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Taxoid 14-beta-hydroxylase (EC 1.14.13.146) (Taxane 14b-hydroxylase)

 T14H_TAXCU              Reviewed;         509 AA.
Q84KI1;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 68.
RecName: Full=Taxoid 14-beta-hydroxylase;
EC=1.14.13.146;
AltName: Full=Taxane 14b-hydroxylase;
Taxus cuspidata (Japanese yew).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Pinidae; Cupressales; Taxaceae; Taxus.
NCBI_TaxID=99806;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=12729625; DOI=10.1016/S0003-9861(03)00090-0;
Jennewein S., Rithner C.D., Williams R.M., Croteau R.;
"Taxoid metabolism: Taxoid 14beta-hydroxylase is a cytochrome P450-
dependent monooxygenase.";
Arch. Biochem. Biophys. 413:262-270(2003).
-!- FUNCTION: Catalyzes the conversion of 5-alpha-acetoxy-10beta-ol to
5-alpha-acetoxy-10beta,14beta-dihydroxy taxadiene. Also acts on
taxa-4(20),11-dien-5-alpha-yl acetate.
{ECO:0000269|PubMed:12729625}.
-!- CATALYTIC ACTIVITY: 10-beta-hydroxytaxa-4(20),11-dien-5-alpha-yl
acetate + O(2) + NADPH = 10-beta,14-beta-dihydroxytaxa-4(20),11-
dien-5?-yl acetate + NADP(+) + H(2)O.
{ECO:0000269|PubMed:12729625}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=33 uM for 5-alpha-acetoxy taxadiene
{ECO:0000269|PubMed:12729625};
KM=55 uM for 5-alpha-acetoxy-10-beta-hydroxy taxadiene
{ECO:0000269|PubMed:12729625};
pH dependence:
Optimum pH is 7.5. {ECO:0000269|PubMed:12729625};
-!- PATHWAY: Alkaloid biosynthesis; taxol biosynthesis.
-!- SUBCELLULAR LOCATION: Microsome membrane
{ECO:0000269|PubMed:12729625}; Multi-pass membrane protein
{ECO:0000269|PubMed:12729625}.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; AY188177; AAO66199.1; -; mRNA.
ProteinModelPortal; Q84KI1; -.
SMR; Q84KI1; -.
KEGG; ag:AAO66199; -.
KO; K20512; -.
BioCyc; MetaCyc:MONOMER-13409; -.
BRENDA; 1.14.13.146; 6225.
UniPathway; UPA00842; -.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0036203; F:taxoid 14-beta-hydroxylase activity; IDA:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0042617; P:paclitaxel biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0042616; P:paclitaxel metabolic process; IDA:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
Monooxygenase; NADP; Oxidoreductase; Taxol biosynthesis;
Transmembrane; Transmembrane helix.
CHAIN 1 509 Taxoid 14-beta-hydroxylase.
/FTId=PRO_0000418753.
TRANSMEM 20 40 Helical. {ECO:0000255}.
TRANSMEM 186 206 Helical. {ECO:0000255}.
TRANSMEM 218 238 Helical. {ECO:0000255}.
METAL 443 443 Iron (heme axial ligand). {ECO:0000250}.
SEQUENCE 509 AA; 57147 MW; DE7B3D2980004F15 CRC64;
MDVFYPLKST VAKFNECFPA ILFIVLSAVA GIVLPLLLFL RSKRRSSVGL PPGKLGYPFI
GESLLFLKAL RSNTVEQFLD ERVKNFGNVF KTSLIGHPTV VLCGPAGNRL ILANEEKLVQ
MSWPKSSMKL MGEKSITAKR GEGHMIIRSA LQGFFSPGAL QKYIGQMSKT IENHINEKWK
GNDQVSVVAL VGDLVFDISA CLFFNINEKH ERERLFELLE IIAVGVLAVP VDLPGFAYHR
ALQARSKLNA ILSGLIEKRK MDLSSGLATS NQDLLSVFLT FKDDRGNPCS DEEILDNFSG
LLHGSYDTTV SAMACVFKLL SSNPECYEKV VQEQLGILSN KLEGDEITWK DVKSMKYTWQ
VVQETLRLYP SIFGSFRQAI TDIHYNGYII PKGWKLLWTP YTTHPKEMYF SEPEKFLPSR
FDQEGKLVAP YTFLPFGGGQ RSCPGWEFSK MEILLSVHHF VKTFSTFTPV DPAEIIARDS
LCPLPSNGFS VKLFPRSYSL HTGNQVKKI


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