KEGG   ORTHOLOGY: K09754
Entry
K09754                      KO                                     
Symbol
CYP98A, C3'H
Name
5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase [EC:1.14.14.96]
Pathway
map00940  Phenylpropanoid biosynthesis
map00941  Flavonoid biosynthesis
map00945  Stilbenoid, diarylheptanoid and gingerol biosynthesis
map01100  Metabolic pathways
map01110  Biosynthesis of secondary metabolites
Module
M00039  Monolignol biosynthesis, phenylalanine/tyrosine => monolignol
Reaction
R04342  trans-5-O-(4-coumaroyl)-D-quinate,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (3'-hydroxylating)
R06582  trans-5-O-(4-coumaroyl)-D-shikimate,[reduced NADPH---hemoprotein reductase]:oxygen oxidoreductase (3'-hydroxylating)
Brite
KEGG Orthology (KO) [BR:ko00001]
 09100 Metabolism
  09110 Biosynthesis of other secondary metabolites
   00940 Phenylpropanoid biosynthesis
    K09754  CYP98A, C3'H; 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
   00945 Stilbenoid, diarylheptanoid and gingerol biosynthesis
    K09754  CYP98A, C3'H; 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
   00941 Flavonoid biosynthesis
    K09754  CYP98A, C3'H; 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
 09180 Brite Hierarchies
  09181 Protein families: metabolism
   00199 Cytochrome P450
    K09754  CYP98A, C3'H; 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
Enzymes [BR:ko01000]
 1. Oxidoreductases
  1.14  Acting on paired donors, with incorporation or reduction of molecular oxygen
   1.14.14  With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
    1.14.14.96  5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
     K09754  CYP98A, C3'H; 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
Cytochrome P450 [BR:ko00199]
 Cytochrome P450, plant type
  CYP98 family
   K09754  CYP98A, C3'H; 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase
Other DBs
GO: 0047083
Genes
ATH: AT2G40890(CYP98A3)
ALY: 9315964
CRB: 17887658
CSAT: 104782574 104785308 104792955
EUS: EUTSA_v10016538mg
BRP: 103857960 103865848 103866522
BNA: 106352767 106386334 106391625 106395719 106431114 106438010
BOE: 106335822 106340718 106342398
RSZ: 108847330 108848401 108858042
THJ: 104803227
CPAP: 110811301
PVY: 116130453
TCC: 18598608
DZI: 111293639
GMX: 100811080 606506(CYP98A2)
PVU: 137813888
VRA: 106753926
VAR: 108346061
VUN: 114186352
VUM: 124835773
CCAJ: 109802555
APRC: 113861260
MTR: 120576930
TPRA: 123888242
CAM: 101502624
PSAT: 127126484
LJA: 130730027
ADU: 107494128
AIP: 107604697
LANG: 109326958
PCIN: 129311613
FVE: 101310387
RCN: 112191575
ZJU: 107431535
MNT: 21410476
CSV: 101217257
CMO: 103486874
BHJ: 120091747
CMAX: 111482281
CMOS: 111441713
CPEP: 111790179
JCU: 105636120
HBR: 110668477
MESC: 110621178
QLO: 115953326
TWL: 119992803
VVI: 100263633
VRI: 117920828
INI: 109159148
NNU: 104588272
OSA: 4339188
OBR: 102712257
BDI: 100835531
SITA: 101771055
SVS: 117849885
MUS: 135619798
DCT: 110101632
PEQ: 110024997
AOF: 109819911
NCOL: 116245980
SMO: SELMODRAFT_450942(C3'H1-1) SELMODRAFT_450943(C3'H1-2)
PPP: 112275074
AG: AAL99200(CYP98A13v1) AAL99201(CYP98A13v2) CAE47490(CYP98A11)
 » show all
Reference
PMID:9484480 (CYP98A1)
  Authors
Bak S, Kahn RA, Nielsen HL, Moller BL, Halkier BA
  Title
Cloning of three A-type cytochromes P450, CYP71E1, CYP98, and CYP99 from Sorghum bicolor (L.) Moench by a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome P450 in the biosynthesis of the cyanogenic glucoside dhurrin.
  Journal
Plant Mol Biol 36:393-405 (1998)
DOI:10.1023/A:1005915507497
  Sequence
[sbi:8077042]
Reference
PMID:17160453 (CYP98A11)
  Authors
Morant M, Schoch GA, Ullmann P, Ertunc T, Little D, Olsen CE, Petersen M, Negrel J, Werck-Reichhart D
  Title
Catalytic activity, duplication and evolution of the CYP98 cytochrome P450 family in wheat.
  Journal
Plant Mol Biol 63:1-19 (2007)
DOI:10.1007/s11103-006-9028-8
  Sequence
Reference
PMID:12428018 (CYP98A13)
  Authors
Gang DR, Beuerle T, Ullmann P, Werck-Reichhart D, Pichersky E
  Title
Differential production of meta hydroxylated phenylpropanoids in sweet basil peltate glandular trichomes and leaves is controlled by the activities of specific acyltransferases and hydroxylases.
  Journal
Plant Physiol 130:1536-44 (2002)
DOI:10.1104/pp.007146
  Sequence
Reference
  Authors
Costa MA, Collins RE, Anterola AM, Cochrane FC, Davin LB, Lewis NG.
  Title
An in silico assessment of gene function and organization of the phenylpropanoid pathway metabolic networks in Arabidopsis thaliana and limitations thereof.
  Journal
Phytochemistry 64:1097-112 (2003)
DOI:10.1016/S0031-9422(03)00517-X
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