ID   T7BH_TAXCU              Reviewed;         500 AA.
AC   Q6JTJ0;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Taxoid 7-beta-hydroxylase {ECO:0000303|PubMed:15157877};
DE            EC=1.14.13.147 {ECO:0000269|PubMed:15157877};
OS   Taxus cuspidata (Japanese yew).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales; Taxaceae;
OC   Taxus.
OX   NCBI_TaxID=99806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX   PubMed=15157877; DOI=10.1016/j.chembiol.2004.02.025;
RA   Chau M., Jennewein S., Walker K., Croteau R.;
RT   "Taxol biosynthesis: Molecular cloning and characterization of a cytochrome
RT   P450 taxoid 7 beta-hydroxylase.";
RL   Chem. Biol. 11:663-672(2004).
CC   -!- FUNCTION: Catalyzes the conversion of taxusin to 7-beta-hydroxytaxusin
CC       in taxol biosynthesis (PubMed:15157877). Catalyzes the conversion of 2-
CC       alpha-hydroxytaxusin to 2-alpha-7-beta-hydroxytaxusin in taxol
CC       biosynthesis (PubMed:15157877). {ECO:0000269|PubMed:15157877}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + reduced [NADPH--hemoprotein reductase] + taxusin = 7beta-
CC         hydroxytaxusin + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:31975, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:63664,
CC         ChEBI:CHEBI:63665; EC=1.14.13.147;
CC         Evidence={ECO:0000269|PubMed:15157877};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31976;
CC         Evidence={ECO:0000269|PubMed:15157877};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7beta-hydroxytaxusin + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 2alpha,7beta-dihydroxytaxusin + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:71407, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:63665, ChEBI:CHEBI:190506;
CC         Evidence={ECO:0000269|PubMed:15157877};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71408;
CC         Evidence={ECO:0000269|PubMed:15157877};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.6 uM for taxusin {ECO:0000269|PubMed:15157877};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:15157877};
CC   -!- PATHWAY: Alkaloid biosynthesis; taxol biosynthesis. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:15157877};
CC       Single-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY307951; AAQ75553.1; -; mRNA.
DR   AlphaFoldDB; Q6JTJ0; -.
DR   SMR; Q6JTJ0; -.
DR   KEGG; ag:AAQ75553; -.
DR   BioCyc; MetaCyc:MON-17468; -.
DR   BRENDA; 1.14.13.147; 6225.
DR   UniPathway; UPA00842; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0036239; F:taxoid 7beta-hydroxylase activity; IDA:UniProtKB.
DR   GO; GO:0042617; P:paclitaxel biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042616; P:paclitaxel metabolic 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; Microsome;
KW   Monooxygenase; Oxidoreductase; Taxol biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..500
FT                   /note="Taxoid 7-beta-hydroxylase"
FT                   /id="PRO_0000418752"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         446
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   500 AA;  56324 MW;  6DCE9DF872592A24 CRC64;
     MDALSLVNST VAKFNEVTQL QASPAILSTA LTAIAGIIVL LVITSKRRSS LKLPPGKLGL
     PFIGETLEFV KALRSDTLRQ FVEEREGKFG RVFKTSLLGK PTVILCGPAG NRLVLSNEEK
     LLHVSWSAQI ARILGLNSVA VKRGDDHRVL RVALAGFLGS AGLQLYIGKM SALIRNHINE
     KWKGKDEVNV LSLVRDLVMD NSAILFFNIY DKERKQQLHE ILKIILASHF GIPLNIPGFL
     YRKALKGSLK RKKILSALLE KRKDELRSRL ASSNQDLLSV LLSFRDERGK PLSDEAVLDN
     CFAMLDASYD TTTSQMTLIL KMLSSNPECF EKVVQEQLEI ASNKKEGEEI TMKDIKAMKY
     TWQVLQESLR MLSPVFGTLR KTMNDINHDG YTIPKGWQVV WTTYSTHQKD IYFKQPDKFM
     PSRFEEEDGH LDAYTFVPFG GGRRTCPGWE YAKVEILLFL HHFVKAFSGY TPTDPHERIC
     GYPVPLVPVK GFPIKLIARS