| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10029541 |
| Family | CE10 |
| Protein Properties | Length: 280 Molecular Weight: 30327.4 Isoelectric Point: 10.7488 |
| Chromosome | Chromosome/Scaffold: 55 Start: 877051 End: 877890 |
| Description | carboxyesterase 18 |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CE10 | 63 | 250 | 8.12753e-44 |
| PSSSTPIQSVVSSDVTVDSSRNLWFRLYTPAATTYASLPIFVFFHGGGFAFLSAASVGYDLVCRRFARTLPAIVVSVNYRLTPEHRFPCQYEDGFDILRF LDADNSGDRDASVLPPSADITKCFLAGDSAGANLAHHVAVRAGRAGHGKFRRLRVVGQVSIQPFFGGEERSESEIRFGSNSVLVSLPR | |||
| Full Sequence |
|---|
| Protein Sequence Length: 280 Download |
| MSTTGPAGSA FDSQPITPPP PPAALPWTTR IAVSVVSALS DTVRRHDGTI NRRLLNFLDL 60 KSPSSSTPIQ SVVSSDVTVD SSRNLWFRLY TPAATTYASL PIFVFFHGGG FAFLSAASVG 120 YDLVCRRFAR TLPAIVVSVN YRLTPEHRFP CQYEDGFDIL RFLDADNSGD RDASVLPPSA 180 DITKCFLAGD SAGANLAHHV AVRAGRAGHG KFRRLRVVGQ VSIQPFFGGE ERSESEIRFG 240 SNSVLVSLPR TDWLGGRGQI GCGRRSCRRG RPGTMRRRT* |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam00135 | COesterase | 7.0e-7 | 90 | 143 | 55 | + Carboxylesterase family. |
| cd00312 | Esterase_lipase | 1.0e-7 | 89 | 145 | 59 | + 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. |
| PRK10162 | PRK10162 | 2.0e-11 | 88 | 197 | 112 | + acetyl esterase; Provisional |
| COG0657 | Aes | 2.0e-20 | 88 | 197 | 110 | + Esterase/lipase [Lipid metabolism] |
| pfam07859 | Abhydrolase_3 | 2.0e-37 | 103 | 254 | 152 | + 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 |
| GenBank | ABB89001.1 | 0 | 9 | 254 | 3 | 243 | CXE carboxylesterase [Malus pumila] |
| RefSeq | XP_002269719.1 | 0 | 25 | 254 | 8 | 227 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002270210.1 | 0 | 25 | 254 | 8 | 227 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002305855.1 | 0 | 17 | 253 | 5 | 239 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002518025.1 | 0 | 19 | 253 | 11 | 240 | Gibberellin receptor GID1, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3ed1_F | 1.99965e-42 | 25 | 253 | 15 | 252 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
| PDB | 3ed1_E | 1.99965e-42 | 25 | 253 | 15 | 252 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
| PDB | 3ed1_D | 1.99965e-42 | 25 | 253 | 15 | 252 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
| PDB | 3ed1_C | 1.99965e-42 | 25 | 253 | 15 | 252 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
| PDB | 3ed1_B | 1.99965e-42 | 25 | 253 | 15 | 252 | A Chain A, Cpgh89 (E483q, E601q), From Clostridium Perfringens, In Complex With Its Substrate Glcnac-Alpha-1,4-Galactose |
