FLS_CITUN
ID FLS_CITUN Reviewed; 335 AA.
AC Q9ZWQ9;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE EC=1.14.11.9 {ECO:0000250|UniProtKB:Q7XZQ6};
DE EC=1.14.20.6 {ECO:0000250|UniProtKB:Q7XZQ6};
DE AltName: Full=CitFLS;
DE Short=FLS;
GN Name=FLS;
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Satsuma Mandarin;
RX PubMed=11903972; DOI=10.1034/j.1399-3054.2002.1140211.x;
RA Moriguchi T., Kita M., Ogawa K., Tomono Y., Endo T., Omura M.;
RT "Flavonol synthase gene expression during citrus fruit development.";
RL Physiol. Plantarum 114:251-258(2002).
RN [2]
RP PROTEIN SEQUENCE OF 1-14, CHARACTERIZATION, AND MUTAGENESIS OF GLY-68 AND
RP GLY-261.
RX PubMed=12180990; DOI=10.1046/j.1432-1033.2002.03108.x;
RA Wellmann F., Lukacin R., Moriguchi T., Britsch L., Schiltz E., Matern U.;
RT "Functional expression and mutational analysis of flavonol synthase from
RT Citrus unshiu.";
RL Eur. J. Biochem. 269:4134-4142(2002).
RN [3]
RP FUNCTION.
RX PubMed=12620339; DOI=10.1016/s0031-9422(02)00567-8;
RA Lukacin R., Wellmann F., Britsch L., Martens S., Matern U.;
RT "Flavonol synthase from Citrus unshiu is a bifunctional dioxygenase.";
RL Phytochemistry 62:287-292(2003).
CC -!- FUNCTION: Catalyzes the formation of flavonols from dihydroflavonols.
CC It can act on dihydrokaempferol to produce kaempferol, on
CC dihydroquercetin to produce quercitin and on dihydromyricetin to
CC produce myricetin (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12620339}.
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:0000250|UniProtKB:Q7XZQ6};
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:0000250|UniProtKB:Q7XZQ6};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC Note=Binds 1 ascorbate molecule per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the juice sacs/segment epidermis (edible part)
CC at the early developmental stage.
CC -!- DEVELOPMENTAL STAGE: Increases in the peel during fruit maturation.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC 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; AB011796; BAA36554.1; -; mRNA.
DR AlphaFoldDB; Q9ZWQ9; -.
DR SMR; Q9ZWQ9; -.
DR KEGG; ag:BAA36554; -.
DR BioCyc; MetaCyc:MON-18283; -.
DR BRENDA; 1.14.20.6; 1428.
DR UniPathway; UPA00154; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Cytoplasm; Dioxygenase; Direct protein sequencing; Flavonoid biosynthesis;
KW Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT CHAIN 1..335
FT /note="Flavonol synthase/flavanone 3-hydroxylase"
FT /id="PRO_0000067292"
FT DOMAIN 196..296
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 221
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
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 277
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MUTAGEN 68
FT /note="G->A: Reduces activity 95%."
FT /evidence="ECO:0000269|PubMed:12180990"
FT MUTAGEN 68
FT /note="G->P: Results in complete loss of activity."
FT /evidence="ECO:0000269|PubMed:12180990"
FT MUTAGEN 207
FT /note="P->G: No effect."
FT MUTAGEN 261
FT /note="G->A: Reduces activity 95%."
FT /evidence="ECO:0000269|PubMed:12180990"
FT MUTAGEN 261
FT /note="G->P: Results in complete loss of activity."
FT /evidence="ECO:0000269|PubMed:12180990"
SQ SEQUENCE 335 AA; 37899 MW; 157E1AFA4C47564B CRC64;
MEVERVQAIA SLSHSNGTIP AEFIRPEKEQ PASTTYHGPA PEIPTIDLDD PVQDRLVRSI
AEASREWGIF QVTNHGIPSD LICKLQAVGK EFFELPQEEK EVYSRPADAK DVQGYGTKLQ
KEVEGKKSWV DHLFHRVWPP SSINYRFWPK NPPSYRAVNE EYAKYMREVV DKLFTYLSLG
LGVEGGVLKE AAGGDDIEYM LKINYYPPCP RPDLALGVVA HTDLSALTVL VPNEVPGLQV
FKDDRWIDAK YIPNALVIHI GDQIEILSNG KYKAVLHRTT VNKDKTRMSW PVFLEPPADT
VVGPLPQLVD DENPPKYKAK KFKDYSYCKL NKLPQ
