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CAZyme Information: FOYG_11828-t42_1-p1

You are here: Home > Sequence: FOYG_11828-t42_1-p1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Fusarium oxysporum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
CAZyme ID FOYG_11828-t42_1-p1
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
391 43116.12 6.9801
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FoxysporumNRRL32931 17642 660029 362 17280
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.26:1 3.2.1.26:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 220 384 1.2e-35 0.590443686006826
CBM38 34 162 1.6e-35 0.9844961240310077

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
224536 SacC 1.59e-44 207 389 20 215
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
395193 Glyco_hydro_32N 7.26e-39 220 389 1 184
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.
350137 GH32_BfrA-like 1.32e-38 226 383 1 176
glycoside hydrolase family 32 protein such as Thermotoga maritima invertase (BfrA or Tm1414). This subfamily of glycosyl hydrolase family GH32 includes beta-fructosidase (invertase, EC 3.2.1.26) that 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. 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.
350110 GH32_FFase 4.99e-38 226 389 1 176
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 1.78e-36 220 389 1 188
Glycosyl hydrolases family 32.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.35e-278 1 391 1 411
7.78e-235 1 391 1 411
1.57e-234 1 391 1 411
2.91e-172 5 391 14 422
1.59e-135 6 389 14 428

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.86e-24 216 382 3 181
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]
5.86e-24 216 382 3 181
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]
5.53e-23 192 381 5 204
Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara],7VCP_A Chain A, Sucrose-6-phosphate hydrolase [Frischella perrara]
5.76e-19 216 391 49 232
Bombyx mori GH32 beta-fructofuranosidase BmSUC1 [Bombyx mori]
8.68e-19 217 382 41 224
beta-fructofuranosidase from 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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.26e-25 217 385 26 207
Sucrose-6-phosphate hydrolase OS=Escherichia coli OX=562 GN=cscA PE=3 SV=1
2.54e-24 216 382 3 181
Beta-fructosidase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=bfrA PE=1 SV=1
1.05e-21 217 387 30 217
Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 / NCIMB 8938 / NRRL B-806 / ZM1) OX=555217 GN=sacA PE=3 SV=1
6.35e-21 217 387 30 217
Sucrose-6-phosphate hydrolase OS=Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) OX=264203 GN=sacA PE=1 SV=1
3.92e-20 205 389 24 219
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.002376 0.997605 CS pos: 16-17. Pr: 0.9513

TMHMM  Annotations      help

There is no transmembrane helices in FOYG_11828-t42_1-p1.