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Cytochrome P450 98A3 (EC 1.14.-.-) (Protein REDUCED EPIDERMAL FLUORESCENCE 8) (p-coumaroylshikimate/quinate 3'-hydrolxylase) (C3'H)

 C98A3_ARATH             Reviewed;         508 AA.
O22203; Q0WWH4; Q940C7;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=Cytochrome P450 98A3;
EC=1.14.-.-;
AltName: Full=Protein REDUCED EPIDERMAL FLUORESCENCE 8;
AltName: Full=p-coumaroylshikimate/quinate 3'-hydrolxylase;
Short=C3'H;
Name=CYP98A3; Synonyms=C3'H, REF8; OrderedLocusNames=At2g40890;
ORFNames=T20B5.9;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-508.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION BY
WOUNDING.
STRAIN=cv. Columbia;
PubMed=11429408; DOI=10.1074/jbc.M104047200;
Schoch G., Goepfert S., Morant M., Hehn A., Meyer D., Ullmann P.,
Werck-Reichhart D.;
"CYP98A3 from Arabidopsis thaliana is a 3'-hydroxylase of phenolic
esters, a missing link in the phenylpropanoid pathway.";
J. Biol. Chem. 276:36566-36574(2001).
[6]
FUNCTION, MUTAGENESIS OF GLY-444, TISSUE SPECIFICITY, CATALYTIC
ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=11967091; DOI=10.1046/j.1365-313X.2002.01266.x;
Franke R., Humphreys J.M., Hemm M.R., Denault J.W., Ruegger M.O.,
Cusumano J.C., Chapple C.;
"The Arabidopsis REF8 gene encodes the 3-hydroxylase of
phenylpropanoid metabolism.";
Plant J. 30:33-45(2002).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=11967092; DOI=10.1046/j.1365-313X.2002.01267.x;
Franke R., Hemm M.R., Denault J.W., Ruegger M.O., Humphreys J.M.,
Chapple C.;
"Changes in secondary metabolism and deposition of an unusual lignin
in the ref8 mutant of Arabidopsis.";
Plant J. 30:47-59(2002).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia;
PubMed=16405932; DOI=10.1016/j.phytochem.2005.11.006;
Kai K., Shimizu B., Mizutani M., Watanabe K., Sakata K.;
"Accumulation of coumarins in Arabidopsis thaliana.";
Phytochemistry 67:379-386(2006).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16377748; DOI=10.1104/pp.105.069690;
Abdulrazzak N., Pollet B., Ehlting J., Larsen K., Asnaghi C.,
Ronseau S., Proux C., Erhardt M., Seltzer V., Renou J.P., Ullmann P.,
Pauly M., Lapierre C., Werck-Reichhart D.;
"A coumaroyl-ester-3-hydroxylase insertion mutant reveals the
existence of nonredundant meta-hydroxylation pathways and essential
roles for phenolic precursors in cell expansion and plant growth.";
Plant Physiol. 140:30-48(2006).
[10]
CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND 3D-STRUCTURE MODELING.
PubMed=19779199; DOI=10.1126/science.1174095;
Matsuno M., Compagnon V., Schoch G.A., Schmitt M., Debayle D.,
Bassard J.E., Pollet B., Hehn A., Heintz D., Ullmann P., Lapierre C.,
Bernier F., Ehlting J., Werck-Reichhart D.;
"Evolution of a novel phenolic pathway for pollen development.";
Science 325:1688-1692(2009).
[11]
CRYSTALLIZATION.
PubMed=21549841; DOI=10.1016/j.pep.2011.04.013;
Kim Y.H., Kwon T., Yang H.J., Kim W., Youn H., Lee J.Y., Youn B.;
"Gene engineering, purification, crystallization and preliminary X-ray
diffraction of cytochrome P450 p-coumarate-3-hydroxylase (C3H), the
Arabidopsis membrane protein.";
Protein Expr. Purif. 79:149-155(2011).
-!- FUNCTION: Cytochrome P450 which catalyzes 3'-hydroxylation of p-
coumaric esters of shikimic/quinic acids to form lignin monomers.
Can use p-coumarate, p-coumaraldehyde, p-coumaroyl methyl ester,
5-O-(4-coumaroyl) D-quinate and 5-O-(4-coumaroyl) shikimate as
substrates, but not p-coumaryl alcohol, p-coumaroyl CoA, 1-O-p-
coumaroyl-beta-D-glucose, p-hydroxy-cinnamyl alcohol, cinnamate,
caffeate or ferulate. Has a weak activity on tri(p-
coumaroyl)spermidine, but none on triferuloylspermidine.
