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O22203

- C98A3_ARATH

UniProt

O22203 - C98A3_ARATH

Protein

Cytochrome P450 98A3

Gene

CYP98A3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    Heme group.By 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 Source: InterPro
    6. p-coumarate 3-hydroxylase activity Source: TAIR
    7. protein binding 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

    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

    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

    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 26-487.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

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

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000218628.
    InParanoidiO22203.
    KOiK09754.
    OMAiPVRFRCY.
    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

    MSWFLIAVAT IAAVVSYKLI QRLRYKFPPG PSPKPIVGNL YDIKPVRFRC    50
    YYEWAQSYGP IISVWIGSIL NVVVSSAELA KEVLKEHDQK LADRHRNRST 100
    EAFSRNGQDL IWADYGPHYV KVRKVCTLEL FTPKRLESLR PIREDEVTAM 150
    VESVFRDCNL PENRAKGLQL RKYLGAVAFN NITRLAFGKR FMNAEGVVDE 200
    QGLEFKAIVS NGLKLGASLS IAEHIPWLRW MFPADEKAFA EHGARRDRLT 250
    RAIMEEHTLA RQKSSGAKQH FVDALLTLKD QYDLSEDTII GLLWDMITAG 300
    MDTTAITAEW AMAEMIKNPR VQQKVQEEFD RVVGLDRILT EADFSRLPYL 350
    QCVVKESFRL HPPTPLMLPH RSNADVKIGG YDIPKGSNVH VNVWAVARDP 400
    AVWKNPFEFR PERFLEEDVD MKGHDFRLLP FGAGRRVCPG AQLGINLVTS 450
    MMSHLLHHFV WTPPQGTKPE EIDMSENPGL VTYMRTPVQA VATPRLPSDL 500
    YKRVPYDM 508
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi T00753.
    RefSeqi NP_850337.1. NM_180006.2.
    UniGenei At.19895.
    At.24415.

    3D structure databases

    ProteinModelPortali O22203.
    SMRi O22203. Positions 26-487.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 4023. 1 interaction.
    STRINGi 3702.AT2G40890.1-P.

    Proteomic databases

    PaxDbi O22203.
    PRIDEi O22203.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G40890.1 ; AT2G40890.1 ; AT2G40890 .
    GeneIDi 818686.
    KEGGi ath:AT2G40890.

    Organism-specific databases

    GeneFarmi 1309. 94.
    TAIRi AT2G40890.

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000218628.
    InParanoidi O22203.
    KOi K09754.
    OMAi PVRFRCY.
    PhylomeDBi O22203.

    Enzyme and pathway databases

    BioCyci MetaCyc:AT2G40890-MONOMER.
    SABIO-RK O22203.

    Gene expression databases

    Genevestigatori O22203.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00463. EP450I.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 121 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