ID   T13H_TAXCU              Reviewed;         485 AA.
AC   Q8W4T9;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Taxane 13-alpha-hydroxylase;
DE            EC=1.14.14.106 {ECO:0000269|PubMed:11707604};
DE   AltName: Full=Cytochrome P450 725A2;
GN   Name=CYP725A2;
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, AND
RP   CHARACTERIZATION.
RX   PubMed=11707604; DOI=10.1073/pnas.251539398;
RA   Jennewein S., Rithner C.D., Williams R.M., Croteau R.B.;
RT   "Taxol biosynthesis: taxane 13alpha-hydroxylase is a cytochrome P450-
RT   dependent monooxygenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:13595-13600(2001).
CC   -!- FUNCTION: Involved in the transformation of a taxadienyl acetate by
CC       hydroxylation at C13 to yield taxadien-5-alpha-acetoxy-13-alpha-ol.
CC       {ECO:0000269|PubMed:11707604}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + reduced [NADPH--hemoprotein reductase] + taxa-4(20),11-
CC         dien-5alpha-ol = H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
CC         + taxa-4(20),11-dien-5alpha,13alpha-diol; Xref=Rhea:RHEA:18949,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30038,
CC         ChEBI:CHEBI:30041, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         EC=1.14.14.106; Evidence={ECO:0000269|PubMed:11707604};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Alkaloid biosynthesis; taxol biosynthesis.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AY056019; AAL23619.1; -; mRNA.
DR   AlphaFoldDB; Q8W4T9; -.
DR   SMR; Q8W4T9; -.
DR   KEGG; ag:AAL23619; -.
DR   BioCyc; MetaCyc:MON-13398; -.
DR   BRENDA; 1.14.14.106; 6225.
DR   UniPathway; UPA00842; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0050598; F:taxane 13-alpha-hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042617; P:paclitaxel 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; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Taxol biosynthesis.
FT   CHAIN           1..485
FT                   /note="Taxane 13-alpha-hydroxylase"
FT                   /id="PRO_0000052203"
FT   BINDING         431
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   485 AA;  54653 MW;  CC0B82A430F4F3B7 CRC64;
     MDALKQLEVS PSILFVTLAV MAGIILFFRS KRHSSVKLPP GNLGFPLVGE TLQFVRSLGS
     STPQQFIEER MSKFGDVFKT SIIGHPTVVL CGPAGNRLVL SNENKLVQMS WPSSMMKLIG
     EDCLGGKTGE QHRIVRAALT RFLGPQALQN HFAKMSSGIQ RHINEKWKGK DEATVLPLVK
     DLVFSVASRL FFGITEEHLQ EQLHNLLEVI LVGSFSVPLN IPGFSYHKAI QARATLADIM
     THLIEKRRNE LRAGTASENQ DLLSVLLTFT DERGNSLADK EILDNFSMLL HGSYDSTNSP
     LTMLIKVLAS HPESYEKVAQ EQFGILSTKM EGEEIAWKDL KEMKYSWQVV QETLRMYPPI
     FGTFRKAITD IHYNGYTIPK GWKLLWTTYS TQTKEEYFKD ADQFKPSRFE EEGKHVTPYT
     YLPFGGGMRV CPGWEFAKME TLLFLHHFVK AFSGLKAIDP NEKLSGKPLP PLPVNGLPIK
     LYSRS