CAZyme Information: MGYG000004734_00110

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; HGM11417
• CAZyme ID: MGYG000004734_00110
• CAZy Family: GH137
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
327		37342.83	5.6025

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004734	2053744	MAG	China	Asia

• Gene Location: Start: 111213; End: 112196 Strand: +

Full Sequence      

MQNLFEKYSGFQKTGKPVLTGSGVPGTYNELSVDVPFVFFHAGKYWLLHVGFDGKGYRTA
LAVSDRIDGEFRFSHLVFDRETGSGWSAANAAGTYIFSENNLFGTRTLRKVDGKYWMFFH
SYPGEGYEEGPAKMGMAWCDREDLTEWHKLENPILRPEDGESWECGGLYKEYVVEHEGKY
YLFYNAKNIPPEGAFWTEQTGIAVSDNFYDWTRYPGNPVMRVRKEGFDTRFVSDPFVVWD
GEYWLNFYFGLGADGARGGLAYSTDLLRWNMFPKPILDKGKPGEIDDVHAHKSALFYENG
KLYHFYTAVGNTSAGEHRLITCAVKEI

Enzyme Prediction     

No EC number prediction in MGYG000004734_00110.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH137	11	314	6.4e-80	0.9058823529411765

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18609	GH32-like	5.27e-11	143	288	51	205	Glycosyl hydrolase family 32 family protein. The GH32 family contains glycosyl hydrolase family GH32 proteins that cleave 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.
cd08995	GH32_EcAec43-like	7.03e-11	112	278	9	175	Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2). This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 enzymes cleave 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). GH32 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.
cd08994	GH43_62_32_68_117_130-like	1.18e-10	51	308	36	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.
cd08991	GH43_HoAraf43-like	1.87e-10	36	221	57	225	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.
cd08772	GH43_62_32_68_117_130	1.37e-09	112	316	9	202	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QHW32796.1	4.35e-117	6	308	7	308
QHT63254.1	1.51e-116	6	308	7	308
ACX65262.1	2.02e-110	13	316	11	311
QTH42992.1	2.16e-110	13	327	11	330
QJD81968.1	8.21e-106	13	319	11	313

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5MUI_A	1.45e-29	11	326	38	365	Glycosidehydrolase BT_0996 [Bacteroides thetaiotaomicron VPI-5482]
5MT2_A	1.02e-28	11	326	38	365	Glycosidehydrolase BT_0996 [Bacteroides thetaiotaomicron VPI-5482],5MUJ_A BT0996 RGII Chain B Complex [Bacteroides thetaiotaomicron VPI-5482]
1W2T_A	1.09e-07	113	286	26	190	beta-fructosidasefrom Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_B beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_C beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_D beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_E beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_F beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8]
1UYP_A	1.46e-07	113	269	26	174	Thethree-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_B The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_C The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_D The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_E The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_F The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33833	2.53e-07	113	269	26	174	Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000031	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004734_00110.