| Basic Information | |
|---|---|
| Species | Brassica rapa |
| Cazyme ID | Bra001454 |
| Family | GH19 |
| Protein Properties | Length: 472 Molecular Weight: 52170.1 Isoelectric Point: 7.6485 |
| Chromosome | Chromosome/Scaffold: 03 Start: 16439896 End: 16443013 |
| Description | basic chitinase |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH19 | 89 | 320 | 0 |
| GIISRDQFYKMLKHMNDNACPARGFFTYDAFITAAKFFPSFGNTGDLATRKKEIAAFFGQTSHETTGGWTDAPDGANTWGYCFKDEIGKSNPYCDSNNLE WPCAPGQFYYGRGPMMLSWNYNYGQCGRDLGLDLLRRPAIASSDPVIAFETAIWFWMTPQAPKPSCHDVITDQWQPSAADISAGRLPGYGVITNIINGGL ECAGRNVAQVEDRISFYTRYCGMFGVDPGTVL | |||
| Full Sequence |
|---|
| Protein Sequence Length: 472 Download |
| MKTYLLLLLI FSLLLSYSSG QQCGRQAQGA LCPNGLCCSE YGWCGTTEAY CGRGCQSQCT 60 PTPPTPTPTP PSPTPPRPTP PGPSGDLSGI ISRDQFYKML KHMNDNACPA RGFFTYDAFI 120 TAAKFFPSFG NTGDLATRKK EIAAFFGQTS HETTGGWTDA PDGANTWGYC FKDEIGKSNP 180 YCDSNNLEWP CAPGQFYYGR GPMMLSWNYN YGQCGRDLGL DLLRRPAIAS SDPVIAFETA 240 IWFWMTPQAP KPSCHDVITD QWQPSAADIS AGRLPGYGVI TNIINGGLEC AGRNVAQVED 300 RISFYTRYCG MFGVDPGTVL GRLPGTTVYR NMKQYPEAYT YNGIVIVRVD APIYFANISY 360 IKDSCHIHRL KRRGSLERTL AVSNPNKEVL LTLARSGIVE LIGKEWYFVR VHDAVQVCLH 420 YVESKNQTPT NVEESSSSSL WRRCNAKNSS HTEVEPDSKL VLKEPLLFND K* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam00187 | Chitin_bind_1 | 1.0e-17 | 22 | 59 | 38 | + Chitin recognition protein. | ||
| cd06921 | ChtBD1_GH19_hevein | 1.0e-17 | 21 | 59 | 39 | + Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl hydrolases or with barwin domains. This subfamily includes Hevein, a major IgE-binding allergen in natural rubber latex. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements. | ||
| TIGR00815 | sulP | 4.0e-25 | 316 | 414 | 136 | + high affinity sulphate transporter 1. The SulP family is a large and ubiquitous family with over 30 sequenced members derived from bacteria, fungi, plants and animals. Many organisms including Bacillus subtilis, Synechocystis sp, Saccharomyces cerevisiae, Arabidopsis thaliana and Caenorhabditis elegans possess multiple SulP family paralogues. Many of these proteins are functionally characterized, and all are sulfate uptake transporters. Some transport their substrate with high affinities, while others transport it with relatively low affinities. Most function by SO42- :H+symport, but SO42- :HCO3- antiport has been reported for the rat protein (spP45380). The bacterial proteins vary in size from 434 residues to 566 residues with one exception, a Mycobacterium tuberculosis protein with 784 residues. The eukaryotic proteins vary in size from 611 residues to 893 residues with one exception, a protein designated "early nodulin 70 protein" from Glycine max which is reported to be of 485 residues. Thus, the eukaryotic proteins are almost without exception larger than the prokaryotic proteins. These proteins exhibit 10-13 putative transmembrane a-helical spanners (TMSs) depending on the protein. The phylogenetic tree for the SulP family reveals five principal branches. Three of these are bacterial specific as follows: one bears a single protein from M. tuberculosis; a second bears two proteins, one from M. tuberculosis, the other from Synechocystis sp, and the third bears all remaining prokaryotic proteins. The remaining two clusters bear only eukaryotic proteins with the animal proteins all localized to one branch and the plant and fungal proteins localized to the other. The generalized transport reactions catalyzed by SulP family proteins are: (1) SO42- (out) + nH+ (out) --> SO42- (in) + nH+ (in). (2) SO42- (out) + nHCO3- (in) SO42- (in) + nHCO3- (out) [Transport and binding proteins, Anions]. | ||
| pfam00182 | Glyco_hydro_19 | 1.0e-124 | 90 | 317 | 228 | + Chitinase class I. | ||
| cd00325 | chitinase_glyco_hydro_19 | 1.0e-125 | 91 | 321 | 231 | + Glycoside hydrolase family 19 chitinase domain. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases but they are smaller in size due to certain deletions. Despite any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the procaryotic/eucaryotic divergence. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004568 | chitinase activity |
| GO:0006032 | chitin catabolic process |
| GO:0008061 | chitin binding |
| GO:0016998 | cell wall macromolecule catabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2Z37 | 0 | 86 | 320 | 1 | 235 | A Chain A, Crystal Structure Of Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
| PDB | 2Z38 | 0 | 85 | 320 | 3 | 238 | A Chain A, Crystal Structure Of Chloride Bound Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
| PDB | 2Z39 | 0 | 85 | 320 | 2 | 237 | A Chain A, Crystal Structure Of Brassica Juncea Chitinase Catalytic Module Glu234ala Mutant (Bjchi3-E234a) |
| GenBank | AAF02299.1 | 0.0000000000003 | 1 | 60 | 1 | 62 | AF098302_1 chitinase [Brassica juncea] |
| GenBank | AAF02299.1 | 0 | 22 | 320 | 73 | 380 | AF098302_1 chitinase [Brassica juncea] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2z38_A | 0 | 85 | 320 | 3 | 238 | A Chain A, Crystal Structure Of Chloride Bound Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
| PDB | 2z37_D | 0 | 86 | 320 | 1 | 235 | A Chain A, Crystal Structure Of Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
| PDB | 2z37_C | 0 | 86 | 320 | 1 | 235 | A Chain A, Crystal Structure Of Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
| PDB | 2z37_B | 0 | 86 | 320 | 1 | 235 | A Chain A, Crystal Structure Of Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
| PDB | 2z37_A | 0 | 86 | 320 | 1 | 235 | A Chain A, Crystal Structure Of Brassica Juncea Chitinase Catalytic Module (Bjchi3) |
| 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 |
