ID   C99A1_SORBI             Reviewed;         519 AA.
AC   O48957;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cytochrome P450 CYP99A1;
DE            EC=1.14.-.-;
DE   Flags: Fragment;
GN   Name=CYP99A1;
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).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF029857; AAC39317.1; -; mRNA.
DR   PIR; T14639; T14639.
DR   AlphaFoldDB; O48957; -.
DR   SMR; O48957; -.
DR   STRING; 4558.Sb06g001030.1; -.
DR   PRIDE; O48957; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   ExpressionAtlas; O48957; differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   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   2: Evidence at transcript level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           <1..519
FT                   /note="Cytochrome P450 CYP99A1"
FT                   /id="PRO_0000052200"
FT   BINDING         453
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"
FT   NON_TER         1
SQ   SEQUENCE   519 AA;  57050 MW;  DBA10539D1D7387F CRC64;
     RLISAVILAV CSLISRRKPS PGSKKKRPPG PWRLPLIGNL LHLATSQPHV ALRDLAMKHG
     PVMYLRLGQV DAVVISSPAA AQEVLRDKDT TFASRPSLLV ADIILYGSMD MSFAPYGGNW
     RMLRKLCMSE LLNTHKVRQL AAVRDSETLS LVRKVVYAAG AGGGGRGQRG EAPVVNLGRL
     VLSCSMAITG RATLGKLCGD EIMSVVDVAV LYGSGFCAGD LFPSLWFVDV VTGLTRRLWT
     ARRRLDAIFD RILAECEARQ RQEEKMTGDD GFLGVLLRIR DDDGEPETGG ISTTSIKAIL
     FDMLAGGTET TSSAAEWIMS ELMRKPEAMA KAQAEVRGAL DGKSPEDHEG QMDKLSYTRM
     VVKEGLRLHP VLPLLLPRSC QETCDVGGFE VTKGTKVIVN AWALARSPER WHDPEEFRPE
     RFADDDGSSA AVAVDYRGSQ FEYIPFGSGR RMCPGNTFGL AALELMVARL LYYFDWSLPD
     GMRPEELDMD TVVGSTMRRR NHLHLVPSPY KETELTVGI