CAZyme Information: FVEG_10082-t26_1-p1

Basic Information

• Species: Fusarium verticillioides
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium verticillioides
• CAZyme ID: FVEG_10082-t26_1-p1
• CAZy Family: GH3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
535	CM000586.1|CGC5	59156.74	4.4549

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fverticillioides7600	16240	334819	371	15869

• Gene Location: location=CM000586.1:2467785-2469392(+)

Full Sequence      

MLRFPKLVSQRLVIRRFSFLLSIFYASAVLATPISTRPSYHITPEKNWMSDPQRPFFLGD
EWHFYYLYNSNFDISNPGSGGTEWYHITSTDMVHWTRRGVVMEKYKPNPPSGIILGDIET
GSAVVDVNNTAGFGQNAVVAIVTQMADGVQQQSLFYSTDNGYSFSPYESNPVMPNPSSTS
KPAFRDPKIFWDDKQGHWVMSLAEGDKIGFYTSTDLKTWAYMSEFKPENTGVDLGTLECP
DLYQIDLDGDSTKRTWILAMGANGYRYNRTTGTAYWTGNWDGNGFTATESYPQWMDDGPD
FYATVSWENPDNKYGSRYAIAWMNNWEYAASLPYYADFAGQQSLVREIKLKTINGSPTLV
SIPIEGYGEIVGSPKSVSDKTITTDPASASLPGGMEQGAYIIHATISKNDGDKGNEVRFV
IRFDGDFSTTVGYDFVRSQAFLVRDSDGSATDSMADGPKNVYDTVRTASNPSGGSTVKLV
IYVDWNSVEIVVNDGVAVLSGLIYPNEGANGVQVVSDTGSLTLASFSYAACESIY

Enzyme Prediction     

No EC number prediction in FVEG_10082-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	41	355	4e-72	0.9761092150170648

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350134	GH32_Inu-like	1.07e-129	46	350	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.
214757	Glyco_32	1.40e-100	41	495	1	437	Glycosyl hydrolases family 32.
224536	SacC	9.39e-98	37	529	29	483	Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
395193	Glyco_hydro_32N	2.16e-85	41	355	1	302	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.
350110	GH32_FFase	6.69e-58	47	350	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QPC72046.1|GH32	0.0	1	534	1	534
CZS72073.1|GH32	0.0	4	534	3	533
CEF85116.1|GH32	0.0	4	534	3	533
CCT73859.1|GH32	0.0	1	535	1	535
QGI86832.1|GH32	0.0	1	535	1	535

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4FFF_A	5.16e-76	40	519	4	466	Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_B Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_C Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens],4FFF_D Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens [Paenarthrobacter ureafaciens]
4FFG_A	5.43e-76	40	519	4	466	Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_B Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_C Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens],4FFG_D Crystal Structure of Levan Fructotransferase from Arthrobacter ureafaciens in complex with DFA-IV [Paenarthrobacter ureafaciens]
4FFH_A	2.95e-75	40	519	4	466	Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_B Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_C Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFH_D Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with sucrose [Paenarthrobacter ureafaciens],4FFI_A Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_B Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_C Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens],4FFI_D Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose [Paenarthrobacter ureafaciens]
1Y4W_A	8.47e-67	37	520	8	502	Crystal structure 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	2.64e-50	37	525	29	507	First crystal 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
sp|O07003|LEVB_BACSU	8.28e-102	37	535	44	515	Levanbiose-producing levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=levB PE=1 SV=1
sp|P94469|LEVB_GEOSE	2.48e-92	51	382	1	318	Levanbiose-producing levanase (Fragment) OS=Geobacillus stearothermophilus OX=1422 GN=levB PE=1 SV=2
sp|P05656|SACC_BACSU	3.42e-83	37	535	35	513	Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
sp|A2R0E0|INUE_ASPNC	6.21e-68	37	520	27	521	Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
sp|Q76HP6|INUE_ASPNG	1.21e-67	37	520	27	521	Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.009213	0.990766	CS pos: 31-32. Pr: 0.9573

TMHMM  Annotations     

Start	End
12	34