CAZyme Information: MGYG000001346_01281

Basic Information

• Species: Bacteroides uniformis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides uniformis
• CAZyme ID: MGYG000001346_01281
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
375	MGYG000001346_13|CGC15	42091.55	4.7672

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001346	4452540	Isolate	not provided	not provided

• Gene Location: Start: 851670; End: 852797 Strand: -

Full Sequence      

MKKKLLFIIATVFLVAACHNDDYIPGLPAPGNEDNETEMAEQVAGRVALGYVTYYGTSIP
DAKYLTHINYAFAELYVKNGIYEKFGLQGDKSRFDKVKKIKSQYPHVKILLSFTNSVSNS
DNSQDGGFSALAKSPEMRKQFAQDCRAFVLSEGIDGIDIDWEFPGMTFSSNAYDELVDVE
NFTLLMKDLRAELGQSTLLTYAGYCMDKRPQGEGYKYIDVKAVDPYVDFVNIMAYDLVGA
PQHQSALNKPSNYWDCQRSVDEYLNAGVSADKLVLGIPFYGRADFNAGGSINYRDILNLS
KDDGYVIENWDTEGNVPYVTKNGSFYCGYDNPRSIAAKGEWILKNGMKGMMFWDYEGDDT
MGTLRKALWNAVMKK

Enzyme Prediction     

No EC number prediction in MGYG000001346_01281.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH18	59	366	2.6e-62	0.8783783783783784

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06548	GH18_chitinase	2.33e-87	50	358	3	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	1.71e-67	50	358	4	307	Glycosyl hydrolases family 18.
smart00636	Glyco_18	3.07e-65	49	358	3	334	Glyco_18 domain.
cd02872	GH18_chitolectin_chitotriosidase	2.06e-55	61	363	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	5.79e-44	21	368	13	436	Chitinase, GH18 family [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPH57581.1	1.69e-282	1	375	1	375
QBJ17256.1	1.39e-281	1	375	1	375
QQA31286.1	1.14e-280	1	375	1	375
QUT99830.1	1.14e-280	1	375	1	375
QUT62873.1	1.14e-280	1	375	1	375

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4NZC_A	8.53e-36	61	359	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]
6HM1_A	8.83e-36	61	359	27	381	Structuraland thermodynamic signatures of ligand binding to an enigmatic chitinase-D from Serratia proteamaculans [Serratia proteamaculans 568]
4PTM_A	9.30e-36	61	359	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	9.79e-36	61	359	33	387	Structureof Chitinase D from Serratia proteamaculans revealed an unusually constrained substrate binding site [Serratia proteamaculans 568]
6F8N_A	2.98e-35	61	359	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
Q9W092	1.46e-28	61	365	66	396	Probable chitinase 2 OS=Drosophila melanogaster OX=7227 GN=Cht2 PE=1 SV=1
P11220	5.99e-28	31	368	231	605	Chitinase 63 OS=Streptomyces plicatus OX=1922 GN=chtA PE=1 SV=2
Q95M17	1.43e-26	61	363	47	370	Acidic mammalian chitinase OS=Bos taurus OX=9913 GN=CHIA PE=1 SV=1
P36909	4.29e-26	47	362	241	598	Chitinase C OS=Streptomyces lividans OX=1916 GN=chiC PE=2 SV=1
P36362	4.58e-26	55	362	42	379	Endochitinase OS=Manduca sexta OX=7130 PE=2 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	0.000000	1.000085	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001346_01281.