y
Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g036408m |
Family | CE10 |
Protein Properties | Length: 184 Molecular Weight: 20752.7 Isoelectric Point: 6.5122 |
Chromosome | Chromosome/Scaffold: 00076 Start: 422838 End: 423389 |
Description | carboxyesterase 18 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 11 | 174 | 2.7e-37 |
TTSSSPVIVYFHGGGFILLATNSKRFDDHYRRLAKEIPAVVISVNYRLAPENQYPSQYDDGIDMLKFIDSKISTVEHFPACTNLKRCFVTGDSAGENLAH NVAVRANECKFSMLMLLRVVLIQPFFGGEERTQSEEDLNDITPLVSLKRTDWMWKAFWPEGSDR |
Full Sequence |
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Protein Sequence Length: 184 Download |
FGSLLSTKTA TTSSSPVIVY FHGGGFILLA TNSKRFDDHY RRLAKEIPAV VISVNYRLAP 60 ENQYPSQYDD GIDMLKFIDS KISTVEHFPA CTNLKRCFVT GDSAGENLAH NVAVRANECK 120 FSMLMLLRVV LIQPFFGGEE RTQSEEDLND ITPLVSLKRT DWMWKAFWPE GSDRDQSKFV 180 LLY* 240 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 9.0e-6 | 16 | 60 | 45 | + 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 | 1.0e-8 | 16 | 61 | 46 | + Carboxylesterase type B [Lipid metabolism] | ||
PRK10162 | PRK10162 | 1.0e-9 | 17 | 109 | 93 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 8.0e-21 | 16 | 183 | 168 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 1.0e-38 | 18 | 175 | 158 | + 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 |
RefSeq | XP_002268654.1 | 0 | 8 | 177 | 81 | 243 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268736.1 | 0 | 1 | 176 | 87 | 255 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268777.1 | 0 | 1 | 176 | 68 | 236 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268824.1 | 0 | 16 | 176 | 111 | 264 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268861.1 | 0 | 16 | 176 | 93 | 246 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 16 | 176 | 114 | 267 | A Chain A, Structure Of Ugt78g1 Complexed With Myricetin And Udp |
PDB | 2zsh_A | 2e-36 | 16 | 176 | 114 | 267 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 2e-33 | 16 | 176 | 113 | 266 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 2e-33 | 16 | 176 | 113 | 266 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 2e-33 | 16 | 176 | 113 | 266 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |