dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001292_02606

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Basic Information help

Species

Bifidobacterium infantis

Lineage

Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium infantis

CAZyme ID

MGYG000001292_02606

CAZy Family

GH18

CAZyme Description

Endo-beta-N-acetylglucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
545	MGYG000001292_1\|CGC41	59825.82	4.5305

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001292	2832748	Isolate	not provided	not provided

Gene Location

Start: 2788893; End: 2790530 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	3.2.1.96

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06542	GH18_EndoS-like	7.22e-51	52	323	2	246	Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
cd00598	GH18_chitinase-like	2.59e-05	53	318	1	210	The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
cd02871	GH18_chitinase_D-like	0.001	82	250	23	198	GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
BAJ70116.1	1	545	1	545
QKY14302.1	1	545	1	545
VEG44861.1	1	545	1	545
ACJ53522.1	1	545	1	545
ALE08664.1	1	545	1	545

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7PUJ_A	3.19e-160	41	482	7	430	ChainA, Beta-N-acetylhexosaminidase [Enterococcus faecalis],7PUK_A Chain A, Beta-N-acetylhexosaminidase [Enterococcus faecalis],7PUK_C Chain C, Beta-N-acetylhexosaminidase [Enterococcus faecalis]
6KPL_A	2.28e-29	56	341	35	292	CrystalStructure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris in apo form [Cordyceps militaris CM01],6KPM_A Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris in complex with L-fucose [Cordyceps militaris CM01]
6KPN_A	2.79e-28	56	341	35	292	CrystalStructure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris D154N/E156Q mutant in complex with fucosyl-N-acetylglucosamine [Cordyceps militaris CM01],6KPO_A Crystal Structure of endo-beta-N-acetylglucosaminidase from Cordyceps militaris D154N/E156Q mutant in complex with fucosyl-N-acetylglucosamine-Asn [Cordyceps militaris CM01]
4NUY_A	4.26e-13	56	319	20	311	Crystalstructure of EndoS, an endo-beta-N-acetyl-glucosaminidase from Streptococcus pyogenes [Streptococcus pyogenes serotype M1]
4NUZ_A	2.25e-12	56	319	20	311	Crystalstructure of a glycosynthase mutant (D233Q) of EndoS, an endo-beta-N-acetyl-glucosaminidase from Streptococcus pyogenes [Streptococcus pyogenes serotype M1]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B7GPC7	0.0	1	545	1	545	Endo-beta-N-acetylglucosaminidase OS=Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) OX=391904 GN=Blon_2468 PE=1 SV=1
P36912	7.49e-30	56	318	66	307	Endo-beta-N-acetylglucosaminidase F2 OS=Elizabethkingia meningoseptica OX=238 GN=endOF2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000630	0.565428	0.431558	0.001857	0.000305	0.000192

TMHMM Annotations download full data without filtering help

start	end
12	34
518	540