dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Alistipes sp001941065

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; Alistipes sp001941065

CAZyme ID

MGYG000000437_01432

CAZy Family

GH32

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
594	MGYG000000437_46\|CGC1	66690.03	5.2792

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000437	3341375	MAG	Sweden	Europe

Gene Location

Start: 13704; End: 15488 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000000437_01432.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH32	134	433	6.4e-99	0.9931740614334471

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	1.54e-163	140	421	2	289	glycoside hydrolase family 32 protein such as Aspergillus ficuum endo-inulinase (Inu2). This subfamily of glycosyl hydrolase family GH32 includes endo-inulinase (inu2, EC 3.2.1.7), exo-inulinase (Inu1, EC 3.2.1.80), invertase (EC 3.2.1.26), and levan fructotransferase (LftA, EC 4.2.2.16), among others. These 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). 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.
COG1621	SacC	6.85e-136	124	588	23	482	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	2.03e-128	134	555	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	6.55e-117	134	434	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.
cd08996	GH32_FFase	1.18e-92	140	421	1	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BBL06517.1	4.42e-267	11	587	13	586
QJE30123.1	1.91e-207	18	589	27	599
QUT52474.1	2.70e-207	18	589	27	599
QCY54656.1	2.70e-207	18	589	27	599
QUR48642.1	3.83e-207	18	589	27	599

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	6.89e-89	129	591	7	513	Crystalstructure of exo-inulinase from Aspergillus awamori in spacegroup P21 [Aspergillus awamori],1Y9G_A Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose [Aspergillus awamori],1Y9M_A Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121 [Aspergillus awamori]
3RWK_X	9.61e-78	124	594	23	516	Firstcrystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum],3SC7_X First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes. [Aspergillus ficuum]
4EQV_A	9.01e-70	130	564	8	481	Structureof Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_B Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_C Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_D Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_E Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_F Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_G Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_H Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C]
6J0T_A	2.72e-65	130	585	39	538	Thecrystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042],6J0T_B The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042]
3KF3_A	1.89e-64	130	422	10	312	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	1.22e-149	129	589	34	507	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
A2R0E0	2.11e-89	129	592	26	533	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
E1ABX2	2.96e-89	129	592	26	533	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6	2.96e-89	129	592	26	533	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
Q96TU3	6.28e-88	129	591	26	532	Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000002	1.000047	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000437_01432.

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