1.14.14.82: flavonoid 3'-monooxygenase
This is an abbreviated version!
For detailed information about flavonoid 3'-monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.82
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1.14.14.82
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anthocyanins
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naringenin
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flavanones
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flavonols
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kaempferol
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dihydrokaempferol
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dihydroflavonols
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b-ring
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delphinidin
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3',5'-hydroxylase
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5'-hydroxylase
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4-reductase
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f3\'hs
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pubescence
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dihydromyricetin
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nutrition
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synthesis
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agriculture
- 1.14.14.82
- anthocyanins
- naringenin
- flavanones
- flavonols
- kaempferol
- dihydrokaempferol
- dihydroflavonols
-
b-ring
- delphinidin
-
3',5'-hydroxylase
-
5'-hydroxylase
-
4-reductase
-
f3\'hs
-
pubescence
- dihydromyricetin
- nutrition
- synthesis
- agriculture
Reaction
Synonyms
CsF3'H, Cyp75B, CYP75B1, CYP75B3, CYP75B4, CYP75B50, EC 1.14.13.21, F3'H, flavonoid 3'-hydroxylase, flavonoid 3-hydroxylase, flavonoid 3’-hydroxylase, More, NADPH:flavonoid-3'-hydroxylase, oxygenase, flavonoid 3'-mono-, oxygenase, flavonoid 3-mono-, PR1, sb04g024710, SF3'H1
ECTree
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Organism on EC 1.14.14.82 - flavonoid 3'-monooxygenase
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ORGANISM 
COMMENTARY 
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two copies of the gene encoding the competing F3Â’H enzyme are present in the grape genome, the second is transcriptionally silent
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cDNA clones of CYP75B3 are isolated from the white rice, Iimi (IM), black rice, Heugnam (HN) and Heugjinju (HJJ), and red rice, Jeogjinju (JJJ) and Hongjinju (HoJJ). Three cDNA clones of CYP75B3 encoded proteins of 526 amino acids (CYP75B3-IM, CYP75B3-HN, and CYP75B3-JJJ). Amino acid sequence comparison reveals that CYP75B3-IM and CYP75B3-JJJ are identical to the registered sequence in UNIPROT database, but one amino acid is substituted in the CYP75B3-HN sequence at position 27. An additional substitution is observed in the CYP75B4-HJJ sequence at position 258. His27 of CYP75B3-HN is located at the N-terminal membrane anchor region; however, the other cytochrome P450-specific conserved regions, such as the oxygen binding pocket, the ExxR motif, and the heme binding domain, are identical among all of the isolated genes, while most of the substrate recognition sites are different between CYP75B3s. The Thr504 of each CYP75B3, known as functional determinant for the specific enzyme activity, is conserved
SwissProt
cDNA clones of CYP75B4 are isolated from the white rice, Iimi (IM), black rice, Heugnam (HN) and Heugjinju (HJJ), and red rice, Jeogjinju (JJJ) and Hongjinju (HoJJ). Five cDNA clones of CYP75B4-encoded proteins of 535 amino acids (CYP75B4-IM, CYP75B4-HN, CYP75B4-HJJ, CYP75B4-JJJ, and CYP75B4-HoJJ). Amino acid sequence comparison reveal that CYP75B4-IM is identical to the registered sequence in UNIPROT, but an amino acid substitution at position 351 is shared by CYP75B4-HN and CYP75B4-HJJ from black rice and another substitution at positions seven is shared by CYP75B4-JJJ and CYP75B4-HoJJ from red rice. An additional substitution is observed in the CYP75B4-HJJ sequence at position 258. Val7 of CYP75B4-JJJ and CYP75B4-HoJJ are located at the N-terminal membrane anchor region; however, the other cytochrome P450-specific conserved regions, such as the oxygen binding pocket, the ExxR motif, and the heme binding domain, are identical among all of the isolated genes, while most of the substrate recognition sites are different between CYP75B4s. The Leu512 of each CYP75B4, known as functional determinant for the specific enzyme activity, is conserved. The other substitutions, His258 of CYP75B4-HJJ and Gln351 of CYP75B4-HN and CYP75B4-HJJ, are located out of the functional regions
SwissProt
F3'H1; i.e. Sorghum vulgare, 3 genes F3'H1, F3'H2, and F3'H3
SwissProt
F3'H2; i.e. Sorghum vulgare, 3 genes F3'H1, F3'H2, and F3'H3
SwissProt
F3'H3; i.e. Sorghum vulgare, 3 genes F3'H1, F3'H2, and F3'H3
SwissProt
two copies of the gene encoding the competing F3Â’H enzyme are present in the grape genome, the second is transcriptionally silent
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