ANS2_ORYSJ
ID ANS2_ORYSJ Reviewed; 373 AA.
AC Q67VR7;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Leucoanthocyanidin dioxygenase 2 {ECO:0000305};
DE Short=LDOX2 {ECO:0000305};
DE Short=Leucocyanidin oxygenase 2 {ECO:0000305};
DE EC=1.14.20.4 {ECO:0000250|UniProtKB:A2WQ39};
DE AltName: Full=Anthocyanidin synthase 2 {ECO:0000305};
DE Short=OsANS2 {ECO:0000305};
DE AltName: Full=Leucoanthocyanidin hydroxylase 2 {ECO:0000305};
GN Name=ANS2 {ECO:0000305};
GN OrderedLocusNames=Os06g0626700 {ECO:0000312|EMBL:BAF20033.1},
GN LOC_Os06g42130 {ECO:0000305};
GN ORFNames=OSJNBa0072A21.33 {ECO:0000312|EMBL:BAD37752.1},
GN P0530H05.4 {ECO:0000312|EMBL:BAD37378.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Involved in anthocyanin and protoanthocyanidin biosynthesis
CC by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins.
CC {ECO:0000250|UniProtKB:Q93VC3}.
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:0000250|UniProtKB:A2WQ39};
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 -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AP003541; BAD37378.1; -; Genomic_DNA.
DR EMBL; AP004737; BAD37752.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF20033.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS98704.1; -; Genomic_DNA.
DR RefSeq; XP_015641525.1; XM_015786039.1.
DR AlphaFoldDB; Q67VR7; -.
DR SMR; Q67VR7; -.
DR STRING; 4530.OS06T0626700-00; -.
DR PaxDb; Q67VR7; -.
DR PRIDE; Q67VR7; -.
DR EnsemblPlants; Os06t0626700-00; Os06t0626700-00; Os06g0626700.
DR GeneID; 4341576; -.
DR Gramene; Os06t0626700-00; Os06t0626700-00; Os06g0626700.
DR KEGG; osa:4341576; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_2_1; -.
DR InParanoid; Q67VR7; -.
DR OMA; PREYIRP; -.
DR OrthoDB; 830141at2759; -.
DR PlantReactome; R-OSA-1119440; Anthocyanin biosynthesis (pelargonidin 3-O-glucoside, cyanidin 3-O-glucoside).
DR PlantReactome; R-OSA-1119514; Anthocyanin biosynthesis (delphinidin 3-O-glucoside).
DR UniPathway; UPA00009; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
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:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..373
FT /note="Leucoanthocyanidin dioxygenase 2"
FT /id="PRO_0000440777"
FT DOMAIN 216..315
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 242
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 296
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 306
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 373 AA; 40712 MW; 05397A7600BEF367 CRC64;
MTDVELRVEA LSLSDVSAIP PEYVRLEEER TDLGDALEVA RAASDDADAA RIPVVDISAF
DGDGRRACVE AVRAAAEEWG VMHIAGHGLP GDVLDRLRAA GEAFFALPIA EKEAYANDPA
AGRLQGYGSK LAANASGKRE WEDYLFHLVH PDHLADHSLW PANPPEYVPV SRDFGGRVRT
LASKLLAILS LGLGLPEETL ERRLRRHDQH GVDDDLLLQL KINYYPRCPR PDLAVGVEAH
TDVSALSFIL HNGVPGLQAH HAGTWVTARS EQGTIVVHVG DALEILTNGR YTSVLHRSLV
SRDAVRVSWV VFCEPPPESV LLQPLPELLA NGAGKPLFAP RTFKQHVQRK LFKKLKDQQD
NNAAAASNGI IPK
