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Protein

Cytochrome P450 98A3

Gene

CYP98A3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Cofactori

hemeBy similarity

Kineticsi

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.1 Publication

  1. KM=7 µM for 5-O-(4-coumaroyl) shikimate1 Publication
  2. KM=18 µM for 5-O-(4-coumaroyl) quinate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi438 – 4381Iron (heme axial ligand)By similarity

GO - Molecular functioni

  1. heme binding Source: InterPro
  2. identical protein binding Source: TAIR
  3. iron ion binding Source: InterPro
  4. monooxygenase activity Source: TAIR
  5. 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 Source: GO_Central
  6. p-coumarate 3-hydroxylase activity Source: TAIR

GO - Biological processi

  1. coumarin biosynthetic process Source: TAIR
  2. flavonoid biosynthetic process Source: TAIR
  3. lignin biosynthetic process Source: TAIR
  4. phenylpropanoid biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:AT2G40890-MONOMER.
SABIO-RKO22203.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytochrome P450 98A3 (EC:1.14.-.-)
Alternative name(s):
Protein REDUCED EPIDERMAL FLUORESCENCE 8
p-coumaroylshikimate/quinate 3'-hydrolxylase
Short name:
C3'H
Gene namesi
Name:CYP98A3
Synonyms:C3'H, REF8
Ordered Locus Names:At2g40890
ORF Names:T20B5.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 2

Organism-specific databases

TAIRiAT2G40890.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1 – 2121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: TAIR
  2. integral component of membrane Source: UniProtKB-KW
  3. intracellular membrane-bounded organelle Source: TAIR
  4. mitochondrion Source: TAIR
  5. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi444 – 4441G → D in ref8; loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508Cytochrome P450 98A3PRO_0000052199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki172 – 172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki189 – 189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiO22203.
PRIDEiO22203.

Expressioni

Tissue specificityi

Highly expressed in stems, roots and siliques. Detected in leaves flowers and seedlings. Highest expression detected in differentiating xylem.3 Publications

Inductioni

Up-regulated by wounding.1 Publication

Gene expression databases

GenevestigatoriO22203.

Interactioni

Protein-protein interaction databases

BioGridi4023. 1 interaction.
STRINGi3702.AT2G40890.1-P.

Structurei

3D structure databases

ProteinModelPortaliO22203.
SMRiO22203. Positions 56-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000218628.
InParanoidiO22203.
KOiK09754.
OMAiWIGSILN.
PhylomeDBiO22203.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O22203-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSWFLIAVAT IAAVVSYKLI QRLRYKFPPG PSPKPIVGNL YDIKPVRFRC
60 70 80 90 100
YYEWAQSYGP IISVWIGSIL NVVVSSAELA KEVLKEHDQK LADRHRNRST
110 120 130 140 150
EAFSRNGQDL IWADYGPHYV KVRKVCTLEL FTPKRLESLR PIREDEVTAM
160 170 180 190 200
VESVFRDCNL PENRAKGLQL RKYLGAVAFN NITRLAFGKR FMNAEGVVDE
210 220 230 240 250
QGLEFKAIVS NGLKLGASLS IAEHIPWLRW MFPADEKAFA EHGARRDRLT
260 270 280 290 300
RAIMEEHTLA RQKSSGAKQH FVDALLTLKD QYDLSEDTII GLLWDMITAG
310 320 330 340 350
MDTTAITAEW AMAEMIKNPR VQQKVQEEFD RVVGLDRILT EADFSRLPYL
360 370 380 390 400
QCVVKESFRL HPPTPLMLPH RSNADVKIGG YDIPKGSNVH VNVWAVARDP
410 420 430 440 450
AVWKNPFEFR PERFLEEDVD MKGHDFRLLP FGAGRRVCPG AQLGINLVTS
460 470 480 490 500
MMSHLLHHFV WTPPQGTKPE EIDMSENPGL VTYMRTPVQA VATPRLPSDL

YKRVPYDM
Length:508
Mass (Da):57,927
Last modified:January 1, 1998 - v1
Checksum:iBD22A574F6B16C35
GO

