C71DC_CATRO
ID C71DC_CATRO Reviewed; 506 AA.
AC P98183; C0KYN4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Tabersonine 16-hydroxylase 1 {ECO:0000303|PubMed:24108213};
DE EC=1.14.14.103 {ECO:0000269|PubMed:12228585, ECO:0000269|PubMed:24108213};
DE AltName: Full=Cytochrome P450 71D12 {ECO:0000303|PubMed:24108213};
GN Name=CYP71D12 {ECO:0000303|PubMed:24108213};
GN Synonyms=T16H1 {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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=21047699; DOI=10.1016/j.jplph.2010.08.018;
RA Guirimand G., Guihur A., Poutrain P., Hericourt F., Mahroug S.,
RA St-Pierre B., Burlat V., Courdavault V.;
RT "Spatial organization of the vindoline biosynthetic pathway in Catharanthus
RT roseus.";
RL J. Plant Physiol. 168:549-557(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-506, AND FUNCTION.
RX 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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=12228585; DOI=10.1104/pp.109.1.131;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16262708; DOI=10.1111/j.1365-313x.2005.02557.x;
RA Murata J., De Luca V.;
RT "Localization of tabersonine 16-hydroxylase and 16-OH tabersonine-16-O-
RT methyltransferase to leaf epidermal cells defines them as a major site of
RT precursor biosynthesis in the vindoline pathway in Catharanthus roseus.";
RL Plant J. 44:581-594(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, AND INDUCTION BY METHYL JASMONATE.
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 flower biosynthesis of vindoline, a precursor
CC of vinblastine and vincristine (PubMed:10481044, PubMed:12228585,
CC PubMed:24108213). Hydroxylates specifically tabersonine, 2,3-
CC dihydrotabersonine and 2,3-dihydro-3-hydroxytabersonine, but has no
CC activity with naringenin, tryptamine, secologanin, strictosidine,
CC ajmalicine, vindoline and catharanthine (PubMed:24108213).
CC {ECO:0000269|PubMed:10481044, ECO:0000269|PubMed:12228585,
CC 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:12228585, 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=11 uM for tabersonine in a T16H/16OMT coupled system
CC {ECO:0000269|PubMed:12228585};
CC KM=350 nM for tabersonine {ECO:0000269|PubMed:24108213};
CC KM=14 uM for NADPH in a T16H/16OMT coupled system
CC {ECO:0000269|PubMed:12228585};
CC Note=concentrations of tabersonine greater than 30 uM are inhibitory.
CC {ECO:0000269|PubMed:12228585};
CC pH dependence:
CC Optimum pH is 7.5 in phosphate buffer and 8.0 in TRIS-HCl.
CC {ECO:0000269|PubMed:12228585};
CC Temperature dependence:
CC Stable at 30 degrees Celsius. {ECO:0000269|PubMed:12228585};
CC -!- PATHWAY: Alkaloid biosynthesis; vindoline biosynthesis. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12228585, ECO:0000269|PubMed:21047699}; Single-pass
CC membrane protein {ECO:0000255}. Note=The ER localization is dependent
CC on the presence of the putative transmembrane helix.
CC {ECO:0000269|PubMed:21047699}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in young leaves of mature
CC plants (PubMed:12228585, PubMed:16262708). Low expression in roots and
CC flowers, but not detected in stems and old leaves (PubMed:12228585,
CC PubMed:16262708). Found predominantly in leaf epidermis
CC (PubMed:12228585, PubMed:16262708). Barely detected in roots,
CC internodes, young and mature leaves, and flower buds, but relatively
CC abundant in fully developped flowers (PubMed:24108213). Not detected in
CC leaf epidermal cells (PubMed:24108213). {ECO:0000269|PubMed:12228585,
CC ECO:0000269|PubMed:16262708, ECO:0000269|PubMed:24108213}.
CC -!- DEVELOPMENTAL STAGE: Peak of expression after light treatment at 9 days
CC of seedling development. {ECO:0000269|PubMed:12228585}.
CC -!- INDUCTION: Up-regulated by methyl jasmonate (PubMed:24108213).
CC Inhibited by cytochrome c, CO, clotrimazole, miconazole, tricliphane,
CC flusilazole and tetcyclasis, and with a lower efficiency, by 1-
CC phenylimidazole and piperonylbutoxide. Not inhibited by potassium
CC cyanide and sodium azide. {ECO:0000269|PubMed:12228585,
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; FJ647194; ACM92061.1; -; mRNA.
DR EMBL; AJ238612; CAB56503.1; -; mRNA.
DR AlphaFoldDB; P98183; -.
DR SMR; P98183; -.
DR KEGG; ag:CAB56503; -.
DR BioCyc; MetaCyc:MON-7709; -.
DR BRENDA; 1.14.14.103; 1211.
DR SABIO-RK; P98183; -.
DR UniPathway; UPA00365; -.
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..506
FT /note="Tabersonine 16-hydroxylase 1"
FT /id="PRO_0000310728"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 447
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 506 AA; 58079 MW; 485FF14E6D34901B CRC64;
MEFYYFLYLA FLLFCFILSK TTKKFGQNSQ YSNHDELPPG PPQIPILGNA HQLSGGHTHH
ILRDLAKKYG PLMHLKIGEV STIVASSPQI AEEIFRTHDI LFADRPSNLE SFKIVSYDFS
DMVVSPYGNY WRQLRKISMM ELLSQKSVQS FRSIREEEVL NFIKSIGSKE GTRINLSKEI
SLLIYGITTR AAFGEKNKNT EEFIRLLDQL TKAVAEPNIA DMFPSLKFLQ LISTSKYKIE
KIHKQFDVIV ETILKGHKEK INKPLSQENG EKKEDLVDVL LNIQRRNDFE APLGDKNIKA
IIFNIFSAGT ETSSTTVDWA MCEMIKNPTV MKKAQEEVRK VFNEEGNVDE TKLHQLKYLQ
AVIKETLRLH PPVPLLLPRE CREQCKIKGY TIPSKSRVIV NAWAIGRDPN YWIEPEKFNP
DRFLESKVDF KGNSFEYLPF GGGRRICPGI TFALANIELP LAQLLFHFDW QSNTEKLNMK
ESRGVTVRRE DDLYLTPVNF SSSSPA
