ID   LDOX_ARATH              Reviewed;         356 AA.
AC   Q96323;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 169.
DE   RecName: Full=Leucoanthocyanidin dioxygenase;
DE            Short=LDOX;
DE            Short=Leucocyanidin oxygenase;
DE            EC=1.14.20.4 {ECO:0000269|PubMed:16153644};
DE   AltName: Full=Anthocyanidin synthase;
DE            Short=ANS;
DE   AltName: Full=Leucoanthocyanidin hydroxylase;
DE   AltName: Full=Protein TANNIN DEFICIENT SEED 4;
DE            Short=TDS4;
DE   AltName: Full=Protein TRANSPARENT TESTA 11;
DE            Short=TT11;
DE   AltName: Full=Protein TRANSPARENT TESTA 17;
DE            Short=TT17;
DE   AltName: Full=Protein TRANSPARENT TESTA 18;
DE            Short=TT18;
GN   Name=LDOX; OrderedLocusNames=At4g22880; ORFNames=F7H19.60;
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 [MRNA], AND INDUCTION BY LIGHT.
RC   STRAIN=cv. Columbia;
RX   PubMed=9112784; DOI=10.1104/pp.113.4.1437;
RA   Pelletier M.K., Murrell J.R., Shirley B.W.;
RT   "Characterization of flavonol synthase and leucoanthocyanidin dioxygenase
RT   genes in Arabidopsis. Further evidence for differential regulation of
RT   'early' and 'late' genes.";
RL   Plant Physiol. 113:1437-1445(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=10394944; DOI=10.1023/a:1026414301100;
RA   Pelletier M.K., Burbulis I.E., Winkel-Shirley B.;
RT   "Disruption of specific flavonoid genes enhances the accumulation of
RT   flavonoid enzymes and end-products in Arabidopsis seedlings.";
RL   Plant Mol. Biol. 40:45-54(1999).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-228.
RC   STRAIN=cv. Wassilewskija-4;
RX   PubMed=12940955; DOI=10.1046/j.1365-313x.2003.01834.x;
RA   Abrahams S., Lee E., Walker A.R., Tanner G.J., Larkin P.J., Ashton A.R.;
RT   "The Arabidopsis TDS4 gene encodes leucoanthocyanidin dioxygenase (LDOX)
RT   and is essential for proanthocyanidin synthesis and vacuole development.";
RL   Plant J. 35:624-636(2003).
RN   [7]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16153644; DOI=10.1016/j.febslet.2005.08.033;
RA   Welford R.W., Kirkpatrick J.M., McNeill L.A., Puri M., Oldham N.J.,
RA   Schofield C.J.;
RT   "Incorporation of oxygen into the succinate co-product of iron(II) and 2-
RT   oxoglutarate dependent oxygenases from bacteria, plants and humans.";
RL   FEBS Lett. 579:5170-5174(2005).
RN   [8]
RP   INDUCTION BY SUCROSE.
RX   PubMed=16384906; DOI=10.1104/pp.105.072579;
RA   Solfanelli C., Poggi A., Loreti E., Alpi A., Perata P.;
RT   "Sucrose-specific induction of the anthocyanin biosynthetic pathway in
RT   Arabidopsis.";
RL   Plant Physiol. 140:637-646(2006).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19433090; DOI=10.1016/j.febslet.2009.05.006;
RA   Preuss A., Stracke R., Weisshaar B., Hillebrecht A., Matern U., Martens S.;
RT   "Arabidopsis thaliana expresses a second functional flavonol synthase.";
RL   FEBS Lett. 583:1981-1986(2009).
RN   [10]
RP   INDUCTION.
RX   PubMed=19596700; DOI=10.1093/jxb/erp223;
RA   Shan X., Zhang Y., Peng W., Wang Z., Xie D.;
RT   "Molecular mechanism for jasmonate-induction of anthocyanin accumulation in
RT   Arabidopsis.";
RL   J. Exp. Bot. 60:3849-3860(2009).
