y
Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma03g41510.1 |
Family | GH18 |
Protein Properties | Length: 304 Molecular Weight: 32588.9 Isoelectric Point: 8.9842 |
Chromosome | Chromosome/Scaffold: 03 Start: 46946510 End: 46947812 |
Description | chitinase A |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH18 | 28 | 249 | 6.3e-30 |
IVVYWGQDESEGTLSETCNSGLYKIVNIGFLAKFGGGREPEINLAGHCDPASNGCKSLSKDIKNCQKRGIKVILSIGGGETGYSLSSANDATKVADYIWN NFLGGKSSKTRPLGDAVLDGVDFDIEVGGGESFYAVLARRLSQHSKGGGRKVYLTAAPQCPFPDEHQNGALSTGLFDFVWVQFYNNGPCQFESSDPTKFQ KSWNQWISSIRARKIYVGLPAS |
Full Sequence |
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Protein Sequence Length: 304 Download |
MGNKTAKVSI LFLLNFLGLV CSSNGGDIVV YWGQDESEGT LSETCNSGLY KIVNIGFLAK 60 FGGGREPEIN LAGHCDPASN GCKSLSKDIK NCQKRGIKVI LSIGGGETGY SLSSANDATK 120 VADYIWNNFL GGKSSKTRPL GDAVLDGVDF DIEVGGGESF YAVLARRLSQ HSKGGGRKVY 180 LTAAPQCPFP DEHQNGALST GLFDFVWVQF YNNGPCQFES SDPTKFQKSW NQWISSIRAR 240 KIYVGLPASP SPATAGSGFV PTRTLITQVL PFVKRSPKYG GVMLWDRAAD KQTGYSTNIK 300 PSV* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00598 | GH18_chitinase-like | 3.0e-10 | 28 | 212 | 199 | + 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. | ||
cd02871 | GH18_chitinase_D-like | 2.0e-11 | 50 | 302 | 301 | + 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. | ||
COG3469 | COG3469 | 5.0e-15 | 50 | 293 | 282 | + Chitinase [Carbohydrate transport and metabolism] | ||
pfam00704 | Glyco_hydro_18 | 1.0e-31 | 28 | 290 | 342 | + Glycosyl hydrolases family 18. | ||
cd02877 | GH18_hevamine_XipI_class_III | 8.0e-137 | 26 | 301 | 283 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2GSJ | 0 | 26 | 303 | 1 | 271 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
GenBank | AAB34670.1 | 0 | 26 | 303 | 1 | 274 | chitinase-B, PLC-B [Phytolacca americana=pokeweed, leaves, Peptide, 274 aa] |
EMBL | CAO78600.1 | 0 | 31 | 303 | 1 | 266 | endochitinase and N-acetylglucosamine-binding hemagglutinin precursor [Parkia platycephala] |
RefSeq | XP_002266583.1 | 0 | 1 | 303 | 1 | 297 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002320838.1 | 0 | 16 | 303 | 1 | 282 | predicted protein [Populus trichocarpa] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2gsj_A | 0 | 26 | 303 | 1 | 271 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
PDB | 2hvm_A | 0 | 26 | 303 | 1 | 273 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
PDB | 1llo_A | 0 | 26 | 303 | 1 | 273 | A Chain A, Cdna Cloning And 1.75a Crystal Structure Determination Of Ppl2, A Novel Chimerolectin From Parkia Platycephala Seeds Exhibiting Endochitinolytic Activity |
PDB | 1hvq_A | 0 | 26 | 303 | 1 | 273 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
PDB | 1kr0_A | 0 | 26 | 303 | 1 | 273 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
chitin degradation II | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12623 | EC-3.2.1.14 | chitinase |
chitin degradation II | RXN-12624 | EC-3.2.1.14 | chitinase |
chitin degradation III (carnivorous plants) | 3.2.1.14-RXN | EC-3.2.1.14 | chitinase |