Hydroxylates preferentially the 5-O-isomer, but can also convert
the 4-O- and 3-O-isomers with a lower efficiency. Involved in the
biosynthesis of the coumarins scopoletin and scopolin. Essential
for the biosynthesis of lignin. {ECO:0000269|PubMed:11429408,
ECO:0000269|PubMed:11967091, ECO:0000269|PubMed:11967092,
ECO:0000269|PubMed:16377748, ECO:0000269|PubMed:16405932}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=7 uM for 5-O-(4-coumaroyl) shikimate
{ECO:0000269|PubMed:11429408};
KM=18 uM for 5-O-(4-coumaroyl) quinate
{ECO:0000269|PubMed:11429408};
Note=Kcat is 612 min(-1) with 5-O-(4-coumaroyl) shikimate as
substrate. Kcat is 399 min(-1) with 5-O-(4-coumaroyl) quinate as
substrate. {ECO:0000269|PubMed:11429408};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Highly expressed in stems, roots and siliques.
Detected in leaves flowers and seedlings. Highest expression
detected in differentiating xylem. {ECO:0000269|PubMed:11429408,
ECO:0000269|PubMed:11967091, ECO:0000269|PubMed:19779199}.
-!- INDUCTION: Up-regulated by wounding.
{ECO:0000269|PubMed:11429408}.
-!- DISRUPTION PHENOTYPE: Dwarf. 91% and 97% reduction of the levels
of scopoletin and scopolin respectively, but increased levels of
skimmin, the beta-glucoside of umbelliferone. Altered lignin
composition and increased susceptiblity to fungal colonization.
{ECO:0000269|PubMed:11967092, ECO:0000269|PubMed:16377748,
ECO:0000269|PubMed:16405932}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB86449.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC002409; AAB86449.2; ALT_INIT; Genomic_DNA.
EMBL; CP002685; AEC09893.1; -; Genomic_DNA.
EMBL; AY056105; AAL06992.1; -; mRNA.
EMBL; AK226377; BAE98524.1; -; mRNA.
PIR; T00753; T00753.
RefSeq; NP_850337.1; NM_180006.2.
UniGene; At.19895; -.
UniGene; At.24415; -.
ProteinModelPortal; O22203; -.
SMR; O22203; -.
BioGrid; 4023; 4.
STRING; 3702.AT2G40890.1; -.
PaxDb; O22203; -.
PRIDE; O22203; -.
EnsemblPlants; AT2G40890.1; AT2G40890.1; AT2G40890.
GeneID; 818686; -.
Gramene; AT2G40890.1; AT2G40890.1; AT2G40890.
KEGG; ath:AT2G40890; -.
Araport; AT2G40890; -.
TAIR; locus:2058440; AT2G40890.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000218628; -.
InParanoid; O22203; -.
KO; K09754; -.
OMA; KMTKMGG; -.
OrthoDB; EOG093607RW; -.
PhylomeDB; O22203; -.
BioCyc; MetaCyc:AT2G40890-MONOMER; -.
SABIO-RK; O22203; -.
PRO; PR:O22203; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; O22203; baseline and differential.
Genevisible; O22203; AT.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:TAIR.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:TAIR.
GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
GO; GO:0046409; F:p-coumarate 3-hydroxylase activity; IDA:TAIR.
GO; GO:0009805; P:coumarin biosynthetic process; IMP:TAIR.
GO; GO:0009813; P:flavonoid biosynthetic process; IMP:TAIR.
GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
GO; GO:0009699; P:phenylpropanoid biosynthetic process; IMP:TAIR.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
Oxidoreductase; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 508 Cytochrome P450 98A3.
/FTId=PRO_0000052199.
TRANSMEM 1 21 Helical. {ECO:0000255}.
METAL 438 438 Iron (heme axial ligand). {ECO:0000250}.
MUTAGEN 444 444 G->D: In ref8; loss of activity.
{ECO:0000269|PubMed:11967091}.
CONFLICT 202 202 G -> E (in Ref. 3; AAL06992).
{ECO:0000305}.
CONFLICT 466 466 G -> V (in Ref. 4; BAE98524).
{ECO:0000305}.
SEQUENCE 508 AA; 57927 MW; BD22A574F6B16C35 CRC64;
MSWFLIAVAT IAAVVSYKLI QRLRYKFPPG PSPKPIVGNL YDIKPVRFRC YYEWAQSYGP
IISVWIGSIL NVVVSSAELA KEVLKEHDQK LADRHRNRST EAFSRNGQDL IWADYGPHYV
KVRKVCTLEL FTPKRLESLR PIREDEVTAM VESVFRDCNL PENRAKGLQL RKYLGAVAFN
NITRLAFGKR FMNAEGVVDE QGLEFKAIVS NGLKLGASLS IAEHIPWLRW MFPADEKAFA
EHGARRDRLT RAIMEEHTLA RQKSSGAKQH FVDALLTLKD QYDLSEDTII GLLWDMITAG
MDTTAITAEW AMAEMIKNPR VQQKVQEEFD RVVGLDRILT EADFSRLPYL QCVVKESFRL
HPPTPLMLPH RSNADVKIGG YDIPKGSNVH VNVWAVARDP AVWKNPFEFR PERFLEEDVD
MKGHDFRLLP FGAGRRVCPG AQLGINLVTS MMSHLLHHFV WTPPQGTKPE EIDMSENPGL
VTYMRTPVQA VATPRLPSDL YKRVPYDM


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