LDOX_ACTCC
ID LDOX_ACTCC Reviewed; 355 AA.
AC A0A2R6PI27; T2DJM4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Anthocyanin synthase {ECO:0000303|PubMed:30912865};
DE Short=AcANS {ECO:0000303|PubMed:30912865};
DE EC=1.14.20.4 {ECO:0000269|PubMed:30912865};
DE AltName: Full=Leucoanthocyanidin dioxygenase {ECO:0000303|PubMed:25143057};
DE Short=AcLDOX {ECO:0000303|PubMed:25143057};
DE Short=Leucocyanidin oxygenase {ECO:0000305};
GN Name=LDOX {ECO:0000303|PubMed:25143057};
GN Synonyms=ANS {ECO:0000303|PubMed:30912865},
GN ANS1 {ECO:0000303|PubMed:21175894}, ANS4 {ECO:0000303|PubMed:21175894};
GN ORFNames=CEY00_Acc28876 {ECO:0000312|EMBL:PSR91531.1};
OS Actinidia chinensis var. chinensis (Chinese soft-hair kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=1590841;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=25143057; DOI=10.1111/ppl.12263;
RA Man Y.P., Wang Y.C., Li Z.Z., Jiang Z.W., Yang H.L., Gong J.J., He S.S.,
RA Wu S.Q., Yang Z.Q., Zheng J., Wang Z.Y.;
RT "High-temperature inhibition of biosynthesis and transportation of
RT anthocyanins results in the poor red coloration in red-fleshed Actinidia
RT chinensis.";
RL Physiol. Plantarum 153:565-583(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Red5;
RX PubMed=29661190; DOI=10.1186/s12864-018-4656-3;
RA Pilkington S.M., Crowhurst R., Hilario E., Nardozza S., Fraser L., Peng Y.,
RA Gunaseelan K., Simpson R., Tahir J., Deroles S.C., Templeton K., Luo Z.,
RA Davy M., Cheng C., McNeilage M., Scaglione D., Liu Y., Zhang Q., Datson P.,
RA De Silva N., Gardiner S.E., Bassett H., Chagne D., McCallum J.,
RA Dzierzon H., Deng C., Wang Y.Y., Barron L., Manako K., Bowen J.,
RA Foster T.M., Erridge Z.A., Tiffin H., Waite C.N., Davies K.M.,
RA Grierson E.P., Laing W.A., Kirk R., Chen X., Wood M., Montefiori M.,
RA Brummell D.A., Schwinn K.E., Catanach A., Fullerton C., Li D.,
RA Meiyalaghan S., Nieuwenhuizen N., Read N., Prakash R., Hunter D., Zhang H.,
RA McKenzie M., Knabel M., Harris A., Allan A.C., Gleave A., Chen A.,
RA Janssen B.J., Plunkett B., Ampomah-Dwamena C., Voogd C., Leif D.,
RA Lafferty D., Souleyre E.J.F., Varkonyi-Gasic E., Gambi F., Hanley J.,
RA Yao J.L., Cheung J., David K.M., Warren B., Marsh K., Snowden K.C.,
RA Lin-Wang K., Brian L., Martinez-Sanchez M., Wang M., Ileperuma N.,
RA Macnee N., Campin R., McAtee P., Drummond R.S.M., Espley R.V.,
RA Ireland H.S., Wu R., Atkinson R.G., Karunairetnam S., Bulley S.,
RA Chunkath S., Hanley Z., Storey R., Thrimawithana A.H., Thomson S.,
RA David C., Testolin R., Huang H., Hellens R.P., Schaffer R.J.;
RT "A manually annotated Actinidia chinensis var. chinensis (kiwifruit) genome
RT highlights the challenges associated with draft genomes and gene prediction
RT in plants.";
RL BMC Genomics 19:257-257(2018).
