FL3H2_CROXC
ID FL3H2_CROXC Reviewed; 372 AA.
AC A0A4D6Q4T7;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Flavanone 3-dioxygenase F3H2 {ECO:0000305};
DE EC=1.14.11.9 {ECO:0000269|PubMed:31004005};
DE AltName: Full=Flavanone 3'-hydroxylase 2 {ECO:0000303|PubMed:31004005};
DE Short=CcF3H-2 {ECO:0000303|PubMed:31004005};
GN Name=F3H-2 {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 3-beta-hydroxylation of (2S)-flavanones to
CC 2R,3R-dihydroflavonols, which are intermediates in the biosynthesis of
CC flavonols, anthocyanidins, catechins and proanthocyanidins in plants
CC (PubMed:31004005). Can act on naringenin to produce dihydrokaempferol,
CC and on eriodictyol to produced dihydroquercetin (PubMed:31004005).
CC {ECO:0000269|PubMed:31004005}.
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:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18622;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-naringenin + 2-oxoglutarate + O2 = (2R,3R)-
CC dihydrokaempferol + CO2 + succinate; Xref=Rhea:RHEA:61084,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15401, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17846, ChEBI:CHEBI:30031;
CC Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61085;
CC Evidence={ECO:0000269|PubMed:31004005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-eriodictyol + 2-oxoglutarate + O2 = (2R,3R)-
CC dihydroquercetin + CO2 + succinate; Xref=Rhea:RHEA:61088,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17948, ChEBI:CHEBI:28412, ChEBI:CHEBI:30031;
CC Evidence={ECO:0000269|PubMed:31004005};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61089;
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; MK562523; QCF41218.1; -; mRNA.
DR AlphaFoldDB; A0A4D6Q4T7; -.
DR SMR; A0A4D6Q4T7; -.
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 GO; GO:0009813; P:flavonoid biosynthetic process; 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..372
FT /note="Flavanone 3-dioxygenase F3H2"
FT /id="PRO_0000448072"
FT DOMAIN 195..299
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 222
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 224
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 280
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 290
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 372 AA; 41384 MW; 03210BB71A4709D6 CRC64;
MAPVATATPF LPTISNETTL RQTFVRDEDE RPKVAYNVFS SEIPVISLEG IDEVDGRRAE
ICKKIVAACE DWGVFQVVDH GVDAGLISDM TRLAREFFAL PPEDKLRFDM TGGKKGGFIV
SSHLQGEAVQ DWREIVTYFS YPIRARDYSR WPDKPEDWRS VTKTYSEKLM ELACKLLGIL
SEAMGLDTEA LTKACVDMDQ KVVVNFYPKC PQPDLTLGLK RHTDPGTITL LLQDQVGGLQ
ATKDGGKTWI TVQPVEGAFV VNLGDHGHFL SNGRFKNADH QAVVNSNTSR LSIATFQNPA
PDAIVYPLAI REGEKPVLDE PITFAEMYRR KMSRDLELAN LKKLAKTENQ QVAEKAEVEA
VVQPKGLSEI LA
