dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001735_00473

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Basic Information help

Species

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides;

CAZyme ID

MGYG000001735_00473

CAZy Family

GH32

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
724	MGYG000001735_4\|CGC2	81822.37	4.9679

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001735	5309957	MAG	Sweden	Europe

Gene Location

Start: 83493; End: 85667 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001735_00473.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH32	264	548	2.1e-67	0.9692832764505119

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	5.30e-116	269	545	1	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	8.79e-98	254	720	23	486	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	8.37e-80	264	683	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	4.07e-66	264	548	1	300	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.
TIGR01322	scrB_fam	3.18e-57	247	693	1	444	sucrose-6-phosphate hydrolase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEG37374.1	5.82e-117	250	723	129	581
BAJ63910.1	3.08e-111	255	690	5	414
BBE18152.1	2.25e-110	238	723	9	480
QEG37392.1	2.36e-110	250	723	277	727
QGY44358.1	1.98e-109	238	722	11	483

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	3.89e-66	255	723	3	518	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]
4EQV_A	1.45e-52	260	697	8	486	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]
3KF3_A	2.58e-52	257	691	7	475	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	2.73e-52	257	691	10	478	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U75_A	2.08e-51	239	691	20	501	ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [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	8.56e-88	254	723	29	514	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
E1ABX2	1.23e-65	255	723	22	537	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6	1.23e-65	255	723	22	537	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
Q96TU3	1.71e-65	236	723	3	537	Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
A2R0E0	3.29e-65	255	723	22	537	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 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
0.000401	0.455561	0.543462	0.000197	0.000193	0.000174

TMHMM Annotations help

There is no transmembrane helices in MGYG000001735_00473.