ID   C79A1_SORBI             Reviewed;         558 AA.
AC   Q43135;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Tyrosine N-monooxygenase;
DE            EC=1.14.13.41;
DE   AltName: Full=Cytochrome P450Tyr;
DE   AltName: Full=Cytochrome P450 79A1;
GN   Name=CYP79A1; Synonyms=CYP79;
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], AND PROTEIN SEQUENCE OF 197-204; 277-282;
RP   330-361; 363-376; 390-399; 454-460; 473-480; 484-490 AND 532-558.
RC   STRAIN=cv. SS1000; TISSUE=Etiolated seedling;
RX   MEDLINE=96019962; PubMed=7487064; DOI=10.1006/abbi.1995.0024;
RA   Koch B.M., Sibbesen O., Halkier B.A., Svendsen I., Moeller B.L.;
RT   "The primary sequence of cytochrome P450tyr, the multifunctional N-
RT   hydroxylase catalyzing the conversion of L-tyrosine to p-
RT   hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic
RT   glucoside dhurrin in Sorghum bicolor (L.) Moench.";
RL   Arch. Biochem. Biophys. 323:177-186(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-17.
RX   PubMed=7937883; DOI=10.1073/pnas.91.21.9740;
RA   Sibbesen O., Koch B., Halkier B.A., Moller B.L.;
RT   "Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which
RT   catalyzes the committed step in the biosynthesis of the cyanogenic
RT   glucoside dhurrin in Sorghum bicolor (L.) Moench.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:9740-9744(1994).
CC   -!- FUNCTION: N-hydroxylase that converts L-tyrosine to p-
CC       hydroxyphenylacetaldehyde oxime.
CC   -!- CATALYTIC ACTIVITY: L-tyrosine + O(2) + NADPH = N-hydroxy-L-
CC       tyrosine + NADP(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: N-hydroxy-L-tyrosine + O(2) + NADPH = N,N-
CC       dihydroxy-L-tyrosine + NADP(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: N,N-dihydroxy-L-tyrosine = (Z)-[4-
CC       hydroxyphenylacetaldehyde oxime] + CO(2) + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- PATHWAY: Secondary metabolite biosynthesis; dhurrin biosynthesis;
CC       dhurrin from L-tyrosine: step 1/3.
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; U32624; AAA85440.1; -; mRNA.
DR   PIR; S68203; S68203.
DR   Gramene; Q43135; -.
DR   OMA; Q43135; MATMEVE.
DR   BioCyc; MetaCyc:MON-521; -.
DR   BRENDA; 1.14.13.41; 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:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050370; F:tyrosine N-monooxygenase activity; IEA:EC.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW   Membrane; Metal-binding; Monooxygenase; NADP; Oxidoreductase;
KW   Transmembrane.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    558       Tyrosine N-monooxygenase.
FT                                /FTId=PRO_0000052152.
FT   TRANSMEM     13     33       Potential.
FT   METAL       493    493       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   558 AA;  61887 MW;  83F435793CF651BA CRC64;
     MATMEVEAAA ATVLAAPLLS SSAILKLLLF VVTLSYLARA LRRPRKSTTK CSSTTCASPP
     AGVGNPPLPP GPVPWPVVGN LPEMLLNKPA FRWIHQMMRE MGTDIACVKL GGVHVVSITC
     PEIAREVLRK QDANFISRPL TFASETFSGG YRNAVLSPYG DQWKKMRRVL TSEIICPSRH
     AWLHDKRTDE ADNLTRYVYN LATKAATGDV AVDVRHVARH YCGNVIRRLM FNRRYFGEPQ
     ADGGPGPMEV LHMDAVFTSL GLLYAFCVSD YLPWLRGLDL DGHEKIVKEA NVAVNRLHDT
     VIDDRWRQWK SGERQEMEDF LDVLITLKDA QGNPLLTIEE VKAQSQDITF AAVDNPSNAV
     EWALAEMVNN PEVMAKAMEE LDRVVGRERL VQESDIPKLN YVKACIREAF RLHPVAPFNV
     PHVALADTTI AGYRVPKGSH VILSRTGLGR NPRVWDEPLR FYPDRHLATA ASDVALTEND
     LRFISFSTGR RGCIAASLGT AMSVMLFGRL LQGFTWSKPA GVEAVDLSES KSDTFMATPL
     VLHAEPRLPA HLYPSISI
//