Sequence cautioni

The sequence AAB86449.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021G → E in AAL06992. (PubMed:14593172)Curated
Sequence conflicti466 – 4661G → V in BAE98524. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002409 Genomic DNA. Translation: AAB86449.2. Different initiation.
CP002685 Genomic DNA. Translation: AEC09893.1.
AY056105 mRNA. Translation: AAL06992.1.
AK226377 mRNA. Translation: BAE98524.1.
PIRiT00753.
RefSeqiNP_850337.1. NM_180006.2.
UniGeneiAt.19895.
At.24415.

Genome annotation databases

EnsemblPlantsiAT2G40890.1; AT2G40890.1; AT2G40890.
GeneIDi818686.
KEGGiath:AT2G40890.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002409 Genomic DNA. Translation: AAB86449.2. Different initiation.
CP002685 Genomic DNA. Translation: AEC09893.1.
AY056105 mRNA. Translation: AAL06992.1.
AK226377 mRNA. Translation: BAE98524.1.
PIRiT00753.
RefSeqiNP_850337.1. NM_180006.2.
UniGeneiAt.19895.
At.24415.

3D structure databases

ProteinModelPortaliO22203.
SMRiO22203. Positions 56-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4023. 1 interaction.
STRINGi3702.AT2G40890.1-P.

Proteomic databases

PaxDbiO22203.
PRIDEiO22203.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G40890.1; AT2G40890.1; AT2G40890.
GeneIDi818686.
KEGGiath:AT2G40890.

Organism-specific databases

GeneFarmi1309. 94.
TAIRiAT2G40890.

Phylogenomic databases

eggNOGiCOG2124.
HOGENOMiHOG000218628.
InParanoidiO22203.
KOiK09754.
OMAiWIGSILN.
PhylomeDBiO22203.

Enzyme and pathway databases

BioCyciMetaCyc:AT2G40890-MONOMER.
SABIO-RKO22203.

Gene expression databases

GenevestigatoriO22203.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00463. EP450I.
PR00385. P450.
SUPFAMiSSF48264. SSF48264. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    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.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-508.
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    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.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "CYP98A3 from Arabidopsis thaliana is a 3'-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway."
    Schoch G., Goepfert S., Morant M., Hehn A., Meyer D., Ullmann P., Werck-Reichhart D.
    J. Biol. Chem. 276:36566-36574(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION BY WOUNDING.
    Strain: cv. Columbia.
  6. "The Arabidopsis REF8 gene encodes the 3-hydroxylase of phenylpropanoid metabolism."
    Franke R., Humphreys J.M., Hemm M.R., Denault J.W., Ruegger M.O., Cusumano J.C., Chapple C.
    Plant J. 30:33-45(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-444, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  7. "Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis."
    Franke R., Hemm M.R., Denault J.W., Ruegger M.O., Humphreys J.M., Chapple C.
    Plant J. 30:47-59(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  8. "Accumulation of coumarins in Arabidopsis thaliana."
    Kai K., Shimizu B., Mizutani M., Watanabe K., Sakata K.
    Phytochemistry 67:379-386(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  9. "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."
    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.
    Plant Physiol. 140:30-48(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants."
    Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.
    Mol. Cell. Proteomics 6:601-610(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-189.
    Strain: cv. Landsberg erecta.
  11. Cited for: CATALYTIC ACTIVITY, TISSUE SPECIFICITY, 3D-STRUCTURE MODELING.
  12. "Gene engineering, purification, crystallization and preliminary X-ray diffraction of cytochrome P450 p-coumarate-3-hydroxylase (C3H), the Arabidopsis membrane protein."
    Kim Y.H., Kwon T., Yang H.J., Kim W., Youn H., Lee J.Y., Youn B.
    Protein Expr. Purif. 79:149-155(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.

Entry informationi

Entry nameiC98A3_ARATH
AccessioniPrimary (citable) accession number: O22203
Secondary accession number(s): Q0WWH4, Q940C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: February 4, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.