y
Basic Information | |
---|---|
Species | Populus trichocarpa |
Cazyme ID | Potri.008G180500.1 |
Family | CE10 |
Protein Properties | Length: 388 Molecular Weight: 42676.1 Isoelectric Point: 7.9127 |
Chromosome | Chromosome/Scaffold: 08 Start: 12309977 End: 12312061 |
Description | carboxyesterase 16 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
CE10 | 48 | 380 | 0 |
IAASNPSFTDGVATKDIHVDPISSLSLRIFLPDTAITSPLPSTHDYGGYLPPPGKFHRKLPVMLQFHGGGFVSGSNESVGNDAFCRRIAKLCDVIVVAVG YRLAPETKYPGAFEDGFKVLNWLAKQANLAACGRLDSQSHIFDSFGASMVEPWLAAHGDPSRCVLLGVSSGANIADYLARRAVEAGKLLDPVKVVAQVLM FPFFIGSTPTHSEVKLANSYFYDKAMCKLAWKLFLPKEQFSLDHPAANPLTAGRQPPLKYMPPTLTIVAEHDFMRDRAISYSEELRKVNVDAPVLDYKDT VHEFATLDVLLHTPQARVCAEDVTIWVKKYISL |
Full Sequence |
---|
Protein Sequence Length: 388 Download |
MPNLIVKLYS VFFKYQQKHL LQTLSLSSLT DQKPTNSFGV SSGPHESIAA SNPSFTDGVA 60 TKDIHVDPIS SLSLRIFLPD TAITSPLPST HDYGGYLPPP GKFHRKLPVM LQFHGGGFVS 120 GSNESVGNDA FCRRIAKLCD VIVVAVGYRL APETKYPGAF EDGFKVLNWL AKQANLAACG 180 RLDSQSHIFD SFGASMVEPW LAAHGDPSRC VLLGVSSGAN IADYLARRAV EAGKLLDPVK 240 VVAQVLMFPF FIGSTPTHSE VKLANSYFYD KAMCKLAWKL FLPKEQFSLD HPAANPLTAG 300 RQPPLKYMPP TLTIVAEHDF MRDRAISYSE ELRKVNVDAP VLDYKDTVHE FATLDVLLHT 360 PQARVCAEDV TIWVKKYISL KGHEFSY* 420 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK10162 | PRK10162 | 3.0e-7 | 59 | 175 | 118 | + acetyl esterase; Provisional | ||
pfam00135 | COesterase | 2.0e-9 | 105 | 225 | 131 | + Carboxylesterase family. | ||
cd00312 | Esterase_lipase | 8.0e-10 | 96 | 244 | 168 | + 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. | ||
COG0657 | Aes | 1.0e-35 | 79 | 364 | 287 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 3.0e-60 | 110 | 352 | 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 | 387 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
RefSeq | XP_002272331.1 | 0 | 1 | 387 | 1 | 395 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002311735.1 | 0 | 1 | 387 | 1 | 387 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002311736.1 | 0 | 1 | 387 | 1 | 388 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515006.1 | 0 | 1 | 387 | 1 | 391 | catalytic, putative [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 | 8e-38 | 49 | 342 | 62 | 319 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 2zsh_A | 8e-38 | 49 | 342 | 62 | 319 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 1e-31 | 107 | 359 | 112 | 335 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 1e-31 | 107 | 359 | 112 | 335 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 1e-31 | 107 | 359 | 112 | 335 | 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 |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
DT485343 | 269 | 120 | 388 | 0 |
ES789976 | 317 | 93 | 388 | 0 |
DT480110 | 246 | 1 | 246 | 0 |
EB438845 | 279 | 125 | 388 | 0 |
GO362523 | 303 | 95 | 378 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|