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CAZyme Information: ORE03013.1

You are here: Home > Sequence: ORE03013.1

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 Rhizopus microsporus
Lineage Mucoromycota; Mucoromycetes; ; Rhizopodaceae; Rhizopus; Rhizopus microsporus
CAZyme ID ORE03013.1
CAZy Family GH109
CAZyme Description glycoside hydrolase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
549 KV922022|CGC2 59211.54 9.2542
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_RmicrosporusATCC52814 11554 N/A 58 11496
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.14:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH18 29 264 2.1e-25 0.668918918918919

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
119356 GH18_hevamine_XipI_class_III 2.35e-122 29 312 3 278
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.
395573 Glyco_hydro_18 5.28e-26 29 300 2 267
Glycosyl hydrolases family 18.
119350 GH18_chitinase_D-like 1.72e-18 29 299 3 303
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
226000 Chi1 2.32e-13 95 293 86 302
Chitinase [Carbohydrate transport and metabolism].
119349 GH18_chitinase-like 1.43e-11 29 296 1 208
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.03e-158 19 544 22 562
8.06e-143 25 544 27 533
1.24e-139 27 544 29 535
1.82e-117 16 549 16 493
1.81e-101 28 318 25 326

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.14e-84 28 316 7 287
ScCTS1_apo crystal structure [Saccharomyces cerevisiae],2UY3_A ScCTS1_8-chlorotheophylline crystal structure [Saccharomyces cerevisiae],2UY4_A ScCTS1_acetazolamide crystal structure [Saccharomyces cerevisiae],2UY5_A ScCTS1_kinetin crystal structure [Saccharomyces cerevisiae],4TXE_A ScCTS1 in complex with compound 5 [Saccharomyces cerevisiae]
3.95e-59 29 316 3 271
cDNA cloning and 1.75A crystal structure determination of PPL2, a novel chimerolectin from Parkia platycephala seeds exhibiting endochitinolytic activity [Parkia platycephala]
7.18e-55 29 293 3 255
CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR [Hevea brasiliensis],1LLO_A Chain A, HEVAMINE [Hevea brasiliensis],2HVM_A Hevamine A At 1.8 Angstrom Resolution [Hevea brasiliensis]
1.00e-54 29 293 3 257
Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum],4TOQ_B Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum],4TOQ_C Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum],4TOQ_D Crystal structure of class III chitinase from pomegranate provides the insight into its metal storage capacity [Punica granatum]
4.00e-53 29 293 3 255
Chain A, Hevamine A [Hevea brasiliensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.43e-143 25 544 27 533
Chitinase 1 OS=Rhizopus oligosporus OX=4847 GN=CHI1 PE=1 SV=1
2.21e-140 27 544 29 535
Chitinase 2 OS=Rhizopus oligosporus OX=4847 GN=CHI2 PE=1 SV=1
3.23e-118 16 549 16 493
Chitinase 1 OS=Rhizopus niveus OX=4844 GN=CHI1 PE=3 SV=1
1.25e-90 7 323 3 317
Chitinase 3 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=CHT3 PE=1 SV=2
4.13e-81 8 316 9 308
Endochitinase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=CTS1 PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000283 0.999671 CS pos: 21-22. Pr: 0.9796

TMHMM  Annotations      help

There is no transmembrane helices in ORE03013.1.