CAZyme Information: PV10_07199-t45_1-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_07199-t45_1-p1
• CAZy Family: GT2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
487		54585.32	5.1179

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EmesophilaCBS40295	9237	N/A	56	9181

• Gene Location: location=KN847524:1230632-1232095(+)

Full Sequence      

MSQPKVAVSMNPLDVRNPSVDGPQGDAIPFFHEGKYHLFYLEAPALKYDQPDRGRTPWRH
IVSDNLVDWQDLGIALPLGTGDDPDIDGIWTGSLIAVDGVLHVFYTGGRRVADIPQTICH
ATSTDGVVFKKSASNPIHVPHSDWFEQRDWRDPYVFWNEEHQQYWMLITSRAREGPPGRR
GVISLSTSDDLMKWTTMREPFYAPGSTYSMECPEVFRLGGKWRLVFSRFTEYAATVYREA
DDLAGPWRTPKYPAFDGPYWYAAKSLEDSQGRRIAFGWVHDRRGFAEGGEWLWGGDMCLP
REIYVGEDDRLCVRIPSEVDAQLTSQQPLLIRHASGGTTTEWQANVAGGFSQAEIETGAL
PRSLTRLSVEVDIQDLAGGVGLALYTNQELTDGLLLFFDASSGVISLGGPTGGQEDDRLP
VPAVTNRIKARSHGKLQIDLYLRGDVLEVFVDRQVALSYRQYFNRPFTAKPYVEDGVVTF
KATLATR

Enzyme Prediction     

No EC number prediction in PV10_07199-t45_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH32	29	312	1.3e-54	0.9385665529010239

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350109	GH32_EcAec43-like	5.42e-138	25	311	1	281	Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2). This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 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). GH32 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.
350121	GH32-like	1.23e-61	30	281	15	287	Glycosyl hydrolase family 32 family protein. The GH32 family contains glycosyl hydrolase family GH32 proteins that 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). 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.
350110	GH32_FFase	5.08e-59	29	305	9	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.
214757	Glyco_32	1.61e-49	23	452	12	435	Glycosyl hydrolases family 32.
395193	Glyco_hydro_32N	8.50e-48	23	303	12	295	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBK92492.1|GH32	2.68e-105	25	478	14	476
ADK82705.1|GH32	1.46e-104	16	480	5	484
CBK83023.1|GH32	3.00e-104	25	480	14	484
QRT30151.1|GH32	2.39e-100	25	487	14	490
UOX61724.1|GH32	1.14e-97	16	480	5	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UYP_A	3.35e-25	31	402	23	389	The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_B The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_C The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_D The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_E The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8],1UYP_F The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima [Thermotoga maritima MSB8]
1W2T_A	8.32e-25	31	402	23	389	beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_B beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_C beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_D beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_E beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8],1W2T_F beta-fructosidase from Thermotoga maritima in complex with raffinose [Thermotoga maritima MSB8]
7VCO_A	2.28e-20	31	462	46	458	Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
6R3R_A	4.50e-18	25	336	40	359	First crystal structure of endo-levanase BT1760 from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron]
7BWB_A	2.33e-16	31	407	69	477	Bombyx mori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P16553|RAFD_ECOLX	5.14e-26	31	329	44	343	Raffinose invertase OS=Escherichia coli OX=562 GN=rafD PE=3 SV=1
sp|O33833|BFRA_THEMA	6.93e-25	31	402	23	389	Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1
sp|P40714|CSCA_ECOLX	5.15e-23	35	303	49	319	Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
sp|B6DXP5|1FEH_LEYCH	1.27e-19	29	316	77	380	Fructan 1-exohydrolase OS=Leymus chinensis OX=52714 GN=1-FEH PE=2 SV=1
sp|Q70XE6|6FEH_BETVU	9.48e-18	29	356	74	420	Fructan 6-exohydrolase OS=Beta vulgaris OX=161934 GN=6-FEH PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000066	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PV10_07199-t45_1-p1.