Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g042415m |
Family | CE10 |
Protein Properties | Length: 152 Molecular Weight: 16940.2 Isoelectric Point: 7.076 |
Chromosome | Chromosome/Scaffold: 02499 Start: 10401 End: 10884 |
Description | alpha/beta-Hydrolases superfamily protein |
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 | 51 | 127 | 2.3e-24 |
PEKDPPLKQTKSSLFYYHGGGLFMGSPFCSTYHNYIGSLSAKANVIVVSIDYRLAPEHLVAAAYEDSWAALKWVASH |
Full Sequence |
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Protein Sequence Length: 152 Download |
MDSKQEHLHM SFFHIFVHTD GHGEGFFGTE KVSASMDSPN VVFSKDVVIV PEKDPPLKQT 60 KSSLFYYHGG GLFMGSPFCS TYHNYIGSLS AKANVIVVSI DYRLAPEHLV AAAYEDSWAA 120 LKWVASHFKI SAHGYETWLN TRANFTCVFT R* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG2272 | PnbA | 9.0e-7 | 55 | 134 | 94 | + Carboxylesterase type B [Lipid metabolism] | ||
cd00312 | Esterase_lipase | 2.0e-7 | 55 | 134 | 92 | + 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. | ||
pfam00135 | COesterase | 6.0e-9 | 48 | 128 | 93 | + Carboxylesterase family. | ||
COG0657 | Aes | 4.0e-17 | 64 | 127 | 64 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 6.0e-24 | 64 | 127 | 64 | + 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 | ABW74473.1 | 2e-34 | 11 | 149 | 38 | 183 | CXE carboxylesterase [Paeonia suffruticosa] |
EMBL | CBI32437.1 | 4e-36 | 1 | 149 | 1 | 158 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284587.1 | 3e-37 | 1 | 149 | 1 | 158 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002285071.1 | 8e-36 | 1 | 149 | 1 | 158 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002518789.1 | 3e-37 | 11 | 149 | 15 | 159 | catalytic, 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 | 2o7v_A | 0.0000000000002 | 64 | 149 | 86 | 164 | A Chain A, Crystal Structure Of A Native Endo Beta-1,3-Glucanase (Hev B 2), A Major Allergen From Hevea Brasiliensis |
PDB | 2o7r_A | 0.0000000000002 | 64 | 149 | 86 | 164 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2c7b_B | 0.00000000002 | 63 | 127 | 75 | 137 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 2c7b_A | 0.00000000002 | 63 | 127 | 75 | 137 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
PDB | 3zwq_B | 0.00000000002 | 63 | 128 | 78 | 141 | A Chain A, The Crystal Structure Of Este1, A New Thermophilic And Thermostable Carboxylesterase Cloned From A Metagenomic Library |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DB892259 | 161 | 1 | 149 | 6e-38 |
EC950278 | 160 | 1 | 149 | 2e-37 |
CK116020 | 161 | 1 | 149 | 5e-37 |
DN503474 | 161 | 1 | 149 | 2e-36 |
FQ432372 | 145 | 15 | 149 | 4e-36 |
Sequence Alignments (This image is cropped. Click for full image.) |
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