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CAZyme Information: RL4_JR_08343-RA-p1

You are here: Home > Sequence: RL4_JR_08343-RA-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 Raffaelea lauricola
Lineage Ascomycota; Sordariomycetes; ; Ophiostomataceae; Raffaelea; Raffaelea lauricola
CAZyme ID RL4_JR_08343-RA-p1
CAZy Family GH78
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
615 JACBXF010000002|CGC6 66723.25 4.8593
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_RlauricolaRL4 10461 N/A 146 10315
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.26:10 2.4.1.100:6 2.4.1.-:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 46 393 2.5e-41 0.962457337883959

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
350133 GH32_XdINV-like 3.66e-128 52 392 1 335
glycoside hydrolase family 32 protein such as Xanthophyllomyces dendrorhous beta-fructofuranosidase (Inv;Xd-INV;XdINV). This subfamily of glycosyl hydrolase family GH32 includes fructan:fructan 1-fructosyltransferase (FT, EC 2.4.1.100) and beta-fructofuranosidase (invertase or Inv, EC 3.2.1.26), 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. Xanthophyllomyces dendrorhous beta-fructofuranosidase (XdINV) also catalyzes the synthesis of fructooligosaccharides (FOS, a beneficial prebiotic), producing neo-FOS, making it an interesting biotechnology target. Structural studies show plasticity of its active site, having a flexible loop that is essential in binding sucrose and beta(2-1)-linked oligosaccharide, making it a valuable biocatalyst to produce novel bioconjugates. 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 3.47e-47 46 568 1 436
Glycosyl hydrolases family 32.
350110 GH32_FFase 2.11e-45 52 392 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.
400517 Glyco_hydro_32C 5.16e-26 452 605 20 162
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.
395193 Glyco_hydro_32N 5.59e-23 67 392 20 297
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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 615 1 618
1.27e-315 1 615 1 618
3.09e-309 1 615 1 618
7.21e-308 1 615 1 618
7.21e-308 1 615 1 618

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.78e-294 20 615 5 604
Aspergillus kawachii beta-fructofuranosidase complexed with glycerol [Aspergillus luchuensis IFO 4308],5XH9_A Aspergillus kawachii beta-fructofuranosidase [Aspergillus luchuensis IFO 4308],5XHA_A Aspergillus kawachii beta-fructofuranosidase complexed with fructose [Aspergillus luchuensis IFO 4308]
5.93e-249 20 614 4 634
Crystal structure of fructosyltransferase (wild-type) from A. japonicus [Aspergillus japonicus],3LFI_A Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus],3LFI_B Crystal structure of fructosyltransferase (wild-type) from A. japonicus in complex with glucose [Aspergillus japonicus]
9.69e-248 20 614 4 634
Crystal Structure of A. japonicus CB05 [Aspergillus japonicus],3LDR_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with 1-Kestose [Aspergillus japonicus],3LEM_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with Nystose [Aspergillus japonicus],3LIG_A Crystal structure of fructosyltransferase (D191A) from A. japonicus [Aspergillus japonicus],3LIH_A Crystal structure of fructosyltransferase (D191A) from A. japonicus in complex with raffinose [Aspergillus japonicus]
2.51e-79 20 614 44 641
Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],5ANN_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma]
2.51e-79 20 614 44 641
Chain A, Beta-fructofuranosidase [Phaffia rhodozyma],6S82_B Chain B, Beta-fructofuranosidase [Phaffia rhodozyma]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.49e-07 42 189 20 167
Extracellular exo-inulinase OS=Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324) OX=294746 GN=PGUG_02777 PE=1 SV=2
5.49e-07 42 189 20 167
Extracellular exo-inulinase inuE OS=Meyerozyma guilliermondii OX=4929 PE=1 SV=3
3.20e-06 30 210 33 210
Invertase OS=Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) OX=284590 GN=INV1 PE=3 SV=1
3.92e-06 42 210 35 195
Invertase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=INV PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999383 0.000662

TMHMM  Annotations      help

There is no transmembrane helices in RL4_JR_08343-RA-p1.