y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_032011m |
Family | CE10 |
Protein Properties | Length: 339 Molecular Weight: 38037.3 Isoelectric Point: 6.8838 |
Chromosome | Chromosome/Scaffold: 08744 Start: 97439 End: 98455 |
Description | carboxyesterase 18 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 45 | 331 | 0 |
FDLRTSPSKKPSNGVKTTDITIDKSRNLWFRLYTPVNTGDGAAAVGNLPVIFFFHGGGFVFMAPSSKPYDEFCYGLARELSAIVISVNYRLAPEHRYPSQ YEDGFDALKFVDTAIIEGFSGNLRQCFLAGDSAGGNLVHHLAVKASEHDFSNLKLIGNILIQPFFGGEERTESELRLTRAPFVTMERSDWMWKAFLPEGS NRDHPAANVFGPNSVDISGVKLPATIIFVGGFDPLQDWQKRYCDGLKKYGKEASLVEFAKTFHSFYAFPELPEFSMLMKEMKDFMRK |
Full Sequence |
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Protein Sequence Length: 339 Download |
MAQNDVPQWP DLPWKLNISI SAFSFTFDVT RRSNGTANRF LMSFFDLRTS PSKKPSNGVK 60 TTDITIDKSR NLWFRLYTPV NTGDGAAAVG NLPVIFFFHG GGFVFMAPSS KPYDEFCYGL 120 ARELSAIVIS VNYRLAPEHR YPSQYEDGFD ALKFVDTAII EGFSGNLRQC FLAGDSAGGN 180 LVHHLAVKAS EHDFSNLKLI GNILIQPFFG GEERTESELR LTRAPFVTME RSDWMWKAFL 240 PEGSNRDHPA ANVFGPNSVD ISGVKLPATI IFVGGFDPLQ DWQKRYCDGL KKYGKEASLV 300 EFAKTFHSFY AFPELPEFSM LMKEMKDFMR KQVESSGM* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 0.0009 | 76 | 185 | 124 | + 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 | 0.0002 | 72 | 179 | 120 | + Carboxylesterase type B [Lipid metabolism] | ||
PRK10162 | PRK10162 | 6.0e-11 | 113 | 330 | 220 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 4.0e-31 | 53 | 334 | 283 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-58 | 113 | 310 | 198 | + 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 | 10 | 329 | 13 | 327 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268861.1 | 0 | 10 | 329 | 13 | 327 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299011.1 | 0 | 29 | 333 | 1 | 308 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523490.1 | 0 | 8 | 332 | 7 | 331 | Arylacetamide deacetylase, putative [Ricinus communis] |
RefSeq | XP_002528343.1 | 0 | 11 | 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 | 3ed1_F | 0 | 12 | 329 | 15 | 347 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 0 | 12 | 329 | 15 | 347 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 0 | 12 | 329 | 15 | 347 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_C | 0 | 12 | 329 | 15 | 347 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_B | 0 | 12 | 329 | 15 | 347 | 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 |
FF380509 | 277 | 10 | 286 | 0 |
DB924701 | 190 | 1 | 189 | 0 |
DY269018 | 329 | 12 | 333 | 0 |
FC908024 | 313 | 12 | 317 | 0 |
DY262759 | 315 | 7 | 319 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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