ID   C76BA_SWEMU             Reviewed;         495 AA.
AC   D1MI46;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Geraniol 8-hydroxylase;
DE            EC=1.14.14.83 {ECO:0000269|PubMed:20699579};
DE   AltName: Full=Cytochrome P450 76B10;
DE   AltName: Full=Geraniol 10-hydroxylase;
DE            Short=SmG10H;
GN   Name=CYP76B10; Synonyms=G10H;
OS   Swertia mussotii (Felwort).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Gentianaceae; Gentianeae; Swertiinae;
OC   Swertia.
OX   NCBI_TaxID=137888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=20699579; DOI=10.1271/bbb.100175;
RA   Wang J., Liu Y., Cai Y., Zhang F., Xia G., Xiang F.;
RT   "Cloning and functional analysis of geraniol 10-hydroxylase, a cytochrome
RT   P450 from Swertia mussotii Franch.";
RL   Biosci. Biotechnol. Biochem. 74:1583-1590(2010).
CC   -!- FUNCTION: Hydroxylase involved in the biosynthesis of hydroxygeraniol,
CC       a precursor of the iridoid monoterpenoid swertiamarin.
CC       {ECO:0000269|PubMed:20699579}.
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:20699579};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems and roots.
CC       {ECO:0000269|PubMed:20699579}.
CC   -!- INDUCTION: Up-regulated by methyl jasmonate treatment.
CC       {ECO:0000269|PubMed:20699579}.
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; GU168041; ACZ48680.1; -; mRNA.
DR   AlphaFoldDB; D1MI46; -.
DR   SMR; D1MI46; -.
DR   PRIDE; D1MI46; -.
DR   KEGG; ag:ACZ48680; -.
DR   BRENDA; 1.14.14.83; 12614.
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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   NADP; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..495
FT                   /note="Geraniol 8-hydroxylase"
FT                   /id="PRO_0000418920"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         438
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   495 AA;  55456 MW;  C84723BF767B49F6 CRC64;
     MDFDFLTIAI GFLFTITLYQ ALNFFSRKSK NLPPGPSPLP LIGNLHLLGD QPHKSLAKLA
     KKHGPIMGLQ LGQVTTIVVT SSGMAKEVLQ KQDLAFSSRS IPNAIHAHDQ YKYSVIWLPV
     ASRWRGLRKA LNSNMFSGNR LDANQHLRSR KVQELIAYCR KSSQTGDAID VGRAAFRTSL
     NLLSNTMFSK DLTDPYSDSA KEFKDLVWNV MVEAGKPNLV DYFPLLDKVD PQGIRKRMTI
     HFGKILELFG GLIDERLQQK KAKGVNDDVL DVLLTTSEES PEEIDRTHIQ RMCLDLFVAG
     TDTTSSTLEW AMSEMLKNPE KMKAAQAELA QVIGKGKAVE EADLARLPYL RCAIKETLRI
     HPPVPLLIPR RTEQEVEVCG YTVPKNSQVL VNVWAISRDD AIWKDPLSFK PERFLESELE
     MRGKDFELIP FGAGRRICPG LPLAVRMVPV MLGSLLNSFD WKLEGGIAPK DLDMEEKFGI
     TLQKAHPLRA VATPL