| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01027012001 |
| Family | GH18 |
| Protein Properties | Length: 458 Molecular Weight: 48567.1 Isoelectric Point: 6.0774 |
| Chromosome | Chromosome/Scaffold: 15 Start: 18574235 End: 18577072 |
| Description | chitinase A |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH18 | 225 | 408 | 4.1e-24 |
| IAIYWGQNGNEGTLAETCGTGNYDFVNIAFLSTFGNGQTPMINLAGHCDPYSNGCTSLSSDINSCQAKGIKVILSIGGGAGSYYLTSKEDAGQVATYLWN NFLGGQSSSRPLGPAVLDGIDFDIEGGTNQHWDDLTTFLSGYSKKGKKVYLTAAPQCPFPDAWVGGALKTGLFDYVWVQFYNNP | |||
| Full Sequence |
|---|
| Protein Sequence Length: 458 Download |
| MEFQLGISLP ILSLVILTLA QGSEASGIAI YWGQNGNEGT LAETCATGNY DFVNLAFLST 60 FGNGRTPMIN LAGHCDPYSN GCTDLSTEIK SCQARGIKVM LSLGGGVKGK KVYLTAAPQC 120 PFPDAWVGGA LKTGLFDYVW VQFYNNPPCH GFIPVADLTS TVLPAIKGSA KCGGVMLWSK 180 YYDDQTGYSS SIKSHHTMAL QSIISLSVLS LVMLILARGS DAGGIAIYWG QNGNEGTLAE 240 TCGTGNYDFV NIAFLSTFGN GQTPMINLAG HCDPYSNGCT SLSSDINSCQ AKGIKVILSI 300 GGGAGSYYLT SKEDAGQVAT YLWNNFLGGQ SSSRPLGPAV LDGIDFDIEG GTNQHWDDLT 360 TFLSGYSKKG KKVYLTAAPQ CPFPDAWVGG ALKTGLFDYV WVQFYNNPPC HGFIPVADLT 420 STVLPAIKGS AKYGGVMLWS KYYDDQTGYS SSIKSHV* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00704 | Glyco_hydro_18 | 6.0e-12 | 28 | 103 | 78 | + Glycosyl hydrolases family 18. | ||
| pfam00704 | Glyco_hydro_18 | 7.0e-26 | 223 | 447 | 242 | + Glycosyl hydrolases family 18. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 7.0e-28 | 113 | 194 | 124 | + 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. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 2.0e-32 | 26 | 103 | 79 | + 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. | ||
| cd02877 | GH18_hevamine_XipI_class_III | 2.0e-110 | 223 | 455 | 280 | + 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 | |
|---|---|
| GO Term | Description |
| GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI40448.1 | 0 | 1 | 457 | 1 | 457 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002279147.1 | 9.99967e-42 | 21 | 116 | 21 | 114 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002279147.1 | 2.00386e-43 | 108 | 195 | 172 | 297 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002279147.1 | 0 | 218 | 457 | 21 | 298 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002279182.1 | 0 | 218 | 457 | 21 | 298 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2hvm_A | 0 | 223 | 457 | 1 | 273 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2hvm_A | 5e-32 | 27 | 107 | 2 | 82 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 2hvm_A | 5e-30 | 108 | 192 | 147 | 269 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 1llo_A | 0 | 223 | 457 | 1 | 273 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| PDB | 1llo_A | 5e-32 | 27 | 107 | 2 | 82 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt85h2- Insights Into The Structural Basis Of A Multifunctional (Iso) Flavonoid Glycosyltransferase |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
