T10H_TAXCU
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 03-AUG-2022, entry version 76.
DE RecName: Full=Taxane 10-beta-hydroxylase;
DE EC=1.14.14.105 {ECO:0000269|PubMed:11171980};
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; 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=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 from
RT 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 by
CC hydroxylation at C10 to yield taxadien-5-alpha-acetoxy-10-beta-ol.
CC {ECO:0000269|PubMed:11171980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + taxa-4(20),11-
CC dien-5alpha-yl acetate = 10beta-hydroxytaxa-4(20),11-dien-5alpha-yl
CC acetate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:15241, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30042, ChEBI:CHEBI:50436, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.105;
CC Evidence={ECO:0000269|PubMed:11171980};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
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. {ECO:0000305}.
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DR EMBL; AF318211; AAK00946.1; -; mRNA.
DR AlphaFoldDB; Q9AXM6; -.
DR SMR; Q9AXM6; -.
DR KEGG; ag:AAK00946; -.
DR BioCyc; MetaCyc:MON-13401; -.
DR BRENDA; 1.14.14.105; 6225.
DR UniPathway; UPA00842; UER00809.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050597; F:taxane 10-beta-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..497
FT /note="Taxane 10-beta-hydroxylase"
FT /id="PRO_0000052202"
FT BINDING 443
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 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
