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CAZyme Information: KIW16955.1

You are here: Home > Sequence: KIW16955.1

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 Exophiala spinifera
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
CAZyme ID KIW16955.1
CAZy Family GH5
CAZyme Description Glyco_hydro_32N domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2BED9]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
507 57109.87 5.9903
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EspiniferaCBS89968 12110 N/A 61 12049
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.26:14 3.2.1.7:6 3.2.1.153:2 3.2.1.80:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 16 316 2.9e-89 0.9692832764505119

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
350134 GH32_Inu-like 4.44e-143 21 312 1 288
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.
224536 SacC 9.06e-110 8 474 25 458
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
214757 Glyco_32 3.66e-101 16 465 1 437
Glycosyl hydrolases family 32.
395193 Glyco_hydro_32N 5.74e-91 16 315 1 299
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 1.83e-65 22 313 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      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.54e-125 6 478 4 482
5.41e-125 12 478 17 486
5.58e-125 9 477 17 482
2.23e-124 9 477 17 482
1.03e-121 11 477 16 480

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.06e-121 3 478 1 480
Chain A, Invertase [Schwanniomyces occidentalis],3KF3_B Chain B, Invertase [Schwanniomyces occidentalis]
1.16e-121 3 478 4 483
Chain A, Invertase [Schwanniomyces occidentalis],3KF5_B Chain B, Invertase [Schwanniomyces occidentalis]
1.86e-120 3 478 27 506
Chain A, Fructofuranosidase [Schwanniomyces occidentalis],3U75_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],3U75_C Chain C, Fructofuranosidase [Schwanniomyces occidentalis],3U75_D Chain D, Fructofuranosidase [Schwanniomyces occidentalis]
3.71e-120 3 478 27 506
Chain A, Fructofuranosidase [Schwanniomyces occidentalis],3U14_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S1T_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_A Chain A, Fructofuranosidase [Schwanniomyces occidentalis],6S2B_B Chain B, Fructofuranosidase [Schwanniomyces occidentalis]
1.91e-113 12 476 39 526
The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042],6J0T_B The crystal structure of exoinulinase INU1 [Kluyveromyces marxianus DMKU3-1042]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.91e-126 9 477 17 482
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
7.90e-125 9 477 17 482
Extracellular exo-inulinase inuE OS=Meyerozyma guilliermondii OX=4929 PE=1 SV=3
9.48e-121 12 482 28 524
Invertase OS=Wickerhamomyces anomalus OX=4927 GN=INV1 PE=3 SV=1
4.61e-114 12 476 35 504
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
2.68e-112 12 476 39 525
Inulinase OS=Kluyveromyces marxianus OX=4911 GN=INU1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000067 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KIW16955.1.