ID   C98A1_SORBI             Reviewed;         512 AA.
AC   O48956;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Cytochrome P450 98A1;
DE            EC=1.14.-.-;
GN   Name=CYP98A1;
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}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF029856; AAC39316.1; -; mRNA.
DR   PIR; T14638; T14638.
DR   RefSeq; XP_002440001.1; XM_002439956.1.
DR   AlphaFoldDB; O48956; -.
DR   SMR; O48956; -.
DR   STRING; 4558.Sb09g024210.1; -.
DR   EnsemblPlants; EES18431; EES18431; SORBI_3009G181800.
DR   GeneID; 8077042; -.
DR   Gramene; EES18431; EES18431; SORBI_3009G181800.
DR   KEGG; sbi:8077042; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_4_0_1; -.
DR   OMA; NYGFRIE; -.
DR   OrthoDB; 702827at2759; -.
DR   ExpressionAtlas; O48956; baseline and differential.
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   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;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..512
FT                   /note="Cytochrome P450 98A1"
FT                   /id="PRO_0000052197"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         441
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   512 AA;  58272 MW;  75CA4D9ACF221465 CRC64;
     MDASLLLSVA LAVVLIPLSL ALLNRLRLGR LPPGPRPWPV LGNLRQIKPI RCRCFQEWAE
     RYGPVISVWF GSGLTVVVST SELAKEVLKE NDQQLADRPR NRSTQRFSRN GQDLIWADYG
     PHYIKVRKLC NLELFTPKRL EALRPIREDE VTAMVESVYR AATAPGNEGK PMVVRNHLSM
     VAFNNITRLA FGKRFMNANG DIDEQGREFK TIVNNGIKIG ASLSVAEFIW YLRWLCPLNE
     ELYKTHNERR DRLTMKIIEE HAKSLKESGA KQHFVDALFT LKQQYDLSED TVIGLLWDMI
     TAGMDTTVIS VEWAMAELVR NPRVQKKLQE ELDRVVGRDR VMLETDFQNL PYLQAVVKES
     LRLHPPTPLM LPHKASTNVK IGGYDIPKGA NVMVNVWAVA RDPKVWSNPL EYRPERFLEE
     NIDIKGSDFR VLPFGAGRRV CPGAQLGINL VASMIGHLLH HFEWSLPEGT RPEDVNMMES
     PGLVTFMGTP LQAVAKPRLE KEELYNRVPV EM