ID   FNSI_PETCR              Reviewed;         365 AA.
AC   Q7XZQ8;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Flavone synthase;
DE            EC=1.14.20.5 {ECO:0000269|PubMed:11524111, ECO:0000269|PubMed:12782296};
DE   AltName: Full=Flavone synthase I;
GN   Name=FNSI;
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], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Italian Giant;
RX   PubMed=11524111; DOI=10.1016/s0031-9422(01)00191-1;
RA   Martens S., Forkmann G., Matern U., Lukacin R.;
RT   "Cloning of parsley flavone synthase I.";
RL   Phytochemistry 58:43-46(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], 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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15913674; DOI=10.1016/j.phytochem.2005.03.030;
RA   Gebhardt Y., Witte S., Forkmann G., Lukacin R., Matern U., Martens S.;
RT   "Molecular evolution of flavonoid dioxygenases in the family Apiaceae.";
RL   Phytochemistry 66:1273-1284(2005).
CC   -!- FUNCTION: Involved in the conversion of naringenin to apigenin. Acts
CC       via a direct 2,3-desaturation of flavanones instead of a sequential
CC       hydroxylation/dehydratation mechanism.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + a flavanone + O2 = a flavone + CO2 + H2O +
CC         succinate; Xref=Rhea:RHEA:10448, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:24043, ChEBI:CHEBI:28863, ChEBI:CHEBI:30031;
CC         EC=1.14.20.5; Evidence={ECO:0000269|PubMed:11524111,
CC         ECO:0000269|PubMed:12782296};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11524111}. Note=In
CC       contrast to the microsmal flavone synthase II, FNSI is a soluble
CC       enzyme.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AY230247; AAP57393.1; -; mRNA.
DR   EMBL; AY817680; AAX21541.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7XZQ8; -.
DR   SMR; Q7XZQ8; -.
DR   KEGG; ag:AAP57393; -.
DR   BioCyc; MetaCyc:MON-12564; -.
DR   BRENDA; 1.14.20.5; 4694.
DR   UniPathway; UPA00154; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033759; F:flavone 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   Cytoplasm; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW   Vitamin C.
FT   CHAIN           1..365
FT                   /note="Flavone synthase"
FT                   /id="PRO_0000386540"
FT   DOMAIN          194..295
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          345..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         76
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         220
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         276
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   365 AA;  41024 MW;  998F555925432115 CRC64;
     MAPTTITALA KEKTLNLDFV RDEDERPKVA YNQFSNEIPI ISLAGLDDDS DGRRPEICRK
     IVKACEDWGI FQVVDHGIDS GLISEMTRLS REFFALPAEE KLEYDTTGGK RGGFTISTVL
     QGDDAMDWRE FVTYFSYPIN ARDYSRWPKK PEGWRSTTEV YSEKLMVLGA KLLEVLSEAM
     GLEKGDLTKA CVDMEQKVLI NYYPTCPQPD LTLGVRRHTD PGTITILLQD MVGGLQATRD
     GGKTWITVQP VEGAFVVNLG DHGHYLSNGR FRNADHQAVV NSTSSRLSIA TFQNPAQNAI
     VYPLKIREGE KAILDEAITY AEMYKKCMTK HIEVATRKKL AKEKRLQDEK AKLEMKSKSA
     DENLA