C71B1_TANPA
ID C71B1_TANPA Reviewed; 499 AA.
AC X2EW55;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=3-beta-hydroxylase {ECO:0000303|PubMed:24704560};
DE Short=Tp8878 {ECO:0000303|PubMed:24704560};
DE EC=1.14.14.- {ECO:0000269|PubMed:24704560};
DE AltName: Full=Cytochrome P450 71CB1 {ECO:0000305};
GN Name=CYP71CB1 {ECO:0000303|PubMed:24704560};
OS Tanacetum parthenium (Feverfew) (Matricaria parthenium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Anthemidinae; Tanacetum.
OX NCBI_TaxID=127999;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=24704560; DOI=10.1016/j.ymben.2014.03.005;
RA Liu Q., Manzano D., Tanic N., Pesic M., Bankovic J., Pateraki I.,
RA Ricard L., Ferrer A., de Vos R., van de Krol S., Bouwmeester H.;
RT "Elucidation and in planta reconstitution of the parthenolide biosynthetic
RT pathway.";
RL Metab. Eng. 23C:145-153(2014).
RN [2]
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 germacrene-derived
CC sesquiterpene lactones (PubMed:30468448). Component of the parthenolide
CC biosynthetic pathway; parthenolide and conjugates are promising anti-
CC cancer drugs highly active against colon cancer cells
CC (PubMed:30468448). Catalyzes the conversion of costunolide and
CC parthenolide to 3-beta-hydroxycostunolide and 3-beta-
CC hydroxyparthenolide, respectively (PubMed:24704560).
CC {ECO:0000269|PubMed:24704560, ECO:0000303|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-costunolide + O2 + reduced [NADPH--hemoprotein reductase]
CC = 3beta-hydroxycostunolide + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:61324, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:3900, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:144560;
CC Evidence={ECO:0000269|PubMed:24704560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61325;
CC Evidence={ECO:0000269|PubMed:24704560};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + parthenolide + reduced [NADPH--hemoprotein reductase] =
CC 3beta-hydroxyparthenolide + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:61328, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:7939, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:144561; Evidence={ECO:0000269|PubMed:24704560};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61329;
CC Evidence={ECO:0000269|PubMed:24704560};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000303|PubMed:30468448}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively during ovary
CC development. {ECO:0000269|PubMed:24704560}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; KC954153; AHM24031.1; -; mRNA.
DR AlphaFoldDB; X2EW55; -.
DR SMR; X2EW55; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102628; F:costunolide 3beta-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102627; F:parthenolide 3beta-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..499
FT /note="3-beta-hydroxylase"
FT /id="PRO_0000448399"
FT TRANSMEM 2..22
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 441
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; 56836 MW; DE512FE68CD0BB86 CRC64;
MFSSFETLIL SFVSLFFMMI FIHSKWISSY SKMAKNLPPS PFGLPIIGNL HQLGMTPYNS
LRTLAHKYGS LMLIHLGSVP VIVASSAEAA QEIMKTHDQI FSTRPKMNIA SIVSFDAKIV
AFSPYGEHWR QSKSVYLLNL LSTKRVQSFR HVREDETNLM LDVIENSCGS EIDLSNMIMS
LTNDVVCRIA YGRKYYEDWF KELMKEVMDV LGVFSVGNYV PSLSWIDRLS GLEGRAYKAA
KQLDAFLEGV VKQHETKSNE SMRDQDVVDI LLETQREQAS AGTPFHRDTL KALMQEMFIA
GTDTTSTAIE WEISEVIKHP RVMKKLQQEL DEIAQGRQRI TEEDLEDTQH PYLEAILKES
MRLHIPVPLL LPREATHDVK VMGYDIAAGT QVLINAWMIA RDPTIWEDAD EFKPERFLDT
NIDYKGLNFE LLPFGAGRRG CPGIQFAMSV NKLALANLVY KFDFKLPNGL RLEQLDMTDS
TGITVRRKYP LLVIPTARF
