C71DZ_CATRO
ID C71DZ_CATRO Reviewed; 512 AA.
AC U5HKE8;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Tabersonine 16-hydroxylase 2 {ECO:0000303|PubMed:24108213};
DE EC=1.14.14.103 {ECO:0000269|PubMed:24108213};
DE AltName: Full=Cytochrome P450 71D351 {ECO:0000303|PubMed:24108213};
GN Name=CYP71D351 {ECO:0000303|PubMed:24108213};
GN Synonyms=T16H2 {ECO:0000303|PubMed:24108213};
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058 {ECO:0000312|EMBL:AEB69788.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, LACK OF INDUCTION BY
RP METHYL JASMONATE, AND TISSUE SPECIFICITY.
RX PubMed=24108213; DOI=10.1104/pp.113.222828;
RA Besseau S., Kellner F., Lanoue A., Thamm A.M., Salim V., Schneider B.,
RA Geu-Flores F., Hoefer R., Guirimand G., Guihur A., Oudin A., Glevarec G.,
RA Foureau E., Papon N., Clastre M., Giglioli-Guivarc'h N., St-Pierre B.,
RA Werck-Reichhart D., Burlat V., De Luca V., O'Connor S.E., Courdavault V.;
RT "A pair of tabersonine 16-hydroxylases initiates the synthesis of vindoline
RT in an organ-dependent manner in Catharanthus roseus.";
RL Plant Physiol. 163:1792-1803(2013).
CC -!- FUNCTION: Involved in the foliar biosynthesis of vindoline, a precursor
CC of vinblastine and vincristine (PubMed:24108213). Hydroxylates
CC specifically tabersonine, 2,3-dihydrotabersonine and 2,3-dihydro-3-
CC hydroxytabersonine, but has no activity with naringenin, tryptamine,
CC secologanin, strictosidine, ajmalicine, vindoline and catharanthine
CC (PubMed:24108213). {ECO:0000269|PubMed:24108213}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-tabersonine + O2 + reduced [NADPH--hemoprotein reductase]
CC = 16-hydroxytabersonine + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:14133, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57893, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:58239; EC=1.14.14.103;
CC Evidence={ECO:0000269|PubMed:24108213};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=70 nM for tabersonine {ECO:0000269|PubMed:24108213};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24108213}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in roots, fruits, stems,
CC flower buds and flowers, but highly expressed in young leaves. Detected
CC in adaxial and abaxial epidermis cells. {ECO:0000269|PubMed:24108213}.
CC -!- INDUCTION: Not regulated by methyl jasmonate treatment.
CC {ECO:0000269|PubMed:24108213}.
CC -!- MISCELLANEOUS: Tabersonine 16-hydroxylation is orchestrated in an
CC organ-dependent manner by two genes including CYP71D351, which encodes
CC the T16H2 isoform acting in the foliar vindoline biosynthesis, and
CC CYP71D12, which encodes the T16H1 isoform acting in the flower
CC vindoline biosynthesis. {ECO:0000269|PubMed:24108213}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; JF742645; AEB69788.1; -; mRNA.
DR AlphaFoldDB; U5HKE8; -.
DR SMR; U5HKE8; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050594; F:tabersonine 16-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Alkaloid metabolism; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..512
FT /note="Tabersonine 16-hydroxylase 2"
FT /id="PRO_5004661923"
FT TOPO_DOM 1
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 445
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q96242"
SQ SEQUENCE 512 AA; 58483 MW; 2B6A1905EEEE1580 CRC64;
MELYYFSTFA FLLFCFILAK TLKKSGQSNL KLPLGPPPIP ILGNAHQLIG GHTHHILRDL
AKKYGPLMHL KTGEVSTIVA SSPEIAEEMF KTHDVLFADR PSNIVAFKIL SYDYSDVVIS
PYGNYWRQLR KISMMELFSQ RSVQSFRSIR EEEVLNFIKS IGSREGTKIN LSKEISLLIY
GITTRAAFGE KNKNTEEFIR LLDQLTVAVA EPNIADMFPS INFLKLISRS KYKIEKIHKN
FDAIVQTILN HHKDRLANHK SSSHEENGEQ NKDLVDVLLN IQQRGDFDTP LGDRSVKAVI
FNIFSAGTET SSTTVDWAMC EMIKNPTIMK KAQEEVRKVY NEEGNVNETK LHQLKYLKAV
IKETLRLHPP VPLLLPRECR EQCEIKGYTI PSKSRVIVNA WAIGRDPNYW IEPENFNPER
FLESEVDFKG NSFEYLPFGG GRRICPGITF ALANIELPLA QLLFHFDWKL ASDETNIDKL
DMTESRGVTV RREDDLCLIP FPYSASSLKG KY
