ID   C71DC_CATRO             Reviewed;         495 AA.
AC   P98183;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=Tabersonine 16-hydroxylase;
DE            EC=1.14.13.73;
DE   AltName: Full=Cytochrome P450 71D12;
DE   Flags: Fragment;
GN   Name=CYP71D12;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99412171; PubMed=10481044; DOI=10.1016/S0014-5793(99)01138-2;
RA   Schroeder G., Unterbusch E., Kaltenbach M., Schmidt J., Strack D.,
RA   Schroeder J.;
RT   "Light-induced cytochrome P450-dependent enzyme in indole alkaloid
RT   biosynthesis: tabersonine 16-hydroxylase.";
RL   FEBS Lett. 458:97-102(1999).
RN   [2]
RP   CHARACTERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12228585;
RA   St Pierre B., De Luca V.;
RT   "A cytochrome P-450 monooxygenase catalyzes the first step in the
RT   conversion of tabersonine to vindoline in Catharanthus roseus.";
RL   Plant Physiol. 109:131-139(1995).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16262708; DOI=10.1111/j.1365-313X.2005.02557.x;
RA   Murata J., Luca V.D.;
RT   "Localization of tabersonine 16-hydroxylase and 16-OH tabersonine-16-
RT   O-methyltransferase to leaf epidermal cells defines them as a major
RT   site of precursor biosynthesis in the vindoline pathway in
RT   Catharanthus roseus.";
RL   Plant J. 44:581-594(2005).
CC   -!- FUNCTION: Involved in the biosynthesis of vindoline, a precursor
CC       of vinblastine and vincristine.
CC   -!- CATALYTIC ACTIVITY: Tabersonine + NADPH + O(2) = 16-
CC       hydroxytabersonine + NADP(+) + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11 uM for tabersonine;
CC         KM=14 uM for NADPH;
CC         Note=concentrations of tabersonine greater than 30 uM are
CC         inhibitory;
CC       pH dependence:
CC         Optimum pH is 7.5 in phosphate buffer and 8.0 in TRIS-HCl;
CC       Temperature dependence:
CC         Stable at 30 degrees Celsius;
CC   -!- PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis; vindoline
CC       from tabersonine: step 1/6.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in young leaves of
CC       mature plants. Low expression in roots and flowers, but not
CC       detected in stems and old leaves. Found predominantly in leaf
CC       epidermis.
CC   -!- DEVELOPMENTAL STAGE: Peak of expression after light treatment at 9
CC       days of seedling development.
CC   -!- INDUCTION: Inhibited by cytochrome c, CO, clotrimazole,
CC       miconazole, tricliphane, flusilazole and tetcyclasis, and with a
CC       lower efficiency, by 1-phenylimidazole and piperonylbutoxide. Not
CC       inhibited by potassium cyanide and sodium azide.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AJ238612; CAB56503.1; -; mRNA.
DR   HSSP; P14779; 1JPZ.
DR   BioCyc; MetaCyc:MON-7709; -.
DR   BRENDA; 1.14.13.73; 20471.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050594; F:tabersonine 16-hydroxylase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Metal-binding; Monooxygenase; NADP;
KW   Oxidoreductase.
FT   CHAIN        <1    495       Tabersonine 16-hydroxylase.
FT                                /FTId=PRO_0000310728.
FT   COMPBIAS    490    493       Poly-Ser.
FT   NON_TER       1      1
SQ   SEQUENCE   495 AA;  56590 MW;  D769003236430161 CRC64;
     LLFCFILSKT TKKFGQNSQY SNHDELPPGP PQIPILGNAH QLSGGHTHHI LRDLAKKYGP
     LMHLKIGEVS TIVASSPQIA EEIFRTHDIL FADRPSNLES FKIVSYDFSD MVVSPYGNYW
     RQLRKISMME LLSQKSVQSF RSIREEEVLN FIKSIGSKEG TRINLSKEIS LLIYGITTRA
     AFGEKNKNTE EFIRLLDQLT KAVAEPNIAD MFPSLKFLQL ISTSKYKIEK IHKQFDVIVE
     TILKGHKEKI NKPLSQENGE KKEDLVDVLL NIQRRNDFEA PLGDKNIKAI IFNIFSAGTE
     TSSTTVDWAM CEMIKNPTVM KKAQEEVRKV FNEEGNVDET KLHQLKYLQA VIKETLRLHP
     PVPLLLPREC REQCKIKGYT IPSKSRVIVN AWAIGRDPNY WIEPEKFNPD RFLESKVDFK
     GNSFEYLPFG GGRRICPGIT FALANIELPL AQLLFHFDWQ SNTEKLNMKE SRGVTVRRED
     DLYLTPVNFS SSSPA
//