y
Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G034917_T02 |
Family | CE10 |
Protein Properties | Length: 381 Molecular Weight: 40485.7 Isoelectric Point: 6.1039 |
Chromosome | Chromosome/Scaffold: 7 Start: 126886012 End: 126887913 |
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 | 30 | 326 | 0 |
ETVPAGFDADTGVTSKDVVVDAATGIATRLYLPAIPTAPSSPQSDGNGNGNGSATAKLPILVIFHGGGFVIGSPADPGFHRYMNSLVASARVVAVSVGYR LAPENPLPAAYEDSWTALNWAVSGADPWLSAHGDLGRVFVAGYSAGSNIAHNMAIAAGVRGLRAAEPPRVEGVILLHPSFAGEQRMEEEDDRFWQVNKRR WKAIFPGARDGLDDPRINPVVAGAPSLAKLVGERLLVCTASEDPRAPRGRAYCEAVRASCWPGKVESFESQNEGHGFFVSGHGSTQAIALMDRVFDS |
Full Sequence |
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Protein Sequence Length: 381 Download |
MDPGSAEIVF DCDFFRIYSD GRVERFAGME TVPAGFDADT GVTSKDVVVD AATGIATRLY 60 LPAIPTAPSS PQSDGNGNGN GSATAKLPIL VIFHGGGFVI GSPADPGFHR YMNSLVASAR 120 VVAVSVGYRL APENPLPAAY EDSWTALNWA VSGADPWLSA HGDLGRVFVA GYSAGSNIAH 180 NMAIAAGVRG LRAAEPPRVE GVILLHPSFA GEQRMEEEDD RFWQVNKRRW KAIFPGARDG 240 LDDPRINPVV AGAPSLAKLV GERLLVCTAS EDPRAPRGRA YCEAVRASCW PGKVESFESQ 300 NEGHGFFVSG HGSTQAIALM DRVFDSLMTP MIARVATVSL RPTLAIGVDQ PSLNYHSSQR 360 LVNPSDKALS PWNKTTPPIS * 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK10162 | PRK10162 | 0.0004 | 42 | 209 | 175 | + acetyl esterase; Provisional | ||
pfam00135 | COesterase | 7.0e-5 | 80 | 191 | 129 | + Carboxylesterase family. | ||
cd00312 | Esterase_lipase | 2.0e-6 | 82 | 194 | 128 | + 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-19 | 34 | 288 | 259 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 8.0e-42 | 90 | 307 | 224 | + 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 | ACN28069.1 | 0 | 1 | 323 | 1 | 308 | unknown [Zea mays] |
RefSeq | NP_001063360.1 | 0 | 1 | 324 | 1 | 313 | Os09g0455900 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001146161.1 | 0 | 1 | 380 | 1 | 380 | hypothetical protein LOC100279730 [Zea mays] |
RefSeq | XP_002462487.1 | 0 | 1 | 323 | 1 | 320 | hypothetical protein SORBIDRAFT_02g026550 [Sorghum bicolor] |
RefSeq | XP_002462487.1 | 0 | 15 | 323 | 329 | 627 | hypothetical protein SORBIDRAFT_02g026550 [Sorghum bicolor] |
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-31 | 41 | 303 | 69 | 327 | A Chain A, Pectin Methylesterase Pema From Erwinia Chrysanthemi |
PDB | 2zsh_A | 2e-31 | 41 | 303 | 69 | 327 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_F | 1e-30 | 19 | 308 | 36 | 329 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_E | 1e-30 | 19 | 308 | 36 | 329 | B Chain B, Structural Basis Of Gibberellin(Ga3)-Induced Della Recognition By The Gibberellin Receptor |
PDB | 3ed1_D | 1e-30 | 19 | 308 | 36 | 329 | 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 |