dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Bacteroides stercorirosoris

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides stercorirosoris

CAZyme ID

MGYG000002273_01622

CAZy Family

GH10

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
642	MGYG000002273_8\|CGC4	72176.63	5.1334

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002273	6091524	Isolate	China	Asia

Gene Location

Start: 97271; End: 99199 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000002273_01622.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH10	30	368	3.5e-102	0.9900990099009901
GH43	410	638	1.6e-83	0.7615658362989324

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18617	GH43_XynB-like	1.38e-120	411	638	1	219	Glycosyl hydrolase family 43, such as Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB). This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have been characterized to have alpha-L-arabinofuranosidase (EC 3.2.1.55) and beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activities. Beta-1,4-xylosidases are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Also included in this subfamily are Bacteroides ovatus alpha-L-arabinofuranosidases, BoGH43A and BoGH43B, both having a two-domain architecture, consisting of an N-terminal 5-bladed beta-propeller domain harboring the catalytic active site, and a C-terminal beta-sandwich domain. However, despite significant functional overlap between these two enzymes, BoGH43A and BoGH43B share just 41% sequence identity. The latter appears to be significantly less active on the same substrates, suggesting that these paralogs may play subtly different roles during the degradation of xyloglucans from different sources, or may function most optimally at different stages in the catabolism of xyloglucan oligosaccharides (XyGOs), for example before or after hydrolysis of certain side-chain moieties. It also includes Phanerochaete chrysosporium BKM-F-1767 Xyl, a bifunctional xylosidase/arabinofuranosidase. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
pfam00331	Glyco_hydro_10	4.30e-114	30	368	1	310	Glycosyl hydrolase family 10.
smart00633	Glyco_10	1.95e-105	73	361	1	258	Glycosyl hydrolase family 10.
COG3693	XynA	6.32e-94	53	368	47	339	Endo-1,4-beta-xylanase, GH35 family [Carbohydrate transport and metabolism].
cd08989	GH43_XYL-like	1.72e-72	411	638	1	213	Glycosyl hydrolase family 43, beta-D-xylosidases and arabinofuranosidases. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes that have been annotated as having beta-1,4-xylosidase (beta-D-xylosidase;xylan 1,4-beta-xylosidase; EC 3.2.1.37) activity, including Selenomonas ruminantium beta-D-xylosidase SXA. These are part of an array of hemicellulases that are involved in the final breakdown of plant cell-wall whereby they degrade xylan. They hydrolyze beta-1,4 glycosidic bonds between two xylose units in short xylooligosaccharides. It also includes various GH43 family GH43 arabinofuranosidases (EC 3.2.1.55) including Humicola insolens alpha-L-arabinofuranosidase AXHd3, Bacteroides ovatus alpha-L-arabinofuranosidase (BoGH43, XynB), and the bifunctional Phanerochaete chrysosporium xylosidase/arabinofuranosidase (Xyl;PcXyl). GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EDV05059.1	0.0	1	636	1	636
ALJ61536.1	0.0	1	636	31	655
QDO69420.1	0.0	1	636	1	625
QUT92894.1	0.0	16	636	1	610
ALJ61519.1	1.16e-204	14	370	15	371

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4PMU_A	1.62e-100	29	367	2	350	Crystalstructure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_B Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_C Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_D Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_E Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306],4PMU_F Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P1211) [Xanthomonas citri pv. citri str. 306]
4PMV_A	1.67e-100	29	367	3	351	Crystalstructure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P43212) [Xanthomonas citri pv. citri str. 306],4PMV_B Crystal structure of a novel reducing-end xylose-releasing exo-oligoxylanase (XynA) belonging to GH10 family (space group P43212) [Xanthomonas citri pv. citri str. 306]
6FHE_A	7.16e-93	28	361	11	333	Highlyactive enzymes by automated modular backbone assembly and sequence design [synthetic construct]
2CNC_A	3.73e-90	30	368	36	376	Family10 xylanase [Cellvibrio mixtus]
1UQY_A	8.10e-90	30	368	27	367	XylanaseXyn10B mutant (E262S) from Cellvibrio mixtus in complex with xylopentaose [Cellvibrio mixtus],1UQZ_A Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with 4-O-methyl glucuronic acid [Cellvibrio mixtus],1UR1_A Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with arabinofuranose alpha-1,3 linked to xylobiose [Cellvibrio mixtus],1UR2_A Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with arabinofuranose alpha 1,3 linked to xylotriose [Cellvibrio mixtus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P49942	5.12e-173	1	368	1	370	Endo-1,4-beta-xylanase A OS=Bacteroides ovatus OX=28116 GN=xylI PE=2 SV=1
P48789	2.49e-128	28	368	24	366	Endo-1,4-beta-xylanase A OS=Prevotella ruminicola OX=839 GN=xynA PE=3 SV=1
Q12603	1.38e-76	28	368	33	351	Beta-1,4-xylanase OS=Dictyoglomus thermophilum OX=14 GN=xynA PE=3 SV=1
O69231	9.15e-74	28	360	6	322	Endo-1,4-beta-xylanase B OS=Paenibacillus barcinonensis OX=198119 GN=xynB PE=1 SV=1
D5EY13	1.65e-71	1	366	1	366	Endo-1,4-beta-xylanase/feruloyl esterase OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=xyn10D-fae1A PE=1 SV=1

SignalP and Lipop Annotations help

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	1.000035	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000002273_01622.

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