106	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHI70669.1	6.64e-59	2	375	34	421
QKX06540.1	2.50e-24	72	369	714	992
QWP70637.1	7.04e-22	61	279	259	468
QWO91390.1	7.04e-22	61	279	259	468
QWO85994.1	7.04e-22	61	279	259	468

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5Y29_A	1.39e-18	65	268	97	351	Crystalstructure of Ostrinia furnacalis Group II chitinase catalytic domain 1 [Ostrinia furnacalis],5Y2B_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with HEPTA-N-ACETYLCHITOOCTAOSE (NAG)7 [Ostrinia furnacalis]
6JAV_A	1.54e-18	65	268	97	351	Crystalstructure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a piperidine-thienopyridine derivative [Ostrinia furnacalis],6JAW_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a napthalimide derivative [Ostrinia furnacalis],6JAX_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with chitooctaose [(GlcN)8] [Ostrinia furnacalis],6JAY_A Crystal structure of Ostrinia furnacalis Group II chitinase catalytic domain 1 in complex with a dipyrido-pyrimidine derivative [Ostrinia furnacalis]
6JM7_A	1.59e-18	68	268	98	350	Crystalstructure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis],6JMB_A Chain A, ofchtiv-allosamidin [Ostrinia furnacalis]
6JM8_A	1.70e-17	68	268	98	350	Crystalstructure of Ostrinia furnacalis Group IV chitinase [Ostrinia furnacalis]
1E9L_A	3.17e-14	64	268	87	344	Thecrystal structure of novel mammalian lectin Ym1 suggests a saccharide binding site [Mus musculus],1VF8_A The Crystal Structure of Ym1 at 1.31 A Resolution [Mus musculus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q9W092	1.13e-13	71	268	143	389	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
O35744	1.95e-13	64	268	108	365	Chitinase-like protein 3 OS=Mus musculus OX=10090 GN=Chil3 PE=1 SV=2
P36362	4.13e-13	70	194	120	271	Endochitinase OS=Manduca sexta OX=7130 PE=2 SV=1
Q91Z98	8.47e-13	64	268	108	365	Chitinase-like protein 4 OS=Mus musculus OX=10090 GN=Chil4 PE=1 SV=2
Q91XA9	1.45e-12	72	268	116	365	Acidic mammalian chitinase OS=Mus musculus OX=10090 GN=Chia PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000043	0.000006	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000608_01927.