CAZyme Information: MGYG000000675_00637

Basic Information

• Species: Bacteroides congonensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides congonensis
• CAZyme ID: MGYG000000675_00637
• CAZy Family: GH32
• CAZyme Description: Levanase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
420	MGYG000000675_8|CGC2	47407.78	6.011

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000675	5782172	MAG	Kazakhstan	Asia

• Gene Location: Start: 65599; End: 66861 Strand: +

Full Sequence      

MRIAPWIKLGKGVLLALAVSCGLTNCHTSDASGTTDTDKFRPAYHHISPDTLEHLFSDDL
KDFYAPKVFWYAPENKWVMIVSAGKEVSFYDSGNQKDWDYMSSFGEGYGAQPCQFEYPDM
VELPVDGDMNHKKWALIVNVNPGCYFGGSGTQYFIGDFDGTKFICDNQPNVTKWLDWGKD
HYVTACLSDTGERTIIVPWMNNRQYCHIVPTGQSRTANALPRELGLYTQDGDIYLSAAPA
ADTKALRKETKKIPAFSVTKEYHIDSLLSENEGAYELSLDMVTGKAEIMGFSLFNDKGEK
VDIYLNLPEKKLVMDRTKSGIVDFGKNSSPHKMEAHERRKTISINYINDFALATWAPVRK
EDRYKLGVFVDKCSVEIFLNDGKIAMTNLVFPTEPYNRMCFYSKGGTFSVDSFNVYRLGL

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	58	233	3.1e-34	0.5631399317406144

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18622	GH32_Inu-like	2.57e-61	58	226	124	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	7.71e-56	61	407	160	474	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	6.58e-50	61	382	132	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	2.35e-36	61	234	129	305	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	3.74e-35	242	416	1	161	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
QIU96984.1	8.62e-243	1	420	1	474
QUT72081.1	1.36e-233	57	420	263	626
QUT39618.1	5.51e-233	57	420	263	626
QQA09906.1	3.17e-232	57	420	263	626
ALJ40818.1	5.19e-231	57	420	263	626

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1Y4W_A	8.17e-39	56	418	161	513	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	5.53e-35	66	394	154	479	ChainA, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
3KF5_A	5.72e-35	66	394	157	482	ChainA, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
3U14_A	7.34e-35	66	394	180	505	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]
3U75_A	4.85e-34	66	394	180	505	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	2.68e-64	61	418	168	509	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
O31411	1.86e-43	62	418	537	875	Levanase (Fragment) OS=Bacillus sp. (strain L7) OX=62626 PE=1 SV=2
A2R0E0	1.15e-38	61	406	185	520	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
E1ABX2	1.15e-38	61	406	185	520	Extracellular exo-inulinase inuE OS=Aspergillus ficuum OX=5058 GN=exoI PE=1 SV=1
Q76HP6	1.15e-38	61	406	185	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 LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000033	0.011890	0.988068	0.000007	0.000014	0.000007

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000675_00637.