C79A1_SORBI
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 03-AUG-2022, entry version 133.
DE RecName: Full=Tyrosine N-monooxygenase;
DE EC=1.14.14.36 {ECO:0000269|PubMed:7937883};
DE AltName: Full=Cytochrome P450 79A1;
DE AltName: Full=Cytochrome P450Tyr;
GN Name=CYP79A1; Synonyms=CYP79;
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], 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 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, FUNCTION, AND CATALYTIC ACTIVITY.
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 catalyzes
RT the committed step in the biosynthesis of the cyanogenic glucoside dhurrin
RT 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. {ECO:0000269|PubMed:7937883}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tyrosine + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] =
CC (E)-4-hydroxyphenylacetaldehyde oxime + CO2 + 2 H(+) + 3 H2O + 2
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:32311,
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:16526, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:58315; EC=1.14.14.36;
CC Evidence={ECO:0000269|PubMed:7937883};
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 1/3.
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; U32624; AAA85440.1; -; mRNA.
DR PIR; S68203; S68203.
DR RefSeq; XP_002466099.1; XM_002466054.1.
DR AlphaFoldDB; Q43135; -.
DR SMR; Q43135; -.
DR STRING; 4558.Sb01g001200.1; -.
DR EnsemblPlants; EER93097; EER93097; SORBI_3001G012300.
DR GeneID; 8061413; -.
DR Gramene; EER93097; EER93097; SORBI_3001G012300.
DR KEGG; sbi:8061413; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR OMA; DEPLKYK; -.
DR OrthoDB; 702827at2759; -.
DR BioCyc; MetaCyc:MON-521; -.
DR BRENDA; 1.14.14.36; 5768.
DR SABIO-RK; Q43135; -.
DR UniPathway; UPA00757; UER00744.
DR ExpressionAtlas; Q43135; 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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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 Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7937883"
FT CHAIN 2..558
FT /note="Tyrosine N-monooxygenase"
FT /id="PRO_0000052152"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 493
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 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
