CYBK1_VITAC
ID CYBK1_VITAC Reviewed; 499 AA.
AC A0A2K9RG08;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Labd-13Z-ene-9,15,16-triol synthase, chloroplastic {ECO:0000303|PubMed:29315936};
DE EC=1.14.-.- {ECO:0000269|PubMed:29315936};
DE AltName: Full=Cytochrome P450 76BK1 {ECO:0000303|PubMed:29315936};
DE Short=VacCYP76BK1 {ECO:0000303|PubMed:29315936};
GN Name=CYP76BK1 {ECO:0000303|PubMed:29315936};
OS Vitex agnus-castus (Chaste tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Viticoideae; Vitex.
OX NCBI_TaxID=54477;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Fruit, Leaf, and Trichome gland;
RX PubMed=29315936; DOI=10.1111/tpj.13822;
RA Heskes A.M., Sundram T.C.M., Boughton B.A., Jensen N.B., Hansen N.L.,
RA Crocoll C., Cozzi F., Rasmussen S., Hamberger B., Hamberger B., Staerk D.,
RA Moeller B.L., Pateraki I.;
RT "Biosynthesis of bioactive diterpenoids in the medicinal plant Vitex agnus-
RT castus.";
RL Plant J. 93:943-958(2018).
RN [2]
RP REVIEW ON MENSTRUAL CYCLE DISORDERS.
RX PubMed=12809367; DOI=10.1078/094471103322004866;
RA Wuttke W., Jarry H., Christoffel V., Spengler B., Seidlova-Wuttke D.;
RT "Chaste tree (Vitex agnus-castus)--pharmacology and clinical indications.";
RL Phytomedicine 10:348-357(2003).
RN [3]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid
CC including cleroda-dienols, and peregrinol lactones and furan
CC derivatives, dopaminergic diterpenoids that can bind to dopamine
CC receptors in the human pituitary gland, have probably ability to lower
CC prolactin levels, and are used to treat menstrual cycle disorders (e.g.
CC premenstrual syndrome and mastodynia) (Probable). Cytochrome P450
CC catalyzing the hydroxylation of peregrinol to form labd-13Z-ene-
CC 9,15,16-triol (PubMed:29315936). {ECO:0000269|PubMed:29315936,
CC ECO:0000305|PubMed:12809367, ECO:0000305|PubMed:29315936,
CC ECO:0000305|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + peregrinol + reduced [NADPH--hemoprotein reductase] =
CC H(+) + H2O + labd-13Z-ene-9,15,16-triol + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:62192, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:145550, ChEBI:CHEBI:145552;
CC Evidence={ECO:0000269|PubMed:29315936};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62193;
CC Evidence={ECO:0000269|PubMed:29315936};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:29315936, ECO:0000305|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000305|PubMed:29315936}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in trichomes of leaves and fruits.
CC {ECO:0000269|PubMed:29315936}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MG696754; AUT77126.1; -; mRNA.
DR AlphaFoldDB; A0A2K9RG08; -.
DR SMR; A0A2K9RG08; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0031969; C:chloroplast 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:0106240; F:labd-13Z-ene-9,15,16-triol synthase activity; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Chloroplast; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Plastid; Transmembrane; Transmembrane helix.
FT CHAIN 1..499
FT /note="Labd-13Z-ene-9,15,16-triol synthase, chloroplastic"
FT /id="PRO_0000449306"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 442
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:P04798"
SQ SEQUENCE 499 AA; 56565 MW; 3632A3D4F8AE4F6F CRC64;
MDISAVVIVV SLISLAYYLL MRPDLRQGKS AKLPPGPYPL PVVGNIFQLG DKPNRSVTKL
AKKYGPVMSL RLGSILNVVI SSPEMAKEVL QKYDHVFSSR FVASSWTAHD HHNVSVPFLP
VGNRWRKMRK LFRDVMLSHP RLDGGRAIRQ TMIKNLYEYL LESSKTGKVV NIGAAATITS
VNLTSVSLFS GQVFHFDEDE STEFKETFEG LTIAAGRPNL SDFFPIIKPF DIQGCKRQMA
FYLGKLLEMF DKIVNERLKE MRTSPASARK NDMLDTLLDF CRDKENDMSL NDIKHVLVDL
FVGASDTASR TIEWAITELL LHPDILAKAK EELKNVIGEN KLVQESDIPN LPYMEAVIKE
VFRVHPVGPF LIPRRLEEDT ELSGYFIPKG TQIFVNVWSI HRDEKVWPNP ESFEPERFLN
NNIDYKGQDF VLLPFGSGRR MCPGVPLAHR MLYTMIGTFI HSFDWKFEPG VTPEKVDMNE
AFGIVLHKAV PLKAIPIKA
