ID   C71E1_SORBI             Reviewed;         531 AA.
AC   O48958;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-MAR-2009, entry version 61.
DE   RecName: Full=4-hydroxyphenylacetaldehyde oxime monooxygenase;
DE            EC=1.14.13.68;
DE   AltName: Full=Cytochrome P450 71E1;
GN   Name=CYP71E1;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
OC   PACCAD clade; Panicoideae; Andropogoneae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. SS1000; TISSUE=Etiolated seedling;
RX   MEDLINE=98145474; PubMed=9484480; DOI=10.1023/A:1005915507497;
RA   Bak S., Kahn R.A., Nielsen H.L., Moeller B.L., Halkier B.A.;
RT   "Cloning of three A-type cytochromes P450, CYP71E1, CYP98, and CYP99
RT   from Sorghum bicolor (L.) Moench by a PCR approach and identification
RT   by expression in Escherichia coli of CYP71E1 as a multifunctional
RT   cytochrome P450 in the biosynthesis of the cyanogenic glucoside
RT   dhurrin.";
RL   Plant Mol. Biol. 36:393-405(1998).
CC   -!- FUNCTION: Catalyzes the conversion of p-hydroxyphenylacetaldoxime
CC       to p-hydroxymandelonitrile. The dehydration of the oxime to the
CC       corresponding nitrile is followed by a C-hydroxylation of the
CC       nitrile to produce p-hydroxymandelonitrile.
CC   -!- CATALYTIC ACTIVITY: (Z)-4-hydroxyphenylacetaldehyde oxime + NADPH
CC       + O(2) = (S)-4-hydroxymandelonitrile + NADP(+) + 2 H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Secondary metabolite biosynthesis; dhurrin biosynthesis;
CC       dhurrin from L-tyrosine: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (Potential).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; AF029858; AAC39318.1; -; mRNA.
DR   PIR; T14640; T14640.
DR   HSSP; P00179; 1DT6.
DR   Gramene; O48958; -.
DR   BioCyc; MetaCyc:MON-522; -.
DR   BRENDA; 1.14.13.68; 1396.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050592; F:4-hydroxyphenylacetaldehyde oxime monooxyge...; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW   Monooxygenase; NADP; Oxidoreductase; Transmembrane.
FT   CHAIN         1    531       4-hydroxyphenylacetaldehyde oxime
FT                                monooxygenase.
FT                                /FTId=PRO_0000052123.
FT   TRANSMEM     18     38       Potential.
FT   METAL       468    468       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   531 AA;  59088 MW;  2272E4AA910890D2 CRC64;
     MATTATPQLL GGSVPQQWQT CLLVLLPVLL VSYYLLTSRS RNRSRSGKLG GAPRLPPGPA
     QLPILGNLHL LGPLPHKNLR ELARRYGPVM QLRLGTVPTV VVSSAEAARE VLKVHDVDCC
     SRPASPGPKR LSYDLKNVGF APYGEYWREM RKLFALELLS MRRVKAACYA REQEMDRLVA
     DLDRAAASKA SIVLNDHVFA LTDGIIGTVA FGNIYASKQF AHKERFQHVL DDAMDMMASF
     SAEDFFPNAA GRLADRLSGF LARRERIFNE LDVFFEKVID QHMDPARPVP DNGGDLVDVL
     INLCKEHDGT LRFTRDHVKA IVLDTFIGAI DTSSVTILWA MSELMRKPQV LRKAQAEVRA
     AVGDDKPRVN SEDAAKIPYL KMVVKETLRL HPPATLLVPR ETMRDTTICG YDVPANTRVF
     VNAWAIGRDP ASWPAPDEFN PDRFVGSDVD YYGSHFELIP FGAGRRICPG LTMGETNVTF
     TLANLLYCYD WALPGAMKPE DVSMEETGAL TFHRKTPLVV VPTKYKNRRA A
//