dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Bacteroides oleiciplenus

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides oleiciplenus

CAZyme ID

MGYG000001422_02228

CAZy Family

GH43

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
334	MGYG000001422_2\|CGC14	38065.45	7.7576

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001422	7071122	Isolate	not provided	Asia

Gene Location

Start: 706589; End: 707593 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000001422_02228.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH43	55	292	1.8e-78	0.9878048780487805

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18821	GH43_Pc3Gal43A-like	1.12e-134	46	307	1	262	Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. 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.
cd18825	GH43_CtGH43-like	9.98e-93	46	307	1	285	Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. 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.
cd18822	GH43_CtGH43-like	3.34e-87	46	307	1	266	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. 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.
cd08985	GH43_CtGH43-like	7.74e-85	46	307	1	273	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. 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.
cd18826	GH43_CtGH43-like	1.07e-74	46	306	1	268	Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. 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
AOW11351.1	6.80e-193	13	334	3	324
QNR87050.1	4.91e-162	10	329	12	338
AXY74132.1	1.86e-156	21	331	16	327
SDT36662.1	2.31e-156	10	332	9	341
AHF14594.1	3.15e-156	26	328	24	326

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7BYS_A	2.79e-63	35	327	6	297	ChainA, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYS_B Chain B, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYT_A Chain A, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]
7BYV_A	2.86e-63	29	327	1	298	ChainA, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]
7BYX_A	2.16e-62	35	327	6	297	ChainA, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYX_B Chain B, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYX_C Chain C, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYX_D Chain D, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]
5FLW_A	1.17e-56	40	310	12	288	Crystalstructure of putative exo-beta-1,3-galactanase from Bifidobacterium bifidum s17 [Bifidobacterium bifidum S17],5FLW_B Crystal structure of putative exo-beta-1,3-galactanase from Bifidobacterium bifidum s17 [Bifidobacterium bifidum S17]
3VSF_A	2.16e-53	25	327	36	351	ChainA, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405]