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   03-AUG-2022, entry version 118.
DE   RecName: Full=4-hydroxyphenylacetaldehyde oxime monooxygenase;
DE            EC=1.14.14.37 {ECO:0000269|PubMed:26361733};
DE   AltName: Full=Cytochrome P450 71E1;
GN   Name=CYP71E1;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. SS1000; TISSUE=Etiolated seedling;
RX   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 from
RT   Sorghum bicolor (L.) Moench by a PCR approach and identification by
RT   expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome
RT   P450 in the biosynthesis of the cyanogenic glucoside dhurrin.";
RL   Plant Mol. Biol. 36:393-405(1998).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=26361733; DOI=10.1111/tpj.13023;
RA   Clausen M., Kannangara R.M., Olsen C.E., Blomstedt C.K., Gleadow R.M.,
RA   Joergensen K., Bak S., Motawie M.S., Moeller B.L.;
RT   "The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic
RT   pathways.";
RL   Plant J. 84:558-573(2015).
CC   -!- FUNCTION: Catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-
CC       hydroxymandelonitrile. The dehydration of the oxime to the
CC       corresponding nitrile is followed by a C-hydroxylation of the nitrile
CC       to produce p-hydroxymandelonitrile. {ECO:0000269|PubMed:26361733}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-hydroxyphenylacetaldehyde oxime + O2 + reduced [NADPH--
CC         hemoprotein reductase] = (S)-4-hydroxymandelonitrile + H(+) + 2 H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:18401,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15666,
CC         ChEBI:CHEBI:16660, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         EC=1.14.14.37; Evidence={ECO:0000269|PubMed:26361733};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; dhurrin biosynthesis;
CC       dhurrin from L-tyrosine: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF029858; AAC39318.1; -; mRNA.
DR   PIR; T14640; T14640.
DR   AlphaFoldDB; O48958; -.
DR   SMR; O48958; -.
DR   STRING; 4558.Sb01g001180.1; -.
DR   PRIDE; O48958; -.
DR   EnsemblPlants; EER93095; EER93095; SORBI_3001G012200.
DR   Gramene; EER93095; EER93095; SORBI_3001G012200.
DR   eggNOG; KOG0156; Eukaryota.
DR   BioCyc; MetaCyc:MON-522; -.
DR   BRENDA; 1.14.14.37; 5768.
DR   SABIO-RK; O48958; -.
DR   UniPathway; UPA00757; UER00745.
DR   ExpressionAtlas; O48958; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050592; F:4-hydroxyphenylacetaldehyde oxime monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0010132; P:dhurrin 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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..531
FT                   /note="4-hydroxyphenylacetaldehyde oxime monooxygenase"
FT                   /id="PRO_0000052123"
FT   TRANSMEM        18..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         468
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   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