RN [3]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21175894; DOI=10.1111/j.1365-313x.2010.04409.x;
RA Montefiori M., Espley R.V., Stevenson D., Cooney J., Datson P.M., Saiz A.,
RA Atkinson R.G., Hellens R.P., Allan A.C.;
RT "Identification and characterisation of F3GT1 and F3GGT1, two
RT glycosyltransferases responsible for anthocyanin biosynthesis in red-
RT fleshed kiwifruit (Actinidia chinensis).";
RL Plant J. 65:106-118(2011).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30912865; DOI=10.1111/tpj.14330;
RA Wang L., Tang W., Hu Y., Zhang Y., Sun J., Guo X., Lu H., Yang Y., Fang C.,
RA Niu X., Yue J., Fei Z., Liu Y.;
RT "A MYB/bHLH complex regulates tissue-specific anthocyanin biosynthesis in
RT the inner pericarp of red-centered kiwifruit Actinidia chinensis cv.
RT Hongyang.";
RL Plant J. 99:359-378(2019).
CC -!- FUNCTION: Involved in anthocyanin biosynthesis by catalyzing the
CC oxidation of leucoanthocyanidins into anthocyanidins (PubMed:30912865).
CC Required for the accumulation of anthocyanin in red-fleshed kiwifruit
CC varieties (PubMed:30912865). {ECO:0000269|PubMed:30912865}.
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:30912865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54433;
CC Evidence={ECO:0000269|PubMed:30912865};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000250|UniProtKB:Q96323};
CC Note=Binds 1 ascorbate molecule per subunit.
CC {ECO:0000250|UniProtKB:Q96323};
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: Pigment biosynthesis; anthocyanin biosynthesis. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in stems and leaves (PubMed:25143057).
CC Expressed at low levels in ovaries (PubMed:25143057, PubMed:21175894).
CC {ECO:0000269|PubMed:21175894, ECO:0000269|PubMed:25143057}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the inner and outer pericarps of
CC developing fruit from 20 to 49 days after flowering (DAF), and
CC expression decreases as the fruit ripens.
CC {ECO:0000269|PubMed:21175894}.
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; KF157392; AGV53047.1; -; mRNA.
DR EMBL; NKQK01000025; PSR91531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6PI27; -.
DR SMR; A0A2R6PI27; -.
DR STRING; 1590841.A0A2R6PI27; -.
DR EnsemblPlants; PSR91531; PSR91531; CEY00_Acc28876.
DR Gramene; PSR91531; PSR91531; CEY00_Acc28876.
DR OMA; PREYIRP; -.
DR UniPathway; UPA00009; -.
DR Proteomes; UP000241394; Chromosome lg25.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0050589; F:leucocyanidin oxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050498; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated; IDA:UniProtKB.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IDA:UniProtKB.
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 Reference proteome; Vitamin C.
FT CHAIN 1..355
FT /note="Anthocyanin synthase"
FT /id="PRO_0000448077"
FT DOMAIN 211..310
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 218..220
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 291
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 301..303
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 301
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96323"
FT CONFLICT 42
FT /note="E -> G (in Ref. 1; AGV53047)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="S -> P (in Ref. 1; AGV53047)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="L -> P (in Ref. 1; AGV53047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 355 AA; 39959 MW; 3153D1F58830B37B CRC64;
MVATVVGTRV ESLASSGIEA IPKEYVRPQE ELTSIGNIFE EEKKENGPQV PTIDLEDLVS
EDEEKRVRCH EELKRAATEW GVMQVVNHGI PIELMERVRA AGAEFFNQSV EEKEKYANDH
ASGNIQGYGS KLANNASGQL EWEDYFFHLV YPEDKRDMSI WPKTPSDYIP ATSAYAEHLR
GLATKILSAL SLGLGLEEGR LEKEVGGMEE LLLQMKINYY PKCPQPELAL GVEAHTDVSA
LTFILHNMVP GLQLFYEGKW VTAKCVPDSL VMHIGDTIEI LSNGKYKSIL HRGLVNKEKV
RISWAVFCEP PKEKIILKPL PETVSEAEPP LYPPRTFAQH IHHKLFRKTQ ELGAK
