FLS5_ARATH
ID FLS5_ARATH Reviewed; 325 AA.
AC Q9FFQ4;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable flavonol synthase 5;
DE EC=1.14.20.6;
GN Name=FLS5; OrderedLocusNames=At5g63600; ORFNames=MBK5.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18467451; DOI=10.1104/pp.108.117457;
RA Owens D.K., Alerding A.B., Crosby K.C., Bandara A.B., Westwood J.H.,
RA Winkel B.S.;
RT "Functional analysis of a predicted flavonol synthase gene family in
RT Arabidopsis.";
RL Plant Physiol. 147:1046-1061(2008).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. No-0;
RX PubMed=18998159; DOI=10.1007/s00425-008-0841-y;
RA Stracke R., De Vos R.C., Bartelniewoehner L., Ishihara H., Sagasser M.,
RA Martens S., Weisshaar B.;
RT "Metabolomic and genetic analyses of flavonol synthesis in Arabidopsis
RT thaliana support the in vivo involvement of leucoanthocyanidin
RT dioxygenase.";
RL Planta 229:427-445(2009).
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;
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: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FFQ4-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in young seedlings.
CC {ECO:0000269|PubMed:18467451}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18467451, ECO:0000269|PubMed:18998159}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AB005234; BAB10453.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97774.1; -; Genomic_DNA.
DR EMBL; AY063971; AAL36327.1; -; mRNA.
DR EMBL; AY114035; AAM45083.1; -; mRNA.
DR RefSeq; NP_201165.1; NM_125755.4. [Q9FFQ4-1]
DR AlphaFoldDB; Q9FFQ4; -.
DR SMR; Q9FFQ4; -.
DR BioGRID; 21722; 2.
DR STRING; 3702.AT5G63600.2; -.
DR iPTMnet; Q9FFQ4; -.
DR PaxDb; Q9FFQ4; -.
DR PRIDE; Q9FFQ4; -.
DR ProteomicsDB; 230605; -. [Q9FFQ4-1]
DR EnsemblPlants; AT5G63600.1; AT5G63600.1; AT5G63600. [Q9FFQ4-1]
DR GeneID; 836480; -.
DR Gramene; AT5G63600.1; AT5G63600.1; AT5G63600. [Q9FFQ4-1]
DR KEGG; ath:AT5G63600; -.
DR Araport; AT5G63600; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_2_1; -.
DR InParanoid; Q9FFQ4; -.
DR OMA; NEEYCRY; -.
DR PhylomeDB; Q9FFQ4; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q9FFQ4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFQ4; baseline and differential.
DR Genevisible; Q9FFQ4; AT.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0045431; F:flavonol synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..325
FT /note="Probable flavonol synthase 5"
FT /id="PRO_0000418027"
FT DOMAIN 180..280
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 188..190
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 207
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 261
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 271..273
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
SQ SEQUENCE 325 AA; 36964 MW; 56318D7C0482C14B CRC64;
MEEERDHNAS ESSLPSLSKQ LESSTLGGSA VDVPVVDLSV SDEDFLVREV VKASEEWGVF
QVVNHGIPTE LMRQLQMVGT QFFELPDAEK ETVAKEEDFE GYKKNYLGGI NNWDEHLFHR
LSPPSIINYK YWPKNPPQYR EVTEEYTKHM KRLTEKILGW LSEGLGLQRE TFTQSIGGDT
AEYVLRVNFY PPTQDTELVI GAAAHSDMGA IALLIPNEVP GLQAFKDEQW LDLDYIDSAV
VVIIGDQLMR MTNGRLKNVL HRAKSDKDKL RISWPVFVAP RADMSVGPLP EFTGDENPPK
FETLIYNDYI DQKIRGWALE DLPVY
