dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Prevotella sp900554045

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900554045

CAZyme ID

MGYG000001040_01849

CAZy Family

GH32

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
814	MGYG000001040_193\|CGC1	88316.78	4.8959

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001040	2860396	MAG	Denmark	Europe

Gene Location

Start: 8162; End: 10606 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000001040_01849.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH32	261	569	3.1e-58	0.9965870307167235

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd08996	GH32_FFase	2.38e-75	268	559	2	281	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.
smart00640	Glyco_32	1.48e-64	261	691	1	436	Glycosyl hydrolases family 32.
COG1621	SacC	7.23e-57	257	729	29	486	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
pfam00251	Glyco_hydro_32N	9.62e-52	261	569	1	308	Glycosyl hydrolases family 32 N-terminal domain. This domain corresponds to the N-terminal domain of glycosyl hydrolase family 32 which forms a five bladed beta propeller structure.
cd18624	GH32_Fruct1-like	1.41e-34	268	559	2	296	glycoside hydrolase family 32 protein such as Arabidopsis thaliana cell-wall invertase 1 (AtBFruct1;Fruct1;AtcwINV1;At3g13790). This subfamily of glycosyl hydrolase family GH32 includes fructan beta-(2,1)-fructosidase and fructan 1-exohydrolase IIa (1-FEH IIa, EC 3.2.1.153), cell-wall invertase 1 (EC 3.2.1.26), sucrose:fructan 6-fructosyltransferase (6-Sst/6-Dft, EC 2.4.1.10), and levan fructosyltransferases (EC 2.4.1.-) among others. This enzyme 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. 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. 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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AXV49252.1	1.39e-234	46	731	336	1001
QUB90817.1	8.80e-234	46	731	317	982
QUB92629.1	2.56e-233	9	731	1	691
AEA21196.1	9.38e-231	9	731	1	691
QUB89002.1	9.38e-231	9	731	1	691

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7VCO_A	1.27e-32	258	727	27	485	ChainA, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
1UYP_A	8.91e-26	255	701	1	406	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]
1W2T_A	2.15e-25	255	701	1	406	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]
6NU7_A	5.28e-25	260	691	36	452	Structureof sucrose-6-phosphate hydrolase from Lactobacillus gasseri [Lactobacillus gasseri 224-1],6NU8_A Structure of sucrose-6-phosphate hydrolase from Lactobacillus gasseri in complex with fructose [Lactobacillus gasseri 224-1]
2QQU_A	9.63e-22	257	580	5	342	ChainA, Beta-fructofuranosidase [Arabidopsis thaliana]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q5JJV0	1.51e-31	257	727	60	580	Beta-fructofuranosidase, insoluble isoenzyme 4 OS=Oryza sativa subsp. japonica OX=39947 GN=CIN4 PE=2 SV=1
Q56UD0	9.00e-31	257	727	38	571	Beta-fructofuranosidase, insoluble isoenzyme 6 OS=Oryza sativa subsp. japonica OX=39947 GN=CIN6 PE=2 SV=1
B6DXP5	2.20e-30	252	727	54	580	Fructan 1-exohydrolase OS=Leymus chinensis OX=52714 GN=1-FEH PE=2 SV=1
B6DZC8	2.85e-30	252	727	56	582	Fructan 1-exohydrolase w3 OS=Triticum aestivum OX=4565 GN=1-FEHw3 PE=1 SV=1
Q84LA1	5.07e-30	257	727	61	582	Fructan 1-exohydrolase w2 OS=Triticum aestivum OX=4565 GN=1-FEHw2 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.725964	0.259984	0.012088	0.001127	0.000314	0.000530

TMHMM Annotations help

There is no transmembrane helices in MGYG000001040_01849.

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