dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

UBA9506 sp003506415

Lineage

Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA9506; UBA9506; UBA9506 sp003506415

CAZyme ID

MGYG000000820_02303

CAZy Family

GH117

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
322	MGYG000000820_26\|CGC1	37175.9	6.2803

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000820	2712076	MAG	China	Asia

Gene Location

Start: 17899; End: 18867 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000000820_02303.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH117	149	304	1.1e-27	0.7582938388625592

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08994	GH43_62_32_68_117_130-like	1.87e-112	16	304	6	294	Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130. Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. 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. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.
cd08992	GH117	7.25e-16	91	209	100	225	Glycosyl hydrolase family 117 (GH117). This glycoside hydrolase 117 (GH117) family includes alpha-1,3-L-neoagarooligosaccharide hydrolase (EC 3.2.1.-); alpha-1,3-L-neoagarobiase/neoagarobiose hydrolase (NABH, EC 3.2.1.-). In the agarolytic pathway, in order to metabolize agar, NABH is an essential enzyme because it converts alpha-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose). Thus, these enzymes have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate. This family includes Zobellia galactanivorans enzymes, Zg4663 and Zg3615 (also known as ZgAhgA and ZgAhgB, respectively) that have been shown to have similar activity on unsubstituted agarose oligosaccharides while Zg3597 has been shown to be inactive, possibly due to differences in dimerization conformation, active-site structure and function. GH117 shares distant sequence similarity with families GH43 and GH32. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.
cd08772	GH43_62_32_68_117_130	5.28e-14	82	276	51	228	Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130. Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. 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. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.
cd08996	GH32_FFase	1.27e-07	165	260	72	162	Glycosyl hydrolase family 32, beta-fructosidases. Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.
cd08992	GH117	6.25e-06	57	144	130	226	Glycosyl hydrolase family 117 (GH117). This glycoside hydrolase 117 (GH117) family includes alpha-1,3-L-neoagarooligosaccharide hydrolase (EC 3.2.1.-); alpha-1,3-L-neoagarobiase/neoagarobiose hydrolase (NABH, EC 3.2.1.-). In the agarolytic pathway, in order to metabolize agar, NABH is an essential enzyme because it converts alpha-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose). Thus, these enzymes have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate. This family includes Zobellia galactanivorans enzymes, Zg4663 and Zg3615 (also known as ZgAhgA and ZgAhgB, respectively) that have been shown to have similar activity on unsubstituted agarose oligosaccharides while Zg3597 has been shown to be inactive, possibly due to differences in dimerization conformation, active-site structure and function. GH117 shares distant sequence similarity with families GH43 and GH32. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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
QUI25356.1	2.37e-118	1	322	1	332
AYQ34463.1	2.30e-105	1	322	21	338
AEI49029.1	9.57e-105	1	322	21	338
QNN25249.1	1.81e-91	3	322	30	356
QDV63364.1	1.09e-90	1	321	38	366

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3P2N_A	5.37e-11	94	262	175	338	Discoveryand structural characterization of a new glycoside hydrolase family abundant in coastal waters that was annotated as 'hypothetical protein' [Zobellia galactanivorans],3P2N_B Discovery and structural characterization of a new glycoside hydrolase family abundant in coastal waters that was annotated as 'hypothetical protein' [Zobellia galactanivorans]
4AK6_A	9.53e-11	84	234	160	319	ChainA, Anhydro-alpha-l-galactosidase [Phocaeicola plebeius],4AK6_B Chain B, Anhydro-alpha-l-galactosidase [Phocaeicola plebeius]
4AK5_A	1.28e-10	84	234	160	319	ChainA, Anhydro-alpha-l-galactosidase [Phocaeicola plebeius],4AK5_B Chain B, Anhydro-alpha-l-galactosidase [Phocaeicola plebeius]
4AK7_A	2.29e-10	84	234	160	319	ChainA, Anhydro-alpha-l-galactosidase [Phocaeicola plebeius],4AK7_B Chain B, Anhydro-alpha-l-galactosidase [Phocaeicola plebeius]
5TA7_A	2.35e-08	3	234	67	315	Crystalstructure of BuGH117Bwt [Bacteroides uniformis],5TA7_B Crystal structure of BuGH117Bwt [Bacteroides uniformis],5TA9_A Crystal structure of BuGH117Bwt in complex with neoagarobiose [Bacteroides uniformis],5TA9_B Crystal structure of BuGH117Bwt in complex with neoagarobiose [Bacteroides uniformis],5TA9_C Crystal structure of BuGH117Bwt in complex with neoagarobiose [Bacteroides uniformis],5TA9_D Crystal structure of BuGH117Bwt in complex with neoagarobiose [Bacteroides uniformis]