| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G133836_T01 |
| Family | CE10 |
| Protein Properties | Length: 380 Molecular Weight: 41076.9 Isoelectric Point: 9.2012 |
| Chromosome | Chromosome/Scaffold: 7 Start: 126910131 End: 126911577 |
| Description | alpha/beta-Hydrolases superfamily protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| CE10 | 85 | 365 | 1.4013e-45 |
| ARCSAGVDEATGVTSKDVVIDSGTGLAARMYLPPAPRGTQSKGLGKRHPVLVFYHGGAFVIESAFTPLYHAYLNGVAAKARVVAVSVEYRLAPEHRLPTA YDDSWQALNWVARNAGSGPEPWLRDRGNLSRLFVAGDSAGANIAHDMAMRAGTGGGLDGGAAIAGLLLLDPYFWGKKPVAGETTDPARRRQYEATWSFIC GGRYSIDDPLVDPLSMPASEWRKLACSRVAVTSSGLDDFRPRGLAYVAALRDSGWDGETEQYETPGERHVYFLDRPKDPNS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 380 Download |
| MVAKTRTRRQ LAKLALLLLA LLLLLAAILL CVFLIPRHHR RPLPPASPPG AGNASNPDDS 60 IVAFDFSPYL IMYKSGRVNR LDGTARCSAG VDEATGVTSK DVVIDSGTGL AARMYLPPAP 120 RGTQSKGLGK RHPVLVFYHG GAFVIESAFT PLYHAYLNGV AAKARVVAVS VEYRLAPEHR 180 LPTAYDDSWQ ALNWVARNAG SGPEPWLRDR GNLSRLFVAG DSAGANIAHD MAMRAGTGGG 240 LDGGAAIAGL LLLDPYFWGK KPVAGETTDP ARRRQYEATW SFICGGRYSI DDPLVDPLSM 300 PASEWRKLAC SRVAVTSSGL DDFRPRGLAY VAALRDSGWD GETEQYETPG ERHVYFLDRP 360 KDPNSVKELA FVTGFLSRE* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK10162 | PRK10162 | 0.005 | 134 | 228 | 96 | + acetyl esterase; Provisional | ||
| cd00312 | Esterase_lipase | 0.0007 | 120 | 225 | 116 | + 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 | 0.0003 | 129 | 229 | 112 | + Carboxylesterase family. | ||
| COG0657 | Aes | 6.0e-21 | 88 | 379 | 294 | + Esterase/lipase [Lipid metabolism] | ||
| pfam07859 | Abhydrolase_3 | 1.0e-31 | 135 | 357 | 223 | + alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0008152 | metabolic process |
| GO:0016787 | hydrolase activity |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAD09342.1 | 0 | 50 | 378 | 20 | 344 | putative PrMC3 [Oryza sativa Japonica Group] |
| GenBank | EAZ45013.1 | 0 | 38 | 379 | 70 | 408 | hypothetical protein OsJ_29652 [Oryza sativa Japonica Group] |
| RefSeq | NP_001062031.1 | 0 | 40 | 377 | 24 | 357 | Os08g0474800 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001063398.1 | 0 | 38 | 379 | 42 | 380 | Os09g0462100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001151232.1 | 0 | 1 | 379 | 1 | 379 | gibberellin receptor GID1L2 [Zea mays] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2zsi_A | 1e-30 | 86 | 347 | 59 | 322 | A Chain A, The Three-Dimensional Structures Of Two Plant Beta-Glucan Endohydrolases With Distinct Substrate Specificities |
| PDB | 2zsh_A | 1e-30 | 86 | 347 | 59 | 322 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_F | 2e-30 | 96 | 348 | 61 | 322 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_E | 2e-30 | 96 | 348 | 61 | 322 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| PDB | 3ed1_D | 2e-30 | 96 | 348 | 61 | 322 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
