CAZyme Information: MGYG000003429_01761

Basic Information

• Species: CAG-873 sp004552725
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp004552725
• CAZyme ID: MGYG000003429_01761
• CAZy Family: GH32
• CAZyme Description: Levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
325	MGYG000003429_519|CGC1	35575.12	4.9931

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003429	1944366	MAG	Fiji	Oceania

• Gene Location: Start: 1892; End: 2869 Strand: -

Full Sequence      

MLAHALDHEMQFFTSTDLKHWTLASAFGKGLGCQDGVWECPDMFRLTDPTTGEQKWVLLC
NINPGGPFGGSATQYFVGEFDGTKFIPDLDANGQVPTKWMDWGKDNYATVSFFNAPEGRT
TVIGWMSNWQYAPEVPTMTYRSANTLPRDLSLFRGADGQYYMASVPSPECDALRGAVVSK
ANRKRIGTKPVTFALPADGLCEIRLTIDADRAESVDLTLSNVEGNYVKMTFDPKAATLTF
DRTHSGITDFNEQFPVNSVAPTFNADGTVSLRIFVDRASVEVFEAAGRFALTNTVFPISP
YTSLSISATGGKATITNLHVNAIKL

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	7	157	8.6e-36	0.46075085324232085

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	2.65e-69	5	152	148	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	2.16e-62	12	314	192	476	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	1.14e-60	10	287	162	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	1.64e-41	4	162	153	306	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.
pfam08244	Glyco_hydro_32C	3.31e-30	169	320	1	160	Glycosyl hydrolases family 32 C terminal. This domain corresponds to the C terminal domain of glycosyl hydrolase family 32. It forms a beta sandwich module.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ASB38314.1	3.27e-148	1	324	286	612
ANU64796.2	3.27e-148	1	324	286	612
QQR09059.1	3.27e-148	1	324	286	612
QCD36721.1	4.43e-145	1	324	288	613
QCD40830.1	1.67e-139	1	323	278	598

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	1.99e-53	8	311	192	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]
3RWK_X	5.43e-36	1	325	191	515	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]
3KF3_A	2.39e-34	1	296	168	476	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	2.46e-34	1	296	171	479	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U14_A	3.09e-34	1	296	194	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	4.65e-54	1	324	185	510	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
Q96TU3	1.54e-52	8	311	211	520	Extracellular exo-inulinase inuE OS=Aspergillus awamori OX=105351 GN=inuE PE=1 SV=1
Q76HP6	4.44e-50	8	323	211	532	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1
E1ABX2	4.44e-50	8	323	211	532	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
A2R0E0	2.34e-49	8	323	211	532	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

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003429_01761.