位置:首页 > 蛋白库 > C93E1_SOYBN
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025