Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.009G105100.1 |
Family | CE10 |
Protein Properties | Length: 311 Molecular Weight: 34172.8 Isoelectric Point: 6.2279 |
Chromosome | Chromosome/Scaffold: 09 Start: 9181880 End: 9183612 |
Description | carboxyesterase 13 |
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 | 34 | 304 | 0 |
TVRPSNDPHTGVQSKDTVVSQENSLSVRLFIPKIKDPSQKLPLLIYIHGGAFCIESPFSSMYHNYLTNLAHQANVIAVSVQYRRAPEHPLPIAYDDSWAA IQWVASHVNGIGVESWLNKHADFERTFLAGDSAGANIAHNMTVRAGVNGLFGVKTVGMVLAHPFFGGKEPDFFSPVIEYIFPDVKIYDDPRINPAGAGGV ELASLGCSRVLIFVAGNDGLRERGYSYYDALKKSGWSGVVEIVETEGEDHVFHLFNPDCDKAVFMMKLVVS |
Full Sequence |
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Protein Sequence Length: 311 Download |
MDSSNSTGIL HDFPPFFRVY RNGKVERITA DAETVRPSND PHTGVQSKDT VVSQENSLSV 60 RLFIPKIKDP SQKLPLLIYI HGGAFCIESP FSSMYHNYLT NLAHQANVIA VSVQYRRAPE 120 HPLPIAYDDS WAAIQWVASH VNGIGVESWL NKHADFERTF LAGDSAGANI AHNMTVRAGV 180 NGLFGVKTVG MVLAHPFFGG KEPDFFSPVI EYIFPDVKIY DDPRINPAGA GGVELASLGC 240 SRVLIFVAGN DGLRERGYSY YDALKKSGWS GVVEIVETEG EDHVFHLFNP DCDKAVFMMK 300 LVVSFINPVP * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 1.0e-10 | 48 | 184 | 146 | + 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. | ||
COG2272 | PnbA | 2.0e-11 | 30 | 184 | 169 | + Carboxylesterase type B [Lipid metabolism] | ||
pfam00135 | COesterase | 1.0e-11 | 37 | 184 | 161 | + Carboxylesterase family. | ||
COG0657 | Aes | 3.0e-30 | 9 | 291 | 298 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-52 | 77 | 287 | 228 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
Gene Ontology | |
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GO Term | Description |
GO:0008152 | metabolic process |
GO:0016787 | hydrolase activity |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABB89005.1 | 0 | 1 | 307 | 1 | 301 | CXE carboxylesterase [Malus pumila] |
EMBL | CAN61111.1 | 0 | 1 | 307 | 1 | 317 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002285064.1 | 0 | 1 | 307 | 1 | 317 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002313842.1 | 0 | 1 | 310 | 1 | 310 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330323.1 | 0 | 1 | 246 | 1 | 247 | predicted protein [Populus trichocarpa] |
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-34 | 5 | 307 | 26 | 349 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 2zsh_A | 2e-34 | 5 | 307 | 26 | 349 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 4e-32 | 9 | 307 | 22 | 348 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 4e-32 | 9 | 307 | 22 | 348 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 4e-32 | 9 | 307 | 22 | 348 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
Metabolic Pathways | |||
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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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DT478828 | 263 | 1 | 263 | 0 |
DT472516 | 241 | 1 | 241 | 0 |
CV236989 | 226 | 86 | 311 | 0 |
DT516949 | 213 | 99 | 311 | 0 |
BU868022 | 202 | 46 | 247 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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