| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma06g46680.1 |
| Family | CE10 |
| Protein Properties | Length: 339 Molecular Weight: 37734.1 Isoelectric Point: 5.7241 |
| Chromosome | Chromosome/Scaffold: 06 Start: 49266700 End: 49268622 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CE10 | 44 | 312 | 0 |
| EQFIDGVAIRDVAVTHGGGQSGHHVRLYLPEIKPEDSQKLPIVLHFHGGGFCISEPDWFMYYQVYTRFARSTRSIVVSPFLRRAPEHRLPAAIDDGFDTL LWLQTVARSGSLEPWLEQHGDFNRVFLIGDSSGGNSVHEVAARAGSADLSPVRVAGAIPVHPGFVRSNRSRSEMEMPQTPFLTLDMLDKFLALALPVGAT KDHPFTCPMGEAAPPLEGLKLPPVLLCVAEMDLVRDTEMEYYEAMKKANKDVELYVSKGMTHSFYLNKI | |||
| Full Sequence |
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| Protein Sequence Length: 339 Download |
| MVQEKKLVDE VSGWLKIYDD GSVDRTWSGP DQFKFMAEPA PPHEQFIDGV AIRDVAVTHG 60 GGQSGHHVRL YLPEIKPEDS QKLPIVLHFH GGGFCISEPD WFMYYQVYTR FARSTRSIVV 120 SPFLRRAPEH RLPAAIDDGF DTLLWLQTVA RSGSLEPWLE QHGDFNRVFL IGDSSGGNSV 180 HEVAARAGSA DLSPVRVAGA IPVHPGFVRS NRSRSEMEMP QTPFLTLDML DKFLALALPV 240 GATKDHPFTC PMGEAAPPLE GLKLPPVLLC VAEMDLVRDT EMEYYEAMKK ANKDVELYVS 300 KGMTHSFYLN KIAVDMDPNV SAQTDALISR IKEFIEKH* 360 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00312 | Esterase_lipase | 0.004 | 70 | 192 | 141 | + 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 | 0.002 | 70 | 181 | 131 | + Carboxylesterase family. | ||
| pfam10340 | DUF2424 | 0.0002 | 84 | 180 | 98 | + Protein of unknown function (DUF2424). This is a family of proteins conserved in yeasts. The function is not known. | ||
| COG0657 | Aes | 5.0e-35 | 27 | 314 | 290 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 8.0e-65 | 86 | 309 | 224 | + 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 | ABB89011.1 | 0 | 1 | 338 | 1 | 333 | CXE carboxylesterase [Malus pumila] |
| GenBank | ABB89012.1 | 0 | 1 | 338 | 1 | 333 | CXE carboxylesterase [Malus pumila] |
| DDBJ | BAA85654.1 | 0 | 1 | 338 | 1 | 339 | hsr203J homolog [Pisum sativum] |
| RefSeq | XP_002297728.1 | 0 | 1 | 338 | 1 | 340 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002525545.1 | 0 | 1 | 338 | 1 | 337 | 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 | 3e-38 | 76 | 309 | 106 | 330 | A Chain A, Crystal Structure Of Putative Glucoamylase (Yp_210071.1) From Bacteroides Fragilis Nctc 9343 At 2.12 A Resolution |
| PDB | 2zsh_A | 3e-38 | 76 | 309 | 106 | 330 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 8e-36 | 80 | 309 | 109 | 329 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 8e-36 | 80 | 309 | 109 | 329 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 8e-36 | 80 | 309 | 109 | 329 | 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EG631279 | 339 | 1 | 339 | 0 |
| BW653967 | 237 | 1 | 237 | 0 |
| FE708899 | 288 | 39 | 326 | 0 |
| FE706841 | 259 | 68 | 326 | 0 |
| CK251557 | 328 | 1 | 328 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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