Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G323504_T01 |
Family | CE10 |
Protein Properties | Length: 362 Molecular Weight: 39080.9 Isoelectric Point: 5.9664 |
Chromosome | Chromosome/Scaffold: 2 Start: 186818557 End: 186819984 |
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 | 60 | 360 | 0 |
ERFDGTETVPPCPDGDPANGVASKDIVLDPAAGISARLYLPAGVDAGKKLPVVVFFHGGAFMVHTAASPLYHIYAASLAAAVPAVVVSVDYRLAPEHRIP AAYDDAFAALKAVIAACRADGAEAEAEPWLAAHGDASRIVLAGDSAGGNMAHNVAIRLRKEGGIEGYGDMVSGVVLLYPYFWGKEPLGAEPTDPGYRAMF DPTWEFICGGKFGLDHPYVNPMASPEEWRQLGSRRVLVTTADQCWFVERARAYAEGIKKCGWEGELEFYETKGEAHVFFLPKHGSEKAVKELALVAEFVR R |
Full Sequence |
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Protein Sequence Length: 362 Download |
MPKLSCRVLF AALLIASLAA LLVRFPIHRL LNPHAAMDPD SELEFEMPGV LRVYKTGRVE 60 RFDGTETVPP CPDGDPANGV ASKDIVLDPA AGISARLYLP AGVDAGKKLP VVVFFHGGAF 120 MVHTAASPLY HIYAASLAAA VPAVVVSVDY RLAPEHRIPA AYDDAFAALK AVIAACRADG 180 AEAEAEPWLA AHGDASRIVL AGDSAGGNMA HNVAIRLRKE GGIEGYGDMV SGVVLLYPYF 240 WGKEPLGAEP TDPGYRAMFD PTWEFICGGK FGLDHPYVNP MASPEEWRQL GSRRVLVTTA 300 DQCWFVERAR AYAEGIKKCG WEGELEFYET KGEAHVFFLP KHGSEKAVKE LALVAEFVRR 360 C* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK10162 | PRK10162 | 0.0003 | 89 | 240 | 162 | + acetyl esterase; Provisional | ||
cd00312 | Esterase_lipase | 2.0e-5 | 97 | 207 | 120 | + 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 | 4.0e-7 | 97 | 211 | 124 | + Carboxylesterase family. | ||
COG0657 | Aes | 9.0e-20 | 75 | 360 | 301 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-33 | 112 | 339 | 237 | + 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 |
DDBJ | BAD38544.1 | 0 | 41 | 361 | 6 | 321 | putative PrMC3 [Oryza sativa Japonica Group] |
GenBank | EEC84709.1 | 0 | 41 | 361 | 6 | 321 | hypothetical protein OsI_31669 [Oryza sativa Indica Group] |
GenBank | EEE69856.1 | 0 | 41 | 361 | 6 | 283 | hypothetical protein OsJ_29651 [Oryza sativa Japonica Group] |
RefSeq | NP_001063397.1 | 0 | 41 | 361 | 53 | 368 | Os09g0461900 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001150146.1 | 0 | 1 | 361 | 1 | 361 | gibberellin receptor GID1L2 [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 | 2o7v_A | 2e-34 | 31 | 358 | 6 | 327 | A Chain A, Structure Of Y194f Glycogenin Mutant Truncated At Residue 270 |
PDB | 2o7r_A | 2e-34 | 31 | 358 | 6 | 327 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2zsi_A | 4e-31 | 73 | 343 | 63 | 335 | A Chain A, Plant Carboxylesterase Aecxe1 From Actinidia Eriantha With Acyl Adduct |
PDB | 2zsh_A | 4e-31 | 73 | 343 | 63 | 335 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 4e-28 | 76 | 320 | 58 | 312 | 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 |
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 |