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CYP2_CROXC
ID   CYP2_CROXC              Reviewed;         527 AA.
AC   A0A4D6Q414;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Flavonoid 3',5'-hydroxylase CYP75B138 {ECO:0000305};
DE            EC=1.14.14.81 {ECO:0000269|PubMed:31004005};
DE   AltName: Full=Cytochrome P450 2 {ECO:0000303|PubMed:31004005};
DE            Short=CcCYP2 {ECO:0000303|PubMed:31004005};
DE   AltName: Full=Cytochrome P450 75B132 {ECO:0000303|PubMed:31004005};
GN   Name=CYP75B138 {ECO:0000303|PubMed:31004005};
GN   Synonyms=CYP2 {ECO:0000303|PubMed:31004005};
OS   Crocosmia x crocosmiiflora (Montbretia) (Crocosmia aurea x Crocosmia
OS   pottsii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Iridaceae;
OC   Crocoideae; Freesieae; Crocosmia.
OX   NCBI_TaxID=1053288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=31004005; DOI=10.1104/pp.19.00254;
RA   Irmisch S., Ruebsam H., Jancsik S., Man Saint Yuen M., Madilao L.L.,
RA   Bohlmann J.;
RT   "Flavonol biosynthesis genes and their use in engineering the plant
RT   antidiabetic metabolite montbretin A.";
RL   Plant Physiol. 180:1277-1290(2019).
CC   -!- FUNCTION: Flavonoid 3',5'-hydroxylase that catalyzes the 3'- and 5'-
CC       hydroxylation of flavanones, dihydroflavonols and flavonols
CC       (PubMed:31004005). Converts narigenin to dihydrotricetin,
CC       dihydrokaempferol to dihydromyricetin and kaempferol to myricetin
CC       (PubMed:31004005). {ECO:0000269|PubMed:31004005}.
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:0000269|PubMed:31004005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55449;
CC         Evidence={ECO:0000269|PubMed:31004005};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-naringenin + 2 O2 + 2 reduced [NADPH--hemoprotein
CC         reductase] = (2S)-dihydrotricetin + 2 H(+) + 2 H2O + 2 oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61104, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17846,
CC         ChEBI:CHEBI:48026, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:31004005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61105;
CC         Evidence={ECO:0000269|PubMed:31004005};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-dihydrokaempferol + 2 O2 + 2 reduced [NADPH--
CC         hemoprotein reductase] = (2R,3R)-dihydromyricetin + 2 H(+) + 2 H2O +
CC         2 oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61108,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15401,
CC         ChEBI:CHEBI:28429, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000269|PubMed:31004005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61109;
CC         Evidence={ECO:0000269|PubMed:31004005};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=kaempferol + 2 O2 + 2 reduced [NADPH--hemoprotein reductase] =
CC         2 H(+) + 2 H2O + myricetin + 2 oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:61120, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58395,
CC         ChEBI:CHEBI:58573; Evidence={ECO:0000269|PubMed:31004005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61121;
CC         Evidence={ECO:0000269|PubMed:31004005};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- PATHWAY: Flavonoid metabolism. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in young cromes.
CC       {ECO:0000269|PubMed:31004005}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; MK562521; QCF41216.1; -; mRNA.
DR   AlphaFoldDB; A0A4D6Q414; -.
DR   SMR; A0A4D6Q414; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-KW.
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   Flavonoid biosynthesis; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   NADP; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..527
FT                   /note="Flavonoid 3',5'-hydroxylase CYP75B138"
FT                   /id="PRO_0000448075"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         459
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|UniProtKB:Q96242"
SQ   SEQUENCE   527 AA;  58429 MW;  5B3807061154E159 CRC64;
     MTMTSLDIIL FISAIVFLSI YYYNLFSNAK RSNGLKLPPG PKGYPVLGNL PQLGAKPHQA
     LQAFSRVYGP LMRLRLGSVD LVVASSPSVA AQFLKNDSNF CARPPNSGAE HMAFNYHDLV
     FAPYGPRWRL LRKLSAVHLL GPKALDDNQN VREEELAVLA RMLYERSRGG EPVNVGKEMH
     VCSTNALSRA MMGRRVFEKL AVGGGGVEEE EEMKKAEEFK DMVVEVMTLA GVFNIGDFVP
     WLKPFDIQGV VRKMKRVHRR YNVFLDKFIA ECRSSAKPGA NDLLSVLIGQ RGKSDGSGGE
     ITDTAIKALV LNLLTAGTDT SSSTIEWALT ELIRHPDILK KAQQEIDSAV GRDRLVTESD
     VPKLPYLQAI VKENFRMHPA TPLSLPRMSI EECDIGGYHI PKNSTLFVNI WAMGRDPSIW
     PDPMEFRPSR FLPGGQGEHL EVRGNHFELM PFGAGRRICA GTSMGIRVVH STVATLIHAF
     DWKLPEGLTA EKIDMEEAFG ISLQKAIPLM AHPIPRLAPK AYSPKMK
 
 
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