| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_006786m |
| Family | CE10 |
| Protein Properties | Length: 476 Molecular Weight: 52725.1 Isoelectric Point: 8.0726 |
| Chromosome | Chromosome/Scaffold: 03245 Start: 162841 End: 168304 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CE10 | 169 | 464 | 0 |
| YRGYSPSVDNSRKLPIMLQFHGGGWVSGSKDSVANDLFCRRIARFCDVIVVAVGYRLAPENRYPAAFEDGMKVLNWLAKQANLAECSKSMGNAKGGTEFK KADLQRHVVDAFGASMVEPWLAAHGDPSRCILLGVSCGANIADYVARKAVEAGKLLDPVKVVAQVLMYPFFIGSVPTHSEIKLANSYFYDKQMCMLAWKL FLPEEEFSLDHPAANPLVPGRGPPLKLMPPTLTIVAEHDWMRDRAIAYSEELRKVNVDAPVLEYKDAVHEFATLDMLLKTPQAQACAEDIAIWVKK | |||
| Full Sequence |
|---|
| Protein Sequence Length: 476 Download |
| MPSVAVKLYS VFFKLLLKHR LQNRIQTQHD DSDPFGVTTR PEESVAAPNP SFADGFATKD 60 IHIDAFTSLS VRIFLPESAL NPPEPDSRPP SRIKSKSNLK RLDLDQNDNT TGLIANRHNQ 120 SWRRNSVGPS ATNIITGSSL REESRRNSYG GSNDVEAFNF KSDGVGGVYR GYSPSVDNSR 180 KLPIMLQFHG GGWVSGSKDS VANDLFCRRI ARFCDVIVVA VGYRLAPENR YPAAFEDGMK 240 VLNWLAKQAN LAECSKSMGN AKGGTEFKKA DLQRHVVDAF GASMVEPWLA AHGDPSRCIL 300 LGVSCGANIA DYVARKAVEA GKLLDPVKVV AQVLMYPFFI GSVPTHSEIK LANSYFYDKQ 360 MCMLAWKLFL PEEEFSLDHP AANPLVPGRG PPLKLMPPTL TIVAEHDWMR DRAIAYSEEL 420 RKVNVDAPVL EYKDAVHEFA TLDMLLKTPQ AQACAEDIAI WVKKYISFRG HEFSY* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 2.0e-5 | 172 | 307 | 147 | + Esterases and lipases (includes fungal lipases, cholinesterases, etc.) These enzymes act on carboxylic esters (EC: 3.1.1.-). The catalytic apparatus involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.These catalytic residues are responsible for the nucleophilic attack on the carbonyl carbon atom of the ester bond. In contrast with other alpha/beta hydrolase fold family members, p-nitrobenzyl esterase and acetylcholine esterase have a Glu instead of Asp at the active site carboxylate. | ||
| pfam00135 | COesterase | 3.0e-6 | 172 | 227 | 57 | + Carboxylesterase family. | ||
| PRK10162 | PRK10162 | 4.0e-7 | 189 | 250 | 62 | + acetyl esterase; Provisional | ||
| COG0657 | Aes | 3.0e-38 | 163 | 459 | 297 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 7.0e-63 | 185 | 440 | 256 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | NP_001030781.1 | 0 | 1 | 475 | 1 | 428 | hydrolase [Arabidopsis thaliana] |
| RefSeq | NP_189367.1 | 0 | 1 | 475 | 1 | 460 | hydrolase [Arabidopsis thaliana] |
| RefSeq | XP_002267088.1 | 0 | 1 | 475 | 1 | 464 | PREDICTED: hypothetical protein isoform 1 [Vitis vinifera] |
| RefSeq | XP_002267130.1 | 0 | 1 | 475 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
| RefSeq | XP_002526925.1 | 0 | 1 | 475 | 1 | 472 | conserved hypothetical protein [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2zsi_A | 4e-32 | 182 | 442 | 113 | 331 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
| PDB | 2zsh_A | 4e-32 | 182 | 442 | 113 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 3e-30 | 182 | 442 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 3e-30 | 182 | 442 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 3e-30 | 182 | 442 | 112 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| formononetin biosynthesis | RXN-3284 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| formononetin biosynthesis | RXN-3625 | - | 2,7-dihydroxy-4'-methoxyisoflavanone dehydratase |
| isoflavonoid biosynthesis I | RXN-3284 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| isoflavonoid biosynthesis II | RXN-3303 | EC-4.2.1.105 | 2-hydroxyisoflavanone dehydratase |
| isoflavonoid biosynthesis II | RXN-5502 | - | 2,7,5-trihydroxy-4'-methoxyisoflavanone dehydratase |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| ES789976 | 379 | 105 | 476 | 0 |
| EB438845 | 279 | 200 | 476 | 0 |
| JK515504 | 267 | 211 | 476 | 0 |
| DR937200 | 272 | 206 | 476 | 0 |
| DR937200 | 20 | 194 | 213 | 5.7 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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