FLS1_CROXC
ID FLS1_CROXC Reviewed; 331 AA.
AC A0A4D6Q440;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 10.
DE RecName: Full=Flavonol synthase 1 {ECO:0000303|PubMed:31004005};
DE Short=CcFLS1 {ECO:0000303|PubMed:31004005};
DE EC=1.14.20.6 {ECO:0000269|PubMed:31004005};
GN Name=FLS1 {ECO:0000303|PubMed:31004005};
GN Synonyms=FLS {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, COFACTOR, AND
RP TISSUE 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: Catalyzes the formation of flavonols from dihydroflavonols
CC (PubMed:31004005). Can act on dihydrokaempferol to produce kaempferol,
CC on dihydroquercetin to produce quercitin and on dihydromyricetin to
CC produce myricetin (PubMed:31004005). {ECO:0000269|PubMed:31004005}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a (2R,3R)-dihydroflavonol + O2 = a flavonol +
CC CO2 + H2O + succinate; Xref=Rhea:RHEA:21088, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:28802, ChEBI:CHEBI:30031, ChEBI:CHEBI:138188;
CC EC=1.14.20.6; Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21089;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-dihydrokaempferol + 2-oxoglutarate + O2 = CO2 + H(+) +
CC H2O + kaempferol + succinate; Xref=Rhea:RHEA:61132,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15401, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:58573;
CC Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61133;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-dihydroquercetin + 2-oxoglutarate + O2 = CO2 + H(+) +
CC H2O + quercetin + succinate; Xref=Rhea:RHEA:61136, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17948, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:57694; Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61137;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-dihydromyricetin + 2-oxoglutarate + O2 = CO2 + H(+) +
CC H2O + myricetin + succinate; Xref=Rhea:RHEA:61140, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28429, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:58395; Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61141;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000305|PubMed:31004005};
CC Note=Binds 1 ascorbate molecule per subunit.
CC {ECO:0000305|PubMed:31004005};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Flavonoid metabolism. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in young cromes.
CC {ECO:0000269|PubMed:31004005}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; MK562524; QCF41219.1; -; mRNA.
DR AlphaFoldDB; A0A4D6Q440; -.
DR SMR; A0A4D6Q440; -.
DR GO; GO:0045431; F:flavonol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR026992; DIOX_N.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Vitamin C.
FT CHAIN 1..331
FT /note="Flavonol synthase 1"
FT /id="PRO_0000448073"
FT DOMAIN 191..292
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 217
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 219
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 273
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 283
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 331 AA; 37569 MW; 8F1E770E3998E692 CRC64;
MEVERVQAIA SLGQKLDTIP SEFIRSEHEQ PGKTTFDGPI PEIPVIDLGD KDGIVGAVAE
AAREWGLFQI INHGIPVEVI KELQRVGKEF FELPQEEKEV YAMDMVTMEG YGTKLQKETE
GKKAWVDHLF HNIWPESRIN YNFWPQNPPD YRKANKEYAK HLLEVMGEIL TSLSLGLGLE
GHVFKEALGG DAIELLLKIN YYPTCPRPDL ALGVPAHTDM SAITLLVPNE VPGLQVFKDD
HWFDAKYIPN AIIVHIGDQI EILSNGKYKS VLHRTTVNKE KVRMSWPVFC SPPGEWMVGT
LPQLVSEDTP AKYKTKKYKD YQYCKLNKLP Q
