Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G003246_T01 |
Family | CE10 |
Protein Properties | Length: 372 Molecular Weight: 39512.1 Isoelectric Point: 6.3486 |
Chromosome | Chromosome/Scaffold: 7 Start: 126535613 End: 126537208 |
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 | 96 | 369 | 0 |
AGLDEATGVTSKDVVLDAGTGLSVRIYLPKLQEPSKKLPVLVYFHGGAFLLESAGSATYHTYVNPLAAAAGVLVVSVDYRLAPEHPVPAAYEDSWAALQW VTSAQDEWIVEHGDTARLFLAGDSAGANIVHDMLMRASGAGGPRVEGAILLHPWFGGNAPIEGEPEGAAAATAGLWTYACPGAVGGADDPRMNPLAPGAP PLERLGCARMLVCAGKKDALYVRDRAYYEAVAASAWPGDVAWLESEGEEHVFFLPKPECENAKLLMDRVVAFIA |
Full Sequence |
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Protein Sequence Length: 372 Download |
MRRALCHRIT CYGRTGPRIL STPLIPAIWP GSVANVPSQK TPSYHRKSTS FATKVTPSTT 60 AMESGADEVA FESPAHFRIY KSGRIERLNR PPVLPAGLDE ATGVTSKDVV LDAGTGLSVR 120 IYLPKLQEPS KKLPVLVYFH GGAFLLESAG SATYHTYVNP LAAAAGVLVV SVDYRLAPEH 180 PVPAAYEDSW AALQWVTSAQ DEWIVEHGDT ARLFLAGDSA GANIVHDMLM RASGAGGPRV 240 EGAILLHPWF GGNAPIEGEP EGAAAATAGL WTYACPGAVG GADDPRMNPL APGAPPLERL 300 GCARMLVCAG KKDALYVRDR AYYEAVAASA WPGDVAWLES EGEEHVFFLP KPECENAKLL 360 MDRVVAFIAG A* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK10162 | PRK10162 | 5.0e-7 | 117 | 250 | 137 | + acetyl esterase; Provisional | ||
cd00312 | Esterase_lipase | 5.0e-9 | 117 | 250 | 148 | + 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 | 9.0e-10 | 121 | 236 | 128 | + Carboxylesterase family. | ||
COG0657 | Aes | 1.0e-24 | 92 | 369 | 281 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 1.0e-41 | 136 | 349 | 220 | + 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 |
GenBank | ACG31461.1 | 0 | 62 | 371 | 1 | 310 | gibberellin receptor GID1L2 [Zea mays] |
GenBank | EAZ03818.1 | 0 | 47 | 370 | 62 | 386 | hypothetical protein OsI_25947 [Oryza sativa Indica Group] |
RefSeq | NP_001063388.1 | 0 | 47 | 370 | 62 | 386 | Os09g0460300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001063389.1 | 0 | 61 | 369 | 2 | 310 | Os09g0460400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001140832.1 | 0 | 1 | 371 | 1 | 371 | hypothetical protein LOC100272907 [Zea mays] |
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 | 5e-35 | 86 | 368 | 54 | 348 | A Chain A, Structure Of The Symmetric Mad2 Dimer |
PDB | 2zsh_A | 5e-35 | 86 | 368 | 54 | 348 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 2o7v_A | 1e-34 | 104 | 253 | 53 | 207 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 2o7r_A | 1e-34 | 104 | 253 | 53 | 207 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 3ed1_F | 1e-29 | 86 | 326 | 46 | 308 | 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 |
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 |