CAZyme Information: MGYG000001701_01715

Basic Information

• Species: Corynebacterium afermentans
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Mycobacteriales; Mycobacteriaceae; Corynebacterium; Corynebacterium afermentans
• CAZyme ID: MGYG000001701_01715
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
466		50694.92	4.2078

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001701	2240769	Isolate	France	Europe

• Gene Location: Start: 65195; End: 66595 Strand: -

Full Sequence      

MTVYRPELHVTAERGILEGPAGIYRTGKAAERMWNMFYQYRPTPDAPSRWGHQQSEEDAF
SWVDCNDVIVPVGGEIAVRAGSISPAGDGVDLFFTSATAAGSTIQVAHVPHVNELCSDLD
DDADLDVSGAAARLGAVVEDVAGVSNFRSPCVVPDWDADTDRDDDHDGWLMLAVSGPETA
PKPVVLTSDDGRDWKLEGVLEFEGDTGFDLDTSLVAPRIVRLRDEVDGQIRDVLFVTLER
DGKDTAVYAVGELRGHTFRVDTPFTIVDHGHDFTRPRNTTYSLAETAKLYERAYLYGFMT
NTDRAGDPTQEPNWDAEGWANALTLPRRITLQGGRLYQVPAPGLPDAVDSTDRARMWAGL
CEVAPGASVVVEVLDGDGEPGVEITHSGDQIVLDRKDGSPASAELHDDDEDNITVIVDGA
TIEVYAGGGSVVMSSRVWLNDGCSGIRTRAYNGAEIHSEWRRGYVR

Enzyme Prediction     

No EC number prediction in MGYG000001701_01715.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	9	340	2.4e-42	0.9965870307167235

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1621	SacC	1.24e-53	4	453	28	473	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
smart00640	Glyco_32	1.11e-27	9	429	1	437	Glycosyl hydrolases family 32.
pfam00251	Glyco_hydro_32N	7.55e-16	169	340	144	308	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	1.65e-15	34	331	16	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.
cd18623	GH32_ScrB-like	8.65e-13	184	333	152	289	glycoside hydrolase family 32 sucrose 6 phosphate hydrolase (sucrase). Glycosyl hydrolase family GH32 subgroup contains sucrose-6-phosphate hydrolase (sucrase, EC:3.2.1.26) among others. The enzyme 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. 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. 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
QNP94830.1	2.83e-302	1	466	1	466
AIL96690.1	1.01e-295	1	465	1	465
QNP91041.1	3.05e-269	1	465	1	462
AKV58638.1	2.84e-222	1	464	1	468
QQU83289.1	4.03e-222	1	464	1	468

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PIG_A	2.77e-08	6	454	41	501	beta-fructofuranosidasefrom Bifidobacterium longum [Bifidobacterium longum],3PIG_B beta-fructofuranosidase from Bifidobacterium longum [Bifidobacterium longum],3PIJ_A beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum],3PIJ_B beta-fructofuranosidase from Bifidobacterium longum - complex with fructose [Bifidobacterium longum]
3RWK_X	1.04e-06	4	456	28	504	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P07819	3.96e-11	4	457	28	472	Sucrose-6-phosphate hydrolase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacA PE=3 SV=2
O74642	3.25e-06	4	456	28	504	Extracellular endo-inulinase inuB OS=Aspergillus niger OX=5061 GN=inuB PE=1 SV=1
O94220	5.68e-06	4	456	28	504	Extracellular endo-inulinase inu2 OS=Aspergillus ficuum OX=5058 GN=inu2 PE=1 SV=1
O74641	9.93e-06	4	456	28	504	Extracellular endo-inulinase inuA OS=Aspergillus niger OX=5061 GN=inuA 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
1.000045	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001701_01715.