CAZyme Information: MGYG000002051_02027

Basic Information

• Species: Prevotella sp900546345
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900546345
• CAZyme ID: MGYG000002051_02027
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578	MGYG000002051_31|CGC1	64814.32	7.8957

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002051	3257941	MAG	China	Asia

• Gene Location: Start: 28180; End: 29916 Strand: +

Full Sequence      

MKKICLTICLLALTLGLATAQSSPLVQQQTSARLNTLSPQFLSGTHAMLRVTPEKRYLLL
PVEEKESESKIRVIKNGHADASIDIRLATGKADYYVPLDLSRYGKGELLLDLVFTGNYRT
VGNIEDYSCWKLMKQSDTFDTTNREQWRPQYHHTPAWGWMNDPNGMFYKDGVWHLYFQYN
PYGSMWGNMTWGHSVSRDLIHWTHEPEAVLPDALGTVFSGSAIVDSTGSAGFGKNAVVAM
YTSARENQTQSLAYSNDGGKTFTKYEGNPVLTAKEPDFRDPKMLWNDDTQEWNLVMATGQ
KMNFYSSKDLKNWKFESSFGEGYGCHKGVWECPDLMKMDNGKWVLVCNINPGGPYGGSAT
QYFVGQWDGHKFTCESKPEVTKWMDYGKDHYATVTFSGAPNGRHVALAWMSNWQYAAVVP
TLQYRSANSIPRDLSLFNEGGEDYVSVKPSPEVLKAFNKPAAGISEACMVEVSRLRPNAT
IELSNGKGERVVMRYNASEQSFSFDRLKSGQTDFSDAFPSVTIAPTHGRVNRVLIFIDKS
SIEVFDADGKFALTNLVFPTSPYNRLTVKGGKAKIRKM

Enzyme Prediction     

EC	3.2.1.26	3.2.1.64	3.2.1.80	3.2.1.65	3.2.1.153

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	152	438	2.7e-92	0.9658703071672355

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	7.56e-148	158	436	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	4.33e-123	140	574	21	476	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	2.03e-119	152	549	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	1.79e-110	152	441	1	302	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	9.03e-84	158	436	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUI94039.1	2.38e-267	41	578	24	560
QUB92623.1	1.42e-266	41	578	24	560
AXV49687.1	5.75e-266	41	578	24	560
BCS84704.1	6.23e-266	41	574	2	539
QUB90811.1	1.34e-264	41	578	24	560

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	5.35e-99	145	571	5	501	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]
3KF3_A	5.87e-82	148	558	10	476	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	6.35e-82	148	558	13	479	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U75_A	8.73e-81	148	558	36	502	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]
3U14_A	1.72e-80	148	558	36	502	ChainA, Fructofuranosidase [Schwanniomyces occidentalis],3U14_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	2.74e-113	145	578	32	504	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3	3.55e-98	132	571	11	520	Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
A2R0E0	1.08e-96	145	571	24	520	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
E1ABX2	1.18e-95	145	571	24	520	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6	1.18e-95	145	571	24	520	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000468	0.998681	0.000307	0.000171	0.000172	0.000164

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002051_02027.