C93E1_SOYBN
ID C93E1_SOYBN Reviewed; 513 AA.
AC Q9XHC6; Q1JV37;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Beta-amyrin 24-hydroxylase;
DE EC=1.14.14.134 {ECO:0000269|PubMed:16478469};
DE AltName: Full=Cytochrome P450 93E1;
DE AltName: Full=Sophoradiol 24-hydroxylase;
GN Name=CYP93E1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10375412; DOI=10.1006/abbi.1999.1238;
RA Steele C.L., Gijzen M., Qutob D., Dixon R.A.;
RT "Molecular characterization of the enzyme catalyzing the aryl migration
RT reaction of isoflavonoid biosynthesis in soybean.";
RL Arch. Biochem. Biophys. 367:146-150(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16478469; DOI=10.1111/j.1742-4658.2006.05120.x;
RA Shibuya M., Hoshino M., Katsube Y., Hayashi H., Kushiro T., Ebizuka Y.;
RT "Identification of beta-amyrin and sophoradiol 24-hydroxylase by expressed
RT sequence tag mining and functional expression assay.";
RL FEBS J. 273:948-959(2006).
CC -!- FUNCTION: Heme-containing cytochrome P450 involved in the biosynthesis
CC of soyasaponins. Hydroxylates specifically the C-24 methyl group of the
CC triterpenes beta-amyrin and sophoradiol. No activity with lupeol,
CC butyrospermol, tirucalla-7,21-dien-3beta-ol, taraxasterol, psi-
CC taraxasterol, bauerenol, alpha-amyrin and multiflorenol as substrates.
CC {ECO:0000269|PubMed:16478469}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-amyrin + O2 + reduced [NADPH--hemoprotein reductase] =
CC 24-hydroxy-beta-amyrin + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:30991, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:10352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:62459; EC=1.14.14.134;
CC Evidence={ECO:0000269|PubMed:16478469};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=O2 + reduced [NADPH--hemoprotein reductase] + sophoradiol =
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + soyasapogenol
CC B; Xref=Rhea:RHEA:30995, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:9209, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:62458; EC=1.14.14.134;
CC Evidence={ECO:0000269|PubMed:16478469};
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; AF135485; AAD38930.1; -; mRNA.
DR EMBL; AB231332; BAE94181.1; -; mRNA.
DR RefSeq; NP_001236154.1; NM_001249225.1.
DR AlphaFoldDB; Q9XHC6; -.
DR SMR; Q9XHC6; -.
DR STRING; 3847.GLYMA08G46520.1; -.
DR EnsemblPlants; KRH46682; KRH46682; GLYMA_08G350800.
DR GeneID; 100037459; -.
DR Gramene; KRH46682; KRH46682; GLYMA_08G350800.
DR KEGG; gmx:100037459; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9XHC6; -.
DR OMA; DYFFIPY; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.134; 2483.
DR Proteomes; UP000008827; Chromosome 8.
DR Genevisible; Q9XHC6; GM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
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 Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..513
FT /note="Beta-amyrin 24-hydroxylase"
FT /id="PRO_0000412836"
FT TRANSMEM 1..21
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT BINDING 451
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 CONFLICT 41
FT /note="I -> V (in Ref. 2; BAE94181)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="V -> L (in Ref. 2; BAE94181)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58262 MW; DAF031C38157C403 CRC64;
MLDIKGYLVL FFLWFISTIL IRSIFKKPQR LRLPPGPPIS IPLLGHAPYL RSLLHQALYK
LSLRYGPLIH VMIGSKHVVV ASSAETAKQI LKTSEEAFCN RPLMIASESL TYGAADYFFI
PYGTYWRFLK KLCMTELLSG KTLEHFVRIR ESEVEAFLKR MMEISGNGNY EVVMRKELIT
HTNNIITRMI MGKKSNAEND EVARLRKVVR EVGELLGAFN LGDVIGFMRP LDLQGFGKKN
METHHKVDAM MEKVLREHEE ARAKEDADSD RKKDLFDILL NLIEADGADN KLTRESAKAF
ALDMFIAGTN GPASVLEWSL AELVRNPHVF KKAREEIESV VGKERLVKES DIPNLPYLQA
VLKETLRLHP PTPIFAREAM RTCQVEGYDI PENSTILIST WAIGRDPNYW DDALEYKPER
FLFSDDPGKS KIDVRGQYYQ LLPFGSGRRS CPGASLALLV MQATLASLIQ CFDWIVNDGK
NHHVDMSEEG RVTVFLAKPL KCKPVPRFTP FAA