y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.001G459400.1 |
Family | CE10 |
Protein Properties | Length: 336 Molecular Weight: 38378.9 Isoelectric Point: 6.1042 |
Chromosome | Chromosome/Scaffold: 01 Start: 49355583 End: 49356811 |
Description | carboxyesterase 18 |
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 | 51 | 315 | 0 |
DKPIDGVTTTDFTIDEDRNLWFRLYNPVFRTSTTDNEVNIPVIFYFHGSGFVCMAANSKLFDDLCYRLARLLPAVIISVNYRLAPEHRYPCQYEDGFDVI KFIDISYLEVLPNHANLKHSFVAGDSAGGNLAHHMALKASKYELSNIKLNGVIAIQPFFGGEERTGSEIKLSRDPIVPMDTTDWMWRSFLPEGSNRDHQV SNVFGPNSVDISELEFPAVLVIIGGLDPLQDWQKRYCEGLKKSGKEVYLVEYDNAFHSFYLFPCV |
Full Sequence |
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Protein Sequence Length: 336 Download |
MSQNSADLPW KVRLFTSLIS FTFKVMIRRS DGSLNRLLLN FLDYKTSPSP DKPIDGVTTT 60 DFTIDEDRNL WFRLYNPVFR TSTTDNEVNI PVIFYFHGSG FVCMAANSKL FDDLCYRLAR 120 LLPAVIISVN YRLAPEHRYP CQYEDGFDVI KFIDISYLEV LPNHANLKHS FVAGDSAGGN 180 LAHHMALKAS KYELSNIKLN GVIAIQPFFG GEERTGSEIK LSRDPIVPMD TTDWMWRSFL 240 PEGSNRDHQV SNVFGPNSVD ISELEFPAVL VIIGGLDPLQ DWQKRYCEGL KKSGKEVYLV 300 EYDNAFHSFY LFPCVPEFSL FIKEVKDFMQ KQMSR* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 0.001 | 39 | 135 | 99 | + 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 | 7.0e-5 | 41 | 136 | 98 | + Carboxylesterase type B [Lipid metabolism] | ||
PRK10162 | PRK10162 | 8.0e-10 | 92 | 309 | 225 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 1.0e-36 | 8 | 328 | 326 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 3.0e-64 | 93 | 311 | 220 | + 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 |
EMBL | CAN76040.1 | 0 | 3 | 329 | 10 | 327 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268861.1 | 0 | 3 | 329 | 10 | 327 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299011.1 | 0 | 26 | 335 | 1 | 310 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523490.1 | 0 | 7 | 332 | 11 | 331 | Arylacetamide deacetylase, putative [Ricinus communis] |
RefSeq | XP_002528343.1 | 0 | 7 | 333 | 9 | 329 | Arylacetamide deacetylase, 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 | 0 | 12 | 332 | 23 | 351 | A Chain A, Solution Structure Of The Uas Domain From Human Fas- Associated Factor 1 |
PDB | 2zsh_A | 0 | 12 | 332 | 23 | 351 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 0 | 12 | 333 | 15 | 351 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 0 | 12 | 333 | 15 | 351 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 0 | 12 | 333 | 15 | 351 | 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 |
DY269018 | 336 | 3 | 333 | 0 |
DY291484 | 335 | 8 | 335 | 0 |
FC908024 | 316 | 3 | 313 | 0 |
DY262759 | 312 | 8 | 319 | 0 |
FC880573 | 300 | 36 | 335 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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