ID T10H_TAXCU Reviewed; 497 AA. AC Q9AXM6; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-MAR-2009, entry version 39. DE RecName: Full=Taxane 10-beta-hydroxylase; DE EC=1.14.13.76; DE AltName: Full=5-alpha-taxadienol-10-beta-hydroxylase; DE AltName: Full=Cytochrome P450 725A1; GN Name=CYP725A1; OS Taxus cuspidata (Japanese yew). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Coniferopsida; Coniferales; Taxaceae; Taxus. OX NCBI_TaxID=99806; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION. RX PubMed=11171980; DOI=10.1073/pnas.98.4.1501; RA Schoendorf A., Rithner C.D., Williams R.M., Croteau R.B.; RT "Molecular cloning of a cytochrome P450 taxane 10beta-hydroxylase cDNA RT from Taxus and functional expression in yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 98:1501-1506(2001). CC -!- FUNCTION: Involved in the transformation of a taxadienyl acetate CC by hydroxylation at C10 to yield taxadien-5-alpha-acetoxy-10-beta- CC ol. CC -!- CATALYTIC ACTIVITY: Taxa-4(20),11-dien-5-alpha-yl acetate + NADPH CC + O(2) = 10-beta-hydroxytaxa-4(20),11-dien-5-alpha-yl acetate + CC NADP(+) + H(2)O. CC -!- COFACTOR: Heme group (By similarity). CC -!- PATHWAY: Alkaloid biosynthesis; taxol biosynthesis; 10-deacetyl-2- CC debenzoylbaccatin III from taxa-4(20),11-dien-5alpha-ol: step 2/3. CC -!- SIMILARITY: Belongs to the cytochrome P450 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF318211; AAK00946.1; -; mRNA. DR BioCyc; MetaCyc:MON-13401; -. DR BRENDA; 1.14.13.76; 261237. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0050597; F:taxane 10-beta-hydroxylase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0042617; P:paclitaxel biosynthetic process; IEA:UniProtKB-KW. DR InterPro; IPR001128; Cyt_P450. DR InterPro; IPR017973; Cyt_P450_C. DR InterPro; IPR017972; Cyt_P450_CS. DR InterPro; IPR002401; Cyt_P450_E_grp-I. DR Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1. DR PANTHER; PTHR19383; Cyt_P450; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR PROSITE; PS00086; CYTOCHROME_P450; 1. PE 1: Evidence at protein level; KW Heme; Iron; Metal-binding; Monooxygenase; NADP; Oxidoreductase; KW Taxol biosynthesis. FT CHAIN 1 497 Taxane 10-beta-hydroxylase. FT /FTId=PRO_0000052202. FT METAL 443 443 Iron (heme axial ligand) (By similarity). SQ SEQUENCE 497 AA; 56691 MW; CFE40415ABC43814 CRC64; MDSFIFLRSI GTKFGQLESS PAILSLTLAP ILAIILLLLF RYNHRSSVKL PPGKLGFPLI GETIQLLRTL RSETPQKFFD DRLKKFGPVY MTSLIGHPTV VLCGPAGNKL VLSNEDKLVE MEGPKSFMKL IGEDSIVAKR GEDHRILRTA LARFLGAQAL QNYLGRMSSE IGHHFNEKWK GKDEVKVLPL VRGLIFSIAS TLFFDVNDGH QQKQLHHLLE TILVGSLSVP LDFPGTRYRK GLQARLKLDE ILSSLIKRRR RDLRSGIASD DQDLLSVLLT FRDEKGNSLT DQGILDNFSA MFHASYDTTV APMALIFKLL YSNPEYHEKV FQEQLEIIGN KKEGEEISWK DLKSMKYTWQ AVQESLRMYP PVFGIFRKAI TDIHYDGYTI PKGWRVLCSP YTTHLREEYF PEPEEFRPSR FEDEGRHVTP YTYVPFGGGL RTCPGWEFSK IEILLFVHHF VKNFSSYIPV DPNEKVLSDP LPPLPANGFS IKLFPRS //