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CAZyme Information: QRC91113.1

You are here: Home > Sequence: QRC91113.1

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 Parastagonospora nodorum
Lineage Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
CAZyme ID QRC91113.1
CAZy Family AA3
CAZyme Description Levanase [Source:UniProtKB/TrEMBL;Acc:A0A7U2ESB5]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
520 56281.50 4.5055
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PnodorumSN15 17580 321614 132 17448
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in QRC91113.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH32 27 338 1e-66 0.9658703071672355

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
350134 GH32_Inu-like 7.86e-114 34 335 3 288
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 2.75e-87 23 516 29 483
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism].
214757 Glyco_32 6.71e-86 27 480 1 436
Glycosyl hydrolases family 32.
395193 Glyco_hydro_32N 7.70e-69 27 349 1 308
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 1.92e-47 34 334 2 279
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
0.0 1 520 1 520
7.42e-264 5 516 19 528
2.74e-263 9 516 22 528
7.28e-263 9 516 23 529
4.51e-262 9 516 22 528

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.17e-72 26 506 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]
1.23e-72 26 506 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]
6.64e-72 26 506 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]
1.37e-61 23 506 8 501
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]
2.86e-44 23 338 8 316
Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_B Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_C Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_D Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_E Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_F Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_G Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C],4EQV_H Structure of Saccharomyces cerevisiae invertase [Saccharomyces cerevisiae S288C]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.40e-96 23 506 44 499
Levanbiose-producing levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=levB PE=1 SV=1
2.68e-87 37 350 1 300
Levanbiose-producing levanase (Fragment) OS=Geobacillus stearothermophilus OX=1422 GN=levB PE=1 SV=2
4.27e-76 23 506 35 497
Levanase OS=Bacillus subtilis (strain 168) OX=224308 GN=sacC PE=1 SV=1
1.03e-61 23 506 27 520
Extracellular exo-inulinase inuE OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=inuE PE=2 SV=1
5.43e-61 23 506 27 520
Extracellular exo-inulinase inuE OS=Aspergillus niger OX=5061 GN=inuE PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000206 0.999752 CS pos: 20-21. Pr: 0.9691

TMHMM  Annotations      help

There is no transmembrane helices in QRC91113.1.