y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_034267m |
Family | GH18 |
Protein Properties | Length: 297 Molecular Weight: 31811 Isoelectric Point: 8.3141 |
Chromosome | Chromosome/Scaffold: 06089 Start: 371418 End: 372308 |
Description | chitinase A |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH18 | 26 | 244 | 1.5e-28 |
IAIYWGQNGNEGTLAETCATGKYSYVNIAFLNKFGNGQTPEINLAGHCNPATNGCTTVSNGIKSCQKQGIKVLLSLGGGIGSYTLASQADARNVADYLWN NFLGGKSSSRPLGDAVLDGIDFDIEQGSTLYWEDLARYLSAYSKPGKKVYLAAAPQCPFPDSNLGTALNTGLFDYVWVQFYNNPPCQYSSGNINNIVNSW NRWTTSVNAGRIFLGLPAA |
Full Sequence |
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Protein Sequence Length: 297 Download |
MSTKPLAVLL PLLLISLFIP SYAGGIAIYW GQNGNEGTLA ETCATGKYSY VNIAFLNKFG 60 NGQTPEINLA GHCNPATNGC TTVSNGIKSC QKQGIKVLLS LGGGIGSYTL ASQADARNVA 120 DYLWNNFLGG KSSSRPLGDA VLDGIDFDIE QGSTLYWEDL ARYLSAYSKP GKKVYLAAAP 180 QCPFPDSNLG TALNTGLFDY VWVQFYNNPP CQYSSGNINN IVNSWNRWTT SVNAGRIFLG 240 LPAAPEAAGS GYVPPNVLTS QILPEIKKSP KYGGIMLWSK FWDDKNGYSS SVLRSV* 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd06545 | GH18_3CO4_chitinase | 4.0e-8 | 47 | 289 | 263 | + The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas. | ||
COG3469 | COG3469 | 1.0e-12 | 87 | 284 | 236 | + Chitinase [Carbohydrate transport and metabolism] | ||
cd02871 | GH18_chitinase_D-like | 2.0e-16 | 47 | 291 | 293 | + 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. | ||
pfam00704 | Glyco_hydro_18 | 2.0e-34 | 24 | 283 | 345 | + Glycosyl hydrolases family 18. | ||
cd02877 | GH18_hevamine_XipI_class_III | 8.0e-141 | 24 | 292 | 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. |
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 | 1HVQ | 0 | 24 | 296 | 1 | 273 | A Chain A, Crystal Structures Of Hevamine, A Plant Defence Protein With Chitinase And Lysozyme Activity, And Its Complex With An Inhibitor |
EMBL | CAA09110.1 | 0 | 24 | 296 | 27 | 299 | chitinase [Hevea brasiliensis] |
Swiss-Prot | P23472 | 0 | 24 | 296 | 27 | 299 | CHLY_HEVBR RecName: Full=Hevamine-A; Includes: RecName: Full=Chitinase; Includes: RecName: Full=Lysozyme; Flags: Precursor |
RefSeq | XP_002331830.1 | 0 | 23 | 296 | 26 | 296 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002513612.1 | 0 | 23 | 296 | 24 | 297 | hevamine-A precursor, putative [Ricinus communis] |
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 | 2hvm_A | 0 | 24 | 296 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1llo_A | 0 | 24 | 296 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A IN COMPLEX WITH TETRA-Nag |
PDB | 1hvq_A | 0 | 24 | 296 | 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 | 24 | 296 | 1 | 273 | A Chain A, Hevamine Mutant D125aY183F IN COMPLEX WITH TETRA-Nag |
PDB | 1kr1_A | 0 | 24 | 296 | 1 | 273 | A Chain A, Hevamine Mutant D125aE127A 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 |