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}.
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; 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