CYP1_CROXC
ID CYP1_CROXC Reviewed; 508 AA.
AC A0A4D6Q415;
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'-monooxygenase CYP75B137 {ECO:0000305};
DE EC=1.14.14.82 {ECO:0000269|PubMed:31004005};
DE AltName: Full=Cytochrome P450 1 {ECO:0000303|PubMed:31004005};
DE Short=CcCYP1 {ECO:0000303|PubMed:31004005};
DE AltName: Full=Cytochrome P450 75B137 {ECO:0000303|PubMed:31004005};
DE AltName: Full=Flavonoid 3'-hydroxylase CYP75B137 {ECO:0000305};
GN Name=CYP75B137 {ECO:0000303|PubMed:31004005};
GN Synonyms=CYP1 {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'-hydroxylase that catalyzes the 3'-hydroxylation
CC of flavanones, dihydroflavonols and flavonols (PubMed:31004005).
CC Converts narigenin to eriodictyol, dihydrokaempferol to
CC dihydroquercetin and kaempferol to quercetin (PubMed:31004005).
CC {ECO:0000269|PubMed:31004005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-unsubstituted flavone + O2 + reduced [NADPH--hemoprotein
CC reductase] = a 3'-hydroxyflavone + H(+) + H2O + oxidized [NADPH--
CC hemoprotein reductase]; Xref=Rhea:RHEA:16337, Rhea:RHEA-COMP:11964,
CC Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27741, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:138726; EC=1.14.14.82;
CC Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16338;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-naringenin + O2 + reduced [NADPH--hemoprotein reductase]
CC = (S)-eriodictyol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:61096, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17846, ChEBI:CHEBI:28412, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61097;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-dihydrokaempferol + O2 + reduced [NADPH--hemoprotein
CC reductase] = (2R,3R)-dihydroquercetin + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:61112, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15401,
CC ChEBI:CHEBI:17948, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61113;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=kaempferol + O2 + reduced [NADPH--hemoprotein reductase] =
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase] + quercetin;
CC Xref=Rhea:RHEA:61124, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:57694, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:58573; Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61125;
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; MK562520; QCF41215.1; -; mRNA.
DR AlphaFoldDB; A0A4D6Q415; -.
DR SMR; A0A4D6Q415; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016711; F:flavonoid 3'-monooxygenase 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..508
FT /note="Flavonoid 3'-monooxygenase CYP75B137"
FT /id="PRO_0000448074"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 445
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 508 AA; 56800 MW; E44B21AD8FFC332B CRC64;
MLTFFFLWIS TLLLSSFIVY LLYRRRSAQC PPLPPGPNGW PILGNLPQLG AKPHQTLDAL
SKQYGPLFRL RLGSVNVVVA SSSAVAAQFL RTHDVNFSNR PPNSGAEHVA YNYQDLVFAP
YGPRWRMLRK LCSVHLFSLK ALDDLRPVRQ GEVACLVRNL RRHADTGVLV NLGKALNVCA
TNALARAMLG RRVFADEDAQ LAEADEFKEM VVELMRLAGV FNVGDFVPGL GWLDLQGVVG
KMKRLHRRYD AFLDRVIEEN QANAKSGDLL SVLIRLKEAD AEGEIKLNNT DIKALLLNLF
TAGTDTSSST VEWVLAELIR HPDILQKTQH ELDSVIGRDR LVAESDLPNL PYLQAVVKET
FRLHPSTPLS LPRMASEECI VNGYKIPKHA TLLVNVWSIG RDAAVWNDPL EFRPSRFLPG
GEREHVDVKG NDFEVIPFGA GRRICAGLSL GLRMVQFMTA TIVHAYDWSL PKGQECQKLD
MEEAYGLTLQ RAVPLMVQPI PRLSHKAY
