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C75A2_SOLME
ID   C75A2_SOLME             Reviewed;         513 AA.
AC   P37120;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Flavonoid 3',5'-hydroxylase;
DE            Short=F3'5'H;
DE            EC=1.14.14.81 {ECO:0000250|UniProtKB:P48418};
DE   AltName: Full=CYPLXXVA2;
DE   AltName: Full=Cytochrome P450 75A2;
DE   AltName: Full=P-450EG1;
GN   Name=CYP75A2; Synonyms=CYP75, CYPEG1;
OS   Solanum melongena (Eggplant) (Aubergine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Sinsadoharanasu; TISSUE=Hypocotyl;
RX   PubMed=8260632; DOI=10.1007/bf00021810;
RA   Toguri T., Umemoto N., Kobayashi O., Ohtani T.;
RT   "Activation of anthocyanin synthesis genes by white light in eggplant
RT   hypocotyl tissues, and identification of an inducible P-450 cDNA.";
RL   Plant Mol. Biol. 23:933-946(1993).
CC   -!- FUNCTION: Catalyzes the 3'5'-hydroxylation of naringenin and
CC       eriodictyol to form 5,7,3,'4',5'-pentahydroxyflavanone and 3',5'-
CC       hydroxylation of dihydrokaempferol and dihydroquercetin to form
CC       dihydromyricetin. {ECO:0000250|UniProtKB:P48418}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 3',5'-unsubstituted flavanone + 2 O2 + 2 reduced [NADPH--
CC         hemoprotein reductase] = a 3',5'-dihydroxyflavanone + 2 H(+) + 2 H2O
CC         + 2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:55448,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:48025,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:138897;
CC         EC=1.14.14.81; Evidence={ECO:0000250|UniProtKB:P48418};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Hypocotyl tissues.
CC   -!- DEVELOPMENTAL STAGE: Most abundant during the mid stage of flower bud
CC       development but not detected in leaf tissues.
CC   -!- INDUCTION: By white light.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X70824; CAA50155.1; -; mRNA.
DR   PIR; S43342; S43342.
DR   AlphaFoldDB; P37120; -.
DR   SMR; P37120; -.
DR   BRENDA; 1.14.14.81; 5755.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0033772; F:flavonoid 3',5'-hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
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; Metal-binding; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..513
FT                   /note="Flavonoid 3',5'-hydroxylase"
FT                   /id="PRO_0000052131"
FT   BINDING         446
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   513 AA;  57784 MW;  D0434B46B68535EB CRC64;
     MVILPSELIG ATIIYIIVYI IIQKLIATGS WRRRRLPPGP EGWPVIGALP LLGGMPHVAL
     AKMAKKYGPI MYLKVGTCGM VVASTPNAAK AFLKTLDINF SNRPPNAGAT HMAYNAQDMV
     FAPYGPRWKL LRKLSNLHML GGKALENWAN VRANELGHML KSMFDASHVG ERIVVADMLT
     FAMANMIGQV MLSKRVFVEK GKEVNEFKNM VVELMTVAGY FNIGDFIPQI AWMDLQGIEK
     GMKKLHKKFD DLLTKMFEEH EATSNERKGK PDFLDFIMAN RDNSEGERLS ITNIKALLLN
     LFTAGTDTSS SVIEWALTEM MKNPTIFKKA QQEMDQIIGK NRRFIESDIP NLPYLRAICK
     EAFRKHPSTP LNLPRVSSDA CTIDGYYIPK NTRLSVNIWA IGRDPDVWEN PLEFIPERFL
     SEKNAKIEHR GNDFELIPFG AGRRICAGTR MGIVMVEYIL GTLIHSFDWK LPNDVVDINM
     EETFGLALQK AVPLEAIVTP RLSFDIYQSS EPF
 
 
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