Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G045433_T01 |
Family | CE10 |
Protein Properties | Length: 419 Molecular Weight: 45204.9 Isoelectric Point: 8.6961 |
Chromosome | Chromosome/Scaffold: 3 Start: 166243891 End: 166246698 |
Description | carboxyesterase 16 |
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 | 89 | 408 | 0 |
HAHLLAHAHPRRASDPTPTTPAPAPANGAPYRGYLPHAVSSPRAAASARRRLPIVVQFHGGGFVTGSNTAAANDAFCRRVAKLCDAIVVAVGYRLAPESR YPAAFDDGVKVLKWIAKQANLAMMTKVGGGVDTFGASTVEPWIAAHGDPARCVLLGASCGANIADYVTRKVVEDGKPFDPVKVVAQVLMYPFFIGSVPTH SEIRLANSYFYDKSTCLLAWRLFLSEKEFNLDHPAANPLAPSRRAPPLKCMPPTLTVIAEHDWMRDRAIAYSEELRKVNVDSPVLDYKDTVHEFATLDVF LKTPQAQACAEDIAIWMKKY |
Full Sequence |
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Protein Sequence Length: 419 Download |
MPSVGVKIYS VFFKLFLRHR LQSLAAAAAG DPDNAAFGVS CRPDEATAPP NPAFSAAADG 60 VASKDLHIDP NSSLSVRIFL PTPPPPSPHA HLLAHAHPRR ASDPTPTTPA PAPANGAPYR 120 GYLPHAVSSP RAAASARRRL PIVVQFHGGG FVTGSNTAAA NDAFCRRVAK LCDAIVVAVG 180 YRLAPESRYP AAFDDGVKVL KWIAKQANLA MMTKVGGGVD TFGASTVEPW IAAHGDPARC 240 VLLGASCGAN IADYVTRKVV EDGKPFDPVK VVAQVLMYPF FIGSVPTHSE IRLANSYFYD 300 KSTCLLAWRL FLSEKEFNLD HPAANPLAPS RRAPPLKCMP PTLTVIAEHD WMRDRAIAYS 360 EELRKVNVDS PVLDYKDTVH EFATLDVFLK TPQAQACAED IAIWMKKYIS LRGHEFSY* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG2272 | PnbA | 3.0e-5 | 140 | 252 | 126 | + Carboxylesterase type B [Lipid metabolism] | ||
cd00312 | Esterase_lipase | 2.0e-7 | 140 | 249 | 119 | + 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. | ||
PRK10162 | PRK10162 | 3.0e-8 | 142 | 224 | 86 | + acetyl esterase; Provisional | ||
COG0657 | Aes | 2.0e-29 | 140 | 402 | 263 | + Esterase/lipase [Lipid metabolism] | ||
pfam07859 | Abhydrolase_3 | 2.0e-59 | 143 | 383 | 241 | + 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 | EAY76860.1 | 0 | 1 | 418 | 1 | 410 | hypothetical protein OsI_04819 [Oryza sativa Indica Group] |
RefSeq | NP_001045117.1 | 0 | 1 | 418 | 1 | 410 | Os01g0902300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001142141.1 | 0 | 1 | 418 | 1 | 418 | hypothetical protein LOC100274306 [Zea mays] |
RefSeq | XP_002267130.1 | 0 | 1 | 418 | 1 | 425 | PREDICTED: hypothetical protein isoform 2 [Vitis vinifera] |
RefSeq | XP_002458935.1 | 0 | 1 | 418 | 1 | 419 | hypothetical protein SORBIDRAFT_03g042970 [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 | 3ed1_F | 3e-33 | 140 | 365 | 112 | 310 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3ed1_E | 3e-33 | 140 | 365 | 112 | 310 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3ed1_D | 3e-33 | 140 | 365 | 112 | 310 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3ed1_C | 3e-33 | 140 | 365 | 112 | 310 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3ed1_B | 3e-33 | 140 | 365 | 112 | 310 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
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 |