Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.009G104900.1 |
Family | CE10 |
Protein Properties | Length: 363 Molecular Weight: 40407.7 Isoelectric Point: 5.8296 |
Chromosome | Chromosome/Scaffold: 09 Start: 9174140 End: 9175780 |
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 | |||
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Family | Start | End | Evalue |
CE10 | 87 | 359 | 0 |
VLSKDAVYSPELNLSSRLYRPHNTNPDKKLPVLVYYHGGGFCIETPFNFRYHDHLNNLVAGSNVIAISVDYRLAPEHPLPIAYDDSWTALKWVASHVNGD GPEEWLNSHADFGQVFLAGDSAGANLAHQLAMRYGQENLSGIDLTGVILVHPYFGGKEPIGTEGENLETKSMIDAIWHFVCPTSSGLDDPLINPLVDPIL DRLGCDRLLVIIGGKDFLRERGWHYYERLSKGGWEGVVEIMEGKDDEHVFHLNDPTCENAVALLKRIASFINK |
Full Sequence |
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Protein Sequence Length: 363 Download |
MCISLSLCPS LTSGSQPFTF HHTLLSSRST TSKNYPFLIR SRLSMDSTIP EVAYDYSPFL 60 RIYKDGYIER LRGTDIVPSG LDPKTNVLSK DAVYSPELNL SSRLYRPHNT NPDKKLPVLV 120 YYHGGGFCIE TPFNFRYHDH LNNLVAGSNV IAISVDYRLA PEHPLPIAYD DSWTALKWVA 180 SHVNGDGPEE WLNSHADFGQ VFLAGDSAGA NLAHQLAMRY GQENLSGIDL TGVILVHPYF 240 GGKEPIGTEG ENLETKSMID AIWHFVCPTS SGLDDPLINP LVDPILDRLG CDRLLVIIGG 300 KDFLRERGWH YYERLSKGGW EGVVEIMEGK DDEHVFHLND PTCENAVALL KRIASFINKD 360 KA* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK10162 | PRK10162 | 3.0e-11 | 92 | 241 | 151 | + acetyl esterase; Provisional | ||
pfam00135 | COesterase | 8.0e-12 | 105 | 225 | 137 | + Carboxylesterase family. | ||
cd00312 | Esterase_lipase | 7.0e-12 | 104 | 225 | 136 | + 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. | ||
COG0657 | Aes | 2.0e-35 | 79 | 358 | 291 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 3.0e-58 | 119 | 338 | 225 | + 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 | XP_002313103.1 | 0 | 37 | 360 | 2 | 326 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330285.1 | 0 | 45 | 358 | 1 | 315 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002336023.1 | 0 | 49 | 362 | 1 | 313 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002518790.1 | 0 | 45 | 362 | 1 | 322 | Gibberellin receptor GID1, putative [Ricinus communis] |
RefSeq | XP_002518792.1 | 0 | 45 | 360 | 1 | 316 | 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 | 2zsi_A | 2e-36 | 77 | 360 | 60 | 351 | A Chain A, Crystal Structure Of N-Acetylglucosaminyltransferase I |
PDB | 2zsh_A | 2e-36 | 77 | 360 | 60 | 351 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 2o7v_A | 3e-36 | 82 | 357 | 46 | 327 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 2o7r_A | 3e-36 | 82 | 357 | 46 | 327 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 3ed1_F | 2e-29 | 65 | 360 | 37 | 350 | 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CV276865 | 249 | 115 | 363 | 0 |
DN491090 | 209 | 155 | 363 | 0 |
DT517396 | 208 | 156 | 363 | 0 |
CA924701 | 223 | 3 | 225 | 0 |
DC895685 | 312 | 51 | 361 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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