| Basic Information | |
|---|---|
| Species | Populus trichocarpa |
| Cazyme ID | Potri.T111700.1 |
| Family | CE10 |
| Protein Properties | Length: 389 Molecular Weight: 42882.3 Isoelectric Point: 8.4469 |
| Chromosome | Chromosome/Scaffold: 172 Start: 12435 End: 14642 |
| Description | alpha/beta-Hydrolases superfamily protein |
| 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 |
| CE10 | 47 | 378 | 0 |
| AASNPSFTDGVATKDIRANPYSSLSLRIFLPDTAVSSSLASSYQIPNYGGYSPVEGRSHRKLPVMLQFHGGGFVSGSNESVGNDAFCRRIAKLCDVIVVA VGYRLAPETKYPGAFEDGFKVLNWLAKQSNLAVCGRLGAQNHIFDSFGASMVEPWLAAHGDTSRCVLLGVSSGANIADYVARKAVEAGKRLDPVKVVAQI LMFPFFIGRTPTHSEIKLASTYFYDKTMCKLAWKLFLPREEFNLDHPAANPLIAGRQPPLKCMPPTITVVAEHDFMRDRAIAYSEELRKVNVDAPLLDYK DAVHEFATLDVLLQTPQAQACAEDVSIWVKKY | |||
| Full Sequence |
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| Protein Sequence Length: 389 Download |
| MPSLMVKLYS VIFKYQQKHL LQGLIETPES NKSNPFGITS RPHESIAASN PSFTDGVATK 60 DIRANPYSSL SLRIFLPDTA VSSSLASSYQ IPNYGGYSPV EGRSHRKLPV MLQFHGGGFV 120 SGSNESVGND AFCRRIAKLC DVIVVAVGYR LAPETKYPGA FEDGFKVLNW LAKQSNLAVC 180 GRLGAQNHIF DSFGASMVEP WLAAHGDTSR CVLLGVSSGA NIADYVARKA VEAGKRLDPV 240 KVVAQILMFP FFIGRTPTHS EIKLASTYFY DKTMCKLAWK LFLPREEFNL DHPAANPLIA 300 GRQPPLKCMP PTITVVAEHD FMRDRAIAYS EELRKVNVDA PLLDYKDAVH EFATLDVLLQ 360 TPQAQACAED VSIWVKKYIS LRGHEFSY* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK10162 | PRK10162 | 7.0e-7 | 95 | 176 | 86 | + acetyl esterase; Provisional | ||
| cd00312 | Esterase_lipase | 2.0e-7 | 97 | 220 | 133 | + 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 | 5.0e-9 | 97 | 225 | 142 | + Carboxylesterase family. | ||
| COG0657 | Aes | 1.0e-32 | 97 | 356 | 261 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 2.0e-60 | 111 | 353 | 243 | + 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 | XP_002267130.1 | 0 | 1 | 388 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
| RefSeq | XP_002272331.1 | 0 | 1 | 388 | 1 | 395 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002311735.1 | 0 | 1 | 388 | 1 | 387 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002311736.1 | 0 | 1 | 388 | 1 | 388 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002515006.1 | 0 | 1 | 388 | 1 | 391 | catalytic, 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 | 2zsi_A | 2e-36 | 47 | 355 | 62 | 331 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
| PDB | 2zsh_A | 2e-36 | 47 | 355 | 62 | 331 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 1e-31 | 108 | 335 | 112 | 310 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 1e-31 | 108 | 335 | 112 | 310 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 1e-31 | 108 | 335 | 112 | 310 | 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 | ||||
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| Hit | Length | Start | End | EValue |
| DT485343 | 269 | 121 | 389 | 0 |
| ES789976 | 384 | 29 | 389 | 0 |
| EB438845 | 279 | 126 | 389 | 0 |
| GO362523 | 303 | 96 | 379 | 0 |
| JK515504 | 267 | 137 | 389 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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