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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 14730 |
Family | CE10 |
Protein Properties | Length: 269 Molecular Weight: 29275.4 Isoelectric Point: 4.6011 |
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 | 7 | 268 | 0 |
VIDEEHGIWARIFLPTDQVQGKGEGDSPKLPVVLFFHGGGFVTLSADFFIFHVLCSSIAEKLGALVIGVNYRLAPENRLPAAYEDGFAALKWLADEQGGR RDPWLASHADLSKILVMGDSAGGNLAHHVTVRAAVEDLGEMRIMGQVLIQPFFGGIARFPSETKPQPPNSTLTTDLSDQLWELALPIGASRDHPYCHVVA PDLKAQLREIEALPKALVVAGSEDVLCDRVVEFAEVMRECGKDLELLVVENAGHAFYIVPES |
Full Sequence |
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Protein Sequence Length: 269 Download |
IASRDAVIDE EHGIWARIFL PTDQVQGKGE GDSPKLPVVL FFHGGGFVTL SADFFIFHVL 60 CSSIAEKLGA LVIGVNYRLA PENRLPAAYE DGFAALKWLA DEQGGRRDPW LASHADLSKI 120 LVMGDSAGGN LAHHVTVRAA VEDLGEMRIM GQVLIQPFFG GIARFPSETK PQPPNSTLTT 180 DLSDQLWELA LPIGASRDHP YCHVVAPDLK AQLREIEALP KALVVAGSED VLCDRVVEFA 240 EVMRECGKDL ELLVVENAGH AFYIVPESE 300 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00312 | Esterase_lipase | 7.0e-8 | 33 | 144 | 126 | + 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 | 3.0e-8 | 28 | 133 | 118 | + Carboxylesterase family. | ||
PRK10162 | PRK10162 | 2.0e-13 | 1 | 262 | 270 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 1.0e-33 | 16 | 266 | 251 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-65 | 39 | 264 | 227 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
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 | 1 | 250 | 53 | 296 | A Chain A, Characterization And Engineering Of The Bifunctional N- And O-glucosyltransferase Involved In Xenobiotic Metabolism In Plants |
PDB | 2o7r_A | 0 | 1 | 250 | 53 | 296 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 3ed1_F | 0 | 1 | 268 | 62 | 333 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 3ed1_E | 0 | 1 | 268 | 62 | 333 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 3ed1_D | 0 | 1 | 268 | 62 | 333 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
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 |
Sequence Alignments (This image is cropped. Click for full image.) |
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