dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Alistipes sp900546065

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp900546065

CAZyme ID

MGYG000000414_01779

CAZy Family

GH43

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
566	MGYG000000414_12\|CGC1	63562.66	4.9826

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000414	2648727	MAG	Sweden	Europe

Gene Location

Start: 39652; End: 41352 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000000414_01779.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH43	43	301	7.5e-94	0.9961832061068703
CBM32	341	455	4.9e-23	0.8145161290322581

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08982	GH43-like	3.02e-154	41	344	3	308	Glycosyl hydrolase family 43 protein; uncharacterized. This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. 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. Many of the enzymes in this family 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.
cd08991	GH43_HoAraf43-like	4.96e-21	44	292	1	272	Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. 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.
cd08978	GH_F	1.42e-20	44	273	1	245	Glycosyl hydrolase families 43 and 62 form CAZY clan GH-F. This glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) includes family 43 (GH43) and 62 (GH62). GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. GH62 includes enzymes characterized as arabinofuranosidases (alpha-L-arabinofuranosidases; EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose side chains from xylans. 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 of the enzymes in this family display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. GH62 are also predicted to be inverting enzymes. A common structural feature of both, GH43 and GH62 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.
pfam00754	F5_F8_type_C	4.75e-19	340	465	2	124	F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.
cd08999	GH43_ABN-like	1.22e-16	44	292	9	278	Glycosyl hydrolase family 43 protein such as endo-alpha-L-arabinanase. This glycosyl hydrolase family 43 (GH43) subgroup includes mostly enzymes with alpha-L-arabinofuranosidase (ABF; EC 3.2.1.55) and endo-alpha-L-arabinanase (ABN; EC 3.2.1.99) activities. 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. The GH43 ABN enzymes hydrolyze alpha-1,5-L-arabinofuranoside linkages while the ABF enzymes cleave arabinose side chains so that the combined actions of these two enzymes reduce arabinan to L-arabinose and/or arabinooligosaccharides. These arabinan-degrading enzymes are important in the food industry for efficient production of L-arabinose from agricultural waste; L-arabinose is often used as a bioactive sweetener. 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
QUT49472.1	5.10e-168	234	566	14	345
BBE16007.1	3.04e-163	16	559	26	567
QOY89859.1	5.11e-163	18	559	36	578
QIA09145.1	8.42e-162	22	562	36	575
ADQ81046.1	9.84e-159	19	559	29	566

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5ZU6_A	7.26e-11	296	450	6	137	ACBM32 derived from alginate lyase B (AlyB-OU02) [Vibrio]
5ZU5_A	1.01e-09	296	450	6	137	Crystalstructure of a full length alginate lyase with CBM domain [Vibrio splendidus]
4QQS_A	6.58e-08	20	261	4	256	Crystalstructure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168],4QQS_B Crystal structure of a thermostable family-43 glycoside hydrolase [Halothermothrix orenii H 168]
2RVA_A	4.31e-06	339	471	12	137	Solutionstructure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]
4ZZ5_A	4.39e-06	339	471	13	138	X-raycrystal structure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZZ5_B X-ray crystal structure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZZ8_A X-ray crystal structure of chitosan-binding module 2 in complex with chitotriose derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis],4ZZ8_B X-ray crystal structure of chitosan-binding module 2 in complex with chitotriose derived from chitosanase/glucanase from Paenibacillus sp. IK-5 [Paenibacillus fukuinensis]