RN   [11]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-78; CYS-220 AND
RP   GLY-228.
RC   STRAIN=cv. Est-1, cv. Landsberg erecta, and cv. Wassilewskija-4;
RX   PubMed=21683773; DOI=10.1016/j.gene.2011.05.031;
RA   Appelhagen I., Jahns O., Bartelniewoehner L., Sagasser M., Weisshaar B.,
RA   Stracke R.;
RT   "Leucoanthocyanidin dioxygenase in Arabidopsis thaliana: characterization
RT   of mutant alleles and regulation by MYB-BHLH-TTG1 transcription factor
RT   complexes.";
RL   Gene 484:61-68(2011).
RN   [12]
RP   REVIEW, AND NOMENCLATURE.
RX   PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA   Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA   Tohge T., Fernie A.R.;
RT   "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT   diversity.";
RL   Plant Physiol. Biochem. 72:21-34(2013).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH THE SUBSTRATE ANALOG
RP   DIHYDROQUERCETIN; 2-OXOGLUTARATE AND IRON ION, AND COFACTOR.
RX   PubMed=11796114; DOI=10.1016/s0969-2126(01)00695-5;
RA   Wilmouth R.C., Turnbull J.J., Welford R.W., Clifton I.J., Prescott A.G.,
RA   Schofield C.J.;
RT   "Structure and mechanism of anthocyanidin synthase from Arabidopsis
RT   thaliana.";
RL   Structure 10:93-103(2002).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-356 IN COMPLEX WITH THE
RP   SUBSTRATE ANALOG NARINGENIN; 2-OXOGLUTARATE AND IRON ION, FUNCTION,
RP   COFACTOR, AND MUTAGENESIS OF LYS-128; ASN-131; TYR-142; GLU-230 AND
RP   LYS-341.
RX   PubMed=16106293; DOI=10.1039/b507153d;
RA   Welford R.W., Clifton I.J., Turnbull J.J., Wilson S.C., Schofield C.J.;
RT   "Structural and mechanistic studies on anthocyanidin synthase catalysed
RT   oxidation of flavanone substrates: the effect of C-2 stereochemistry on
RT   product selectivity and mechanism.";
RL   Org. Biomol. Chem. 3:3117-3126(2005).
CC   -!- FUNCTION: Involved in anthocyanin and protoanthocyanidin biosynthesis
CC       by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins.
CC       Possesses low flavonol synthase activity in vitro towards
CC       dihydrokaempferol and dihydroquercetin producing kaempferol and
CC       quercitin, respectively. {ECO:0000269|PubMed:12940955,
CC       ECO:0000269|PubMed:16106293, ECO:0000269|PubMed:16153644,
CC       ECO:0000269|PubMed:19433090, ECO:0000269|PubMed:21683773}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + a (2R,3S,4S)-leucoanthocyanidin + O2 = a 4-H-
CC         anthocyanidin with a 3-hydroxy group + CO2 + 2 H2O + succinate;
CC         Xref=Rhea:RHEA:54432, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:138176, ChEBI:CHEBI:138177; EC=1.14.20.4;
CC         Evidence={ECO:0000269|PubMed:16153644};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S,4S)-3,4-leucopelargonidin + 2-oxoglutarate + O2 = (4S)-
CC         2,3-dehydroleucopelargonidin + CO2 + H(+) + H2O + succinate;
CC         Xref=Rhea:RHEA:10768, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:17343, ChEBI:CHEBI:30031, ChEBI:CHEBI:138950;
CC         EC=1.14.20.4; Evidence={ECO:0000269|PubMed:16153644};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3S,4S)-leucocyanidin + 2-oxoglutarate + O2 = (4S)-2,3-
CC         dehydroleucocyanidin + CO2 + H(+) + H2O + succinate;
CC         Xref=Rhea:RHEA:10764, ChEBI:CHEBI:11412, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138948;
CC         EC=1.14.20.4; Evidence={ECO:0000269|PubMed:16153644};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000269|PubMed:11796114, ECO:0000269|PubMed:16106293};
CC       Note=Binds 1 ascorbate molecule per subunit.
