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 27-MAR-2024, entry version 91.
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:MONOMER-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 CDD; cd11043; CYP90-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24286:SF371; BETA-AMYRIN 28-OXIDASE-LIKE; 1.
DR PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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
//
