C76B6_CATRO
ID C76B6_CATRO Reviewed; 493 AA.
AC Q8VWZ7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Geraniol 8-hydroxylase;
DE EC=1.14.14.83 {ECO:0000269|PubMed:11718718, ECO:0000269|PubMed:21504162};
DE AltName: Full=Cytochrome P450 76B6;
DE AltName: Full=Geraniol 10-hydroxylase;
DE Short=CrG10H;
GN Name=CYP76B6; Synonyms=G10H;
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], PROTEIN SEQUENCE OF 337-349, FUNCTION,
RP CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=11718718; DOI=10.1016/s0014-5793(01)03045-9;
RA Collu G., Unver N., Peltenburg-Looman A.M., van der Heijden R.,
RA Verpoorte R., Memelink J.;
RT "Geraniol 10-hydroxylase, a cytochrome P450 enzyme involved in terpenoid
RT indole alkaloid biosynthesis.";
RL FEBS Lett. 508:215-220(2001).
RN [2]
RP FUNCTION.
RA Collu G., Garcia A.A., van der Heijden R., Verpoorte R.;
RT "Activity of the cytochrome P450 enzyme geraniol 10-hydroxylase and
RT alkaloid production in plant cell cultures.";
RL Plant Sci. 162:165-172(2002).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=15053766; DOI=10.1111/j.1365-313x.2004.02030.x;
RA Burlat V., Oudin A., Courtois M., Rideau M., St-Pierre B.;
RT "Co-expression of three MEP pathway genes and geraniol 10-hydroxylase in
RT internal phloem parenchyma of Catharanthus roseus implicates multicellular
RT translocation of intermediates during the biosynthesis of monoterpene
RT indole alkaloids and isoprenoid-derived primary metabolites.";
RL Plant J. 38:131-141(2004).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=19504099; DOI=10.1007/s00299-009-0722-2;
RA Guirimand G., Burlat V., Oudin A., Lanoue A., St-Pierre B., Courdavault V.;
RT "Optimization of the transient transformation of Catharanthus roseus cells
RT by particle bombardment and its application to the subcellular localization
RT of hydroxymethylbutenyl 4-diphosphate synthase and geraniol 10-
RT hydroxylase.";
RL Plant Cell Rep. 28:1215-1234(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21504162; DOI=10.1021/jf200259n;
RA Sung P.H., Huang F.C., Do Y.Y., Huang P.L.;
RT "Functional expression of geraniol 10-hydroxylase reveals its dual function
RT in the biosynthesis of terpenoid and phenylpropanoid.";
RL J. Agric. Food Chem. 59:4637-4643(2011).
CC -!- FUNCTION: Hydroxylase involved in the biosynthesis of hydroxygeraniol,
CC a precursor of the terpenoid indole alkaloids such as vinblastine and
CC vincristine. Also able to hydroxylate in vitro nerol and to catalyze
CC 3'-hydroxylation of the flavanone naringenin to form eriodictyol. No
CC activity with apigenin, kaempferol, p-coumaric acid and ferulic acid as
CC substrates. {ECO:0000269|PubMed:11718718, ECO:0000269|PubMed:21504162,
CC ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geraniol + O2 + reduced [NADPH--hemoprotein reductase] =
CC (6E)-8-hydroxygeraniol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:32495, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17447, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:64235; EC=1.14.14.83;
CC Evidence={ECO:0000269|PubMed:11718718, ECO:0000269|PubMed:21504162};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.81 uM for geraniol {ECO:0000269|PubMed:21504162};
CC KM=58.39 uM for naringenin {ECO:0000269|PubMed:21504162};
CC Note=kcat is 3.15 min(-1) for naringenin. kcat is 7.86 min(-1) for
CC geraniol.;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19504099}; Single-pass membrane protein
CC {ECO:0000269|PubMed:19504099}. Note=The N-terminal transmembrane helix
CC is necessary and sufficient for endoplasmic reticulum targeting.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flower buds.
CC Hardly detected in mature flowers and fruits. Expressed in the internal
CC phloem-associated parenchyma. {ECO:0000269|PubMed:15053766}.
CC -!- INDUCTION: Up-regulated by methyl jasmonate treatment.
CC {ECO:0000269|PubMed:11718718}.
CC -!- MISCELLANEOUS: The recommended numbering of geraniol gives (6E)-8-
CC hydroxygeraniol as the product rather than 10-hydroxygeraniol as used
CC in most publications.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AJ251269; CAC80883.1; -; mRNA.
DR AlphaFoldDB; Q8VWZ7; -.
DR SMR; Q8VWZ7; -.
DR KEGG; ag:CAC80883; -.
DR BioCyc; MetaCyc:MON-12352; -.
DR BRENDA; 1.14.14.83; 1211.
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:0102811; F:geraniol 10-hydroxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F: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; IDA:UniProtKB.
DR GO; GO:0016099; P:monoterpenoid biosynthetic process; IDA:UniProtKB.
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 Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; NADP; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..493
FT /note="Geraniol 8-hydroxylase"
FT /id="PRO_0000418919"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 436
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"
SQ SEQUENCE 493 AA; 55658 MW; 45781801A2A5A86A CRC64;
MDYLTIILTL LFALTLYEAF SYLSRRTKNL PPGPSPLPFI GSLHLLGDQP HKSLAKLSKK
HGPIMSLKLG QITTIVISSS TMAKEVLQKQ DLAFSSRSVP NALHAHNQFK FSVVWLPVAS
RWRSLRKVLN SNIFSGNRLD ANQHLRTRKV QELIAYCRKN SQSGEAVDVG RAAFRTSLNL
LSNLIFSKDL TDPYSDSAKE FKDLVWNIMV EAGKPNLVDF FPLLEKVDPQ GIRHRMTIHF
GEVLKLFGGL VNERLEQRRS KGEKNDVLDV LLTTSQESPE EIDRTHIERM CLDLFVAGTD
TTSSTLEWAM SEMLKNPDKM KKTQDELAQV IGRGKTIEES DINRLPYLRC VMKETLRIHP
PVPFLIPRKV EQSVEVCGYN VPKGSQVLVN AWAIGRDETV WDDALAFKPE RFMESELDIR
GRDFELIPFG AGRRICPGLP LALRTVPLML GSLLNSFNWK LEGGMAPKDL DMEEKFGITL
QKAHPLRAVP STL