CC       {ECO:0000269|PubMed:11796114, ECO:0000269|PubMed:16106293};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:11796114, ECO:0000269|PubMed:16106293};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:11796114,
CC       ECO:0000269|PubMed:16106293};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC   -!- TISSUE SPECIFICITY: Expressed in young seedlings (at protein level).
CC       {ECO:0000269|PubMed:10394944}.
CC   -!- INDUCTION: By methyl jasmonate, 6-benzylaminopurine, light and sucrose.
CC       {ECO:0000269|PubMed:16384906, ECO:0000269|PubMed:19596700,
CC       ECO:0000269|PubMed:9112784}.
CC   -!- DISRUPTION PHENOTYPE: No accumulation of anthocyanins, accumulation of
CC       protoanthocyanidin intermediates and presence of numerous small
CC       vacuoles in leaf epidermal cells. {ECO:0000269|PubMed:12940955,
CC       ECO:0000269|PubMed:19433090, ECO:0000269|PubMed:21683773}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; U70478; AAB09572.1; -; mRNA.
DR   EMBL; AL031018; CAA19803.1; -; Genomic_DNA.
DR   EMBL; AL161558; CAB79243.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84672.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE84673.1; -; Genomic_DNA.
DR   EMBL; CP002687; ANM67022.1; -; Genomic_DNA.
DR   EMBL; AY088203; AAM65745.1; -; mRNA.
DR   PIR; T05119; T05119.
DR   RefSeq; NP_001031700.1; NM_001036623.1.
DR   RefSeq; NP_001320035.1; NM_001341563.1.
DR   RefSeq; NP_194019.1; NM_118417.2.
DR   PDB; 1GP4; X-ray; 2.10 A; A=1-356.
DR   PDB; 1GP5; X-ray; 2.20 A; A=1-356.
DR   PDB; 1GP6; X-ray; 1.75 A; A=1-356.
DR   PDB; 2BRT; X-ray; 2.20 A; A=2-356.
DR   PDBsum; 1GP4; -.
DR   PDBsum; 1GP5; -.
DR   PDBsum; 1GP6; -.
DR   PDBsum; 2BRT; -.
DR   AlphaFoldDB; Q96323; -.
DR   SMR; Q96323; -.
DR   BioGRID; 13676; 1.
DR   STRING; 3702.Q96323; -.
DR   iPTMnet; Q96323; -.
DR   PaxDb; 3702-AT4G22880-1; -.
DR   ProteomicsDB; 237135; -.
DR   EnsemblPlants; AT4G22880.1; AT4G22880.1; AT4G22880.
DR   EnsemblPlants; AT4G22880.2; AT4G22880.2; AT4G22880.
DR   EnsemblPlants; AT4G22880.3; AT4G22880.3; AT4G22880.
DR   GeneID; 828387; -.
DR   Gramene; AT4G22880.1; AT4G22880.1; AT4G22880.
DR   Gramene; AT4G22880.2; AT4G22880.2; AT4G22880.
DR   Gramene; AT4G22880.3; AT4G22880.3; AT4G22880.
DR   KEGG; ath:AT4G22880; -.
DR   Araport; AT4G22880; -.
DR   TAIR; AT4G22880; LDOX.
DR   eggNOG; KOG0143; Eukaryota.
DR   HOGENOM; CLU_010119_16_2_1; -.
DR   InParanoid; Q96323; -.
DR   OMA; AGMRILH; -.
DR   OrthoDB; 1057251at2759; -.
DR   PhylomeDB; Q96323; -.
DR   BioCyc; ARA:AT4G22880-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G22880-MONOMER; -.
DR   BRENDA; 1.14.20.4; 399.
DR   UniPathway; UPA00009; -.
DR   EvolutionaryTrace; Q96323; -.
