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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s4666_1V6.1 |
Family | GH18 |
Protein Properties | Length: 238 Molecular Weight: 26162.8 Isoelectric Point: 4.3743 |
Chromosome | Chromosome/Scaffold: 4666 Start: 12 End: 725 |
Description | Glycosyl hydrolase family protein with chitinase insertion domain |
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 | 1 | 238 | 0 |
ITHINYAFGDICWKGAGTTGAECQNPDIELQQGYVFNGGVIQGYPEFDPQGFEELKELKADNPGLKTLISVGGWSWSKNFSLVAADEISRRTFAGSAVQF LRAYGFDGFDIDWEYPVEGGETTNARGPQDKENFTLLVKTVREALDAAGQEDGKYYLLTIASGQGDNFTVNADYANSVQYLDFINIMTYDYNGTWQTEAA HNAPLYYDPNNKTASAKRFNAAGGLQGHLKGGVPNYKL |
Full Sequence |
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Protein Sequence Length: 238 Download |
ITHINYAFGD ICWKGAGTTG AECQNPDIEL QQGYVFNGGV IQGYPEFDPQ GFEELKELKA 60 DNPGLKTLIS VGGWSWSKNF SLVAADEISR RTFAGSAVQF LRAYGFDGFD IDWEYPVEGG 120 ETTNARGPQD KENFTLLVKT VREALDAAGQ EDGKYYLLTI ASGQGDNFTV NADYANSVQY 180 LDFINIMTYD YNGTWQTEAA HNAPLYYDPN NKTASAKRFN AAGGLQGHLK GGVPNYKL 240 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam00704 | Glyco_hydro_18 | 1.0e-54 | 2 | 238 | 238 | + Glycosyl hydrolases family 18. | ||
cd02872 | GH18_chitolectin_chitotriosidase | 6.0e-58 | 2 | 238 | 242 | + This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens. | ||
COG3325 | ChiA | 8.0e-65 | 1 | 238 | 246 | + Chitinase [Carbohydrate transport and metabolism] | ||
smart00636 | Glyco_18 | 4.0e-66 | 2 | 238 | 239 | + Glyco_18 domain. | ||
cd06548 | GH18_chitinase | 3.0e-88 | 1 | 238 | 238 | + The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. |
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 | 1ITX | 0 | 1 | 238 | 38 | 299 | A Chain A, Catalytic Domain Of Chitinase A1 From Bacillus Circulans Wl- 12 |
RefSeq | NP_241782.1 | 0 | 1 | 238 | 66 | 326 | chitinase [Bacillus halodurans C-125] |
RefSeq | XP_001786722.1 | 0 | 1 | 238 | 18 | 255 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | YP_003010543.1 | 0 | 1 | 238 | 350 | 587 | glycoside hydrolase family 18 [Paenibacillus sp. JDR-2] |
RefSeq | YP_003245693.1 | 0 | 1 | 238 | 465 | 704 | Chitinase [Geobacillus sp. Y412MC10] |
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 | 1itx_A | 0 | 1 | 238 | 38 | 299 | A Chain A, Catalytic Domain Of Chitinase A1 From Bacillus Circulans Wl-12 |
PDB | 1hkk_A | 3e-34 | 48 | 238 | 52 | 239 | A Chain A, High Resoultion Crystal Structure Of Human Chitinase In Complex With Allosamidin |
PDB | 1hkm_A | 4e-34 | 48 | 238 | 52 | 239 | A Chain A, High Resoultion Crystal Structure Of Human Chitinase In Complex With Allosamidin |
PDB | 1hkj_A | 4e-34 | 48 | 238 | 52 | 239 | A Chain A, High Resoultion Crystal Structure Of Human Chitinase In Complex With Allosamidin |
PDB | 1hki_A | 4e-34 | 48 | 238 | 52 | 239 | A Chain A, Crystal Structure Of Human Chitinase In Complex With Glucoallosamidin B |
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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO536109 | 167 | 78 | 238 | 2e-37 |
GT044513 | 245 | 1 | 236 | 2e-35 |
GT043479 | 245 | 1 | 236 | 3e-35 |
GT038919 | 245 | 1 | 236 | 2e-34 |
HO536109 | 107 | 1 | 102 | 0.001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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