y
Basic Information | |
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Species | Brassica rapa |
Cazyme ID | Bra005899 |
Family | CE10 |
Protein Properties | Length: 335 Molecular Weight: 36743.6 Isoelectric Point: 6.32 |
Chromosome | Chromosome/Scaffold: 03 Start: 1101825 End: 1104820 |
Description | alpha/beta-Hydrolases superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CE10 | 51 | 331 | 0 |
KDSIYHKPNNLHLRLYKPASASNRSATALLPVVVFFHGGGFCFGSRTWPHFHNFCLTLASSLHALVVSPDYRLAPEHRLPAAFEDAEAALTWLRDQAVSG EGDHWFEGGPGVDFDRVYVLGDSSGGNIAHHLAFRFGSGSTELSPVRVRGYVLLGPFFGGVERTKSEDGPSEALLSLDLLDKFWRLSLPEGATRDHPMAN PFGPTSPALESASIEPMLVIAGGSELLRDRAKEYAYKLKKMEGKKVDYIEFENEEHGFFSSNPSSDAAKQLLRIIGNFTDN |
Full Sequence |
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Protein Sequence Length: 335 Download |
MGSLGEQPQV AEDCMGLLQL LSDGTVVRSK RIDLITQQIP LANHKSNVLF KDSIYHKPNN 60 LHLRLYKPAS ASNRSATALL PVVVFFHGGG FCFGSRTWPH FHNFCLTLAS SLHALVVSPD 120 YRLAPEHRLP AAFEDAEAAL TWLRDQAVSG EGDHWFEGGP GVDFDRVYVL GDSSGGNIAH 180 HLAFRFGSGS TELSPVRVRG YVLLGPFFGG VERTKSEDGP SEALLSLDLL DKFWRLSLPE 240 GATRDHPMAN PFGPTSPALE SASIEPMLVI AGGSELLRDR AKEYAYKLKK MEGKKVDYIE 300 FENEEHGFFS SNPSSDAAKQ LLRIIGNFTD NLNF* 360 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK10162 | PRK10162 | 2.0e-5 | 105 | 179 | 75 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 3.0e-27 | 101 | 331 | 236 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 3.0e-58 | 101 | 310 | 212 | + 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 | NP_196275.1 | 0 | 1 | 333 | 1 | 329 | hydrolase [Arabidopsis thaliana] |
RefSeq | XP_002266241.1 | 0 | 4 | 328 | 1 | 317 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002309272.1 | 0 | 4 | 329 | 1 | 320 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002322758.1 | 0 | 4 | 328 | 1 | 319 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002524110.1 | 0 | 4 | 333 | 1 | 323 | Gibberellin receptor GID1, 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 | 23 | 329 | 29 | 327 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 2o7r_A | 0 | 23 | 329 | 29 | 327 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2zsi_A | 3.00018e-42 | 23 | 309 | 45 | 329 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2zsh_A | 3.00018e-42 | 23 | 309 | 45 | 329 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 9.99995e-41 | 52 | 309 | 66 | 328 | 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 |
EX136155 | 296 | 1 | 295 | 0 |
EX096109 | 252 | 1 | 252 | 0 |
EV113943 | 270 | 1 | 269 | 0 |
EX119597 | 259 | 3 | 260 | 0 |
EX096109 | 27 | 247 | 273 | 0.0004 |
Sequence Alignments (This image is cropped. Click for full image.) |
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