DR   PRO; PR:Q96323; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q96323; baseline and differential.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0050589; F:leucocyanidin oxygenase activity; ISS:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; TAS:TAIR.
DR   GO; GO:0010023; P:proanthocyanidin biosynthetic process; IMP:TAIR.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR   GO; GO:0007033; P:vacuole organization; IMP:TAIR.
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   PANTHER; PTHR47991:SF200; ANTHOCYANIDIN SYNTHASE; 1.
DR   PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
DR   Genevisible; Q96323; AT.
PE   1: Evidence at protein level;
KW   3D-structure; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Reference proteome; Vitamin C.
FT   CHAIN           1..356
FT                   /note="Leucoanthocyanidin dioxygenase"
FT                   /id="PRO_0000067299"
FT   DOMAIN          208..307
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         215..217
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         232
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         234
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         288
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         298..300
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   BINDING         341
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:11796114,
FT                   ECO:0000269|PubMed:16106293"
FT   MUTAGEN         78
FT                   /note="G->E: In tt11-2; no accumulation of anthocyanin."
FT                   /evidence="ECO:0000269|PubMed:21683773"
FT   MUTAGEN         128
FT                   /note="K->A: Retains two-third of the original activity."
FT                   /evidence="ECO:0000269|PubMed:16106293"
FT   MUTAGEN         131
FT                   /note="N->A,D: Retains two-third of the original activity."
FT                   /evidence="ECO:0000269|PubMed:16106293"
FT   MUTAGEN         142
FT                   /note="Y->H: Retains two-third of the original activity."
FT                   /evidence="ECO:0000269|PubMed:16106293"
FT   MUTAGEN         220
FT                   /note="C->Y: In tt17; no accumulation of anthocyanin."
FT                   /evidence="ECO:0000269|PubMed:21683773"
FT   MUTAGEN         228
FT                   /note="G->D: In tds4-1; no accumulation of anthocyanin."
FT                   /evidence="ECO:0000269|PubMed:12940955,
FT                   ECO:0000269|PubMed:21683773"
FT   MUTAGEN         230
FT                   /note="E->Q: Retains one half of the original activity."
FT                   /evidence="ECO:0000269|PubMed:16106293"
FT   MUTAGEN         341
FT                   /note="K->N: Retains two-third of the original activity."
FT                   /evidence="ECO:0000269|PubMed:16106293"
FT   HELIX           7..12
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           26..29
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           35..40
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   TURN            53..56
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           60..76
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           89..103
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           111..113
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           117..119
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:2BRT"
FT   STRAND          141..149
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           155..157
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           165..190
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           197..201
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          209..217
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          228..232
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          236..243
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          249..253
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          256..259
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          267..271
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           273..278
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   TURN            279..281
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          298..306
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   TURN            309..311
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           318..320
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   STRAND          323..325
FT                   /evidence="ECO:0007829|PDB:1GP6"
FT   HELIX           334..349
FT                   /evidence="ECO:0007829|PDB:1GP6"
SQ   SEQUENCE   356 AA;  40396 MW;  1B74AE3A54056201 CRC64;
     MVAVERVESL AKSGIISIPK EYIRPKEELE SINDVFLEEK KEDGPQVPTI DLKNIESDDE
     KIRENCIEEL KKASLDWGVM HLINHGIPAD LMERVKKAGE EFFSLSVEEK EKYANDQATG
     KIQGYGSKLA NNASGQLEWE DYFFHLAYPE EKRDLSIWPK TPSDYIEATS EYAKCLRLLA
     TKVFKALSVG LGLEPDRLEK EVGGLEELLL QMKINYYPKC PQPELALGVE AHTDVSALTF
     ILHNMVPGLQ LFYEGKWVTA KCVPDSIVMH IGDTLEILSN GKYKSILHRG LVNKEKVRIS
     WAVFCEPPKD KIVLKPLPEM VSVESPAKFP PRTFAQHIEH KLFGKEQEEL VSEKND
//