CAZyme Information: MGYG000003308_00890

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-10
• CAZyme ID: MGYG000003308_00890
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
556	MGYG000003308_312|CGC1	61373	5.6229

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003308	2610589	MAG	China	Asia

• Gene Location: Start: 3202; End: 4872 Strand: +

Full Sequence      

MIAKRFALNDPTLHIPVVDSDDFWYVRVSDENAQIGEFYIAVTAARPDFYCPMTLHGCEG
RTVTLSCADEGAPDDLFDGVLTGGSCETRPDLYPNLYREPERQQIHFSPKRGWLNDPNGL
VYAGGAFHMCFQHNPFGPNHGGVNICWGLAVSPDGVHFTEYPDAILPRDSLTHIASGSAI
VDADNLCGLGKDAILAVYTALGSNMKKGRSSSVGTRGQMIEYSTDGGMTFKPLVEGPIIP
VPKGESWRDPKILRLDDGTLCIAVYETYDGRNCVSFYSSKNARDWRFESRTMDLYECPDL
FPLPVAETGERLWVLYGANSMARIGRFENYRFAQIGESRYLDYGTAAYAGQTWNSHPDET
GRYHIAWLRDPAAAWSYDPSFNHGVPFAQGMTVTCRFALHRCADGYRLFRAPIDALKSLR
CGAGEAISLSLKGEPAQGRVSRPAAARIRLDVPGDAEFTVSASSPLRAAVCGQGFDYLPH
ERLLRFTGGKSYSPAGDGPLSIRIITDRRSTEFFINGEISASYGCGDAQKTLELYGDDAR
LDGRLWAMESIWKNNI

Enzyme Prediction     

No EC number prediction in MGYG000003308_00890.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	106	409	1.4e-58	0.9863481228668942

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	8.86e-89	111	399	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	6.56e-66	92	538	19	472	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
pfam00251	Glyco_hydro_32N	4.09e-60	106	371	1	273	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.
smart00640	Glyco_32	2.02e-59	106	517	1	436	Glycosyl hydrolases family 32.
cd08996	GH32_FFase	5.56e-50	112	371	1	258	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
BCJ97704.1	7.17e-121	1	553	1	537
ASV73298.1	4.92e-67	13	554	201	727
AGA28800.1	2.55e-64	2	524	199	687
QEH38715.1	2.37e-63	4	528	31	526
QJW95254.1	6.80e-62	1	553	180	702

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	3.14e-38	97	419	3	359	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	6.36e-31	99	377	7	290	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	6.56e-31	99	377	10	293	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U75_A	8.13e-31	76	377	15	316	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]
6J0T_A	9.68e-31	102	399	39	358	Thecrystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042],6J0T_B The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	3.89e-38	95	516	28	471	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3	1.61e-37	93	419	18	378	Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
A2R0E0	2.20e-37	97	419	22	378	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
Q76HP6	3.00e-37	97	419	22	378	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
E1ABX2	3.00e-37	97	419	22	378	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI 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
1.000021	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003308_00890.