ID B6T8K6_MAIZE Unreviewed; 485 AA.
AC B6T8K6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Cytochrome P450 CYP724B3 {ECO:0000313|EMBL:ACG33439.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ACG33439.1};
RN [1] {ECO:0000313|EMBL:ACG33439.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; EU961321; ACG33439.1; -; mRNA.
DR AlphaFoldDB; B6T8K6; -.
DR ExpressionAtlas; B6T8K6; baseline and differential.
DR GO; GO:0016020; C: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:0016132; P:brassinosteroid biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0009647; P:skotomorphogenesis; IEA:EnsemblPlants.
DR CDD; cd11043; CYP90-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24286; CYTOCHROME P450 26; 1.
DR PANTHER; PTHR24286:SF37; CYTOCHROME P450 724B1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 485 AA; 54399 MW; 96BA55D97D1E7993 CRC64;
MMMMMMAGEH VLAALGTLLL ASLLTLVLNH FLPLLLNPKA PRGSFGWPLL GETLRFLTPH
ASNTLGGFLE DHCSRYGRVF KSHLFCTPTV VSCDQDLNHF ILQNEERLFQ CSYPRPIHGI
LGKSSMLVVL GEDHKRLRNL ALALVTSTKL KPSYLGDIEK IALHVVGAWR RHGSSGGVRV
VAFCEEARKF AFSVIVKQVL GLSPEEPVTA RILEDFLAFM KGLISFPLYI PGTPYAKAVR
ARERISSTVK GIIKERRSAG SWNKQGDFLD VLLSSNELSD EEKVSFVLDS LLGGYETTSL
LISMVVYFLG QSAQDLDLVK REHDSIRSNK GKEECLTSED YKKMEYTQQV INEALRCGNI
VKFVHRKALK DVKYKEYLIP SGWKVLPVFT AVHLNPSLHG DAQQFQPCRW EGTSQGTSKR
FTPFGGGPRL CPGSELAKVE TAFFLHHLVL NYRWRIDGDD IPMAYPYVEF QRGLPIEIEP
TSPES
//
