FLS_PETCR
ID FLS_PETCR Reviewed; 337 AA.
AC Q7XZQ6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE EC=1.14.11.9 {ECO:0000269|PubMed:12782296};
DE EC=1.14.20.6 {ECO:0000269|PubMed:12782296};
GN Name=FLS;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Italian Giant;
RX PubMed=12782296; DOI=10.1016/s0014-5793(03)00479-4;
RA Martens S., Forkmann G., Britsch L., Wellmann F., Matern U., Lukacin R.;
RT "Divergent evolution of flavonoid 2-oxoglutarate-dependent dioxygenases in
RT parsley.";
RL FEBS Lett. 544:93-98(2003).
CC -!- FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols.
CC Acts on (2S)-naringenin and (+)-trans-dihydrokaempferol to produce
CC kaempferol and on (2R)-naringenin to produce (-)-trans-
CC dihydrokaempferol. {ECO:0000269|PubMed:12782296}.
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:12782296};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + a (2S)-flavan-4-one + O2 = a (2R,3R)-
CC dihydroflavonol + CO2 + succinate; Xref=Rhea:RHEA:18621,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:138188, ChEBI:CHEBI:140377;
CC EC=1.14.11.9; Evidence={ECO:0000269|PubMed:12782296};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC Note=Binds 1 ascorbate molecule per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AY230249; AAP57395.1; -; mRNA.
DR AlphaFoldDB; Q7XZQ6; -.
DR SMR; Q7XZQ6; -.
DR KEGG; ag:AAP57395; -.
DR BRENDA; 1.14.20.6; 4694.
DR UniPathway; UPA00154; -.
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 GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:UniProtKB-EC.
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..337
FT /note="Flavonol synthase/flavanone 3-hydroxylase"
FT /id="PRO_0000387507"
FT DOMAIN 198..298
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 223
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 225
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 279
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 337 AA; 38208 MW; A5E4A5C3EF0D6FCD CRC64;
MEVERVQAIS KMSRCMDTIP SEYIRSESEQ PAVTTMQGVV LQVPVIDLGS SNNTEENLVE
LIAEASREWG IFQVVNHGIP DDAIAKLQKV GKEFFELPQQ EKEVIAKPEG YQGVEGYGTK
LQKELGGKKG WVDHLFHIIW PKSAVNYNFW PNNPPLYREA NEEYAVALRG VVDKLFEALS
LGIGLEKHEL KKASGGDDLI YMLKINYYPP CPRPDLALGV VAHTDMSAIT ILVPNEVQGL
QVHKDDHWYD VKYIPNALII HIGDQIEIMS NGKYKSVYHR TTVNKDKTRM SWPVFLEPPP
ELLTGPISKL ITDENPAKFK TKKYKDYVYC KLNKLPQ
