CAZyme Information: MGYG000001217_01543

Basic Information

• Species: Firm-10 sp004552515
• Lineage: Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-10; Firm-10 sp004552515
• CAZyme ID: MGYG000001217_01543
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
556		61397.98	5.6076

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001217	2504977	MAG	Austria	Europe

• Gene Location: Start: 1050; End: 2720 Strand: +

Full Sequence      

MIAKRFALNDPTLHIPIVDSDDFWYVRVSDENAQIGEFYIAVTAAKPDFYCPMTLHGCEG
RTVTLSCADEGAPDDLFEGVLTGGSCETRPDLYPNLYREPERQQIHFSPKRGWLNDPNGL
VYAGGAFHMCFQHNPFGPNHGGVNICWGLAVSPDGVHFTEYPDAILPHDSLTHIASGSAI
VDGDNLCGLGKDTILAVYTALGSNMKKGRSSSVGTRGQMIEYSTDGGVTFKPLVEGPIIP
VPKGESWRDPKILRLDDGTLCIAVYETYDGRNCVSFYSSKNARDWRFESRTMDLYECPDL
FPLPVTETGERLWVLYGANSMARIGRFENYRFAQIGESRYLDYGTAAYAGQTWNSHPDET
GRYHIAWLRDPAAAWSYDPSFNHGVPFAQGMTVTCRFTLHRCADGYRLFRAPIDALKSLR
CGAGEAISLSLKGEPAQGRVSRPAAARIRLDVPGDAEFTVSASSPLRAAVCGQGFDYLPH
ERLLRFTGGKSYSPAGDGPLSIRIITDRRSTEFFINGEISASYGCGDAQKTLELYGDDAR
LDGRLWAMESIWKNNI

Enzyme Prediction     

No EC number prediction in MGYG000001217_01543.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	106	410	2.6e-59	0.9897610921501706

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	2.78e-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	4.50e-66	92	538	19	472	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
pfam00251	Glyco_hydro_32N	3.88e-61	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	5.80e-61	106	517	1	436	Glycosyl hydrolases family 32.
cd08996	GH32_FFase	1.31e-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	2.02e-120	1	553	1	537
ASV73298.1	6.83e-67	13	554	201	727
AGA28800.1	2.59e-65	2	524	199	687
QEH38715.1	1.76e-61	4	528	31	526
QJW95254.1	9.18e-61	1	553	180	702

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	4.56e-36	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]
6J0T_A	1.31e-30	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]
3KF3_A	1.58e-30	99	377	7	290	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	1.62e-30	99	377	10	293	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U75_A	2.71e-30	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P05656	3.25e-37	97	516	30	471	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3	3.13e-35	97	419	22	378	Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
A2R0E0	3.13e-35	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
E1ABX2	4.26e-35	97	419	22	378	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6	4.26e-35	97	419	22	378	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE 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
1.000038	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001217_01543.