ANS1_ORYSI
ID ANS1_ORYSI Reviewed; 375 AA.
AC A2WQ39; P93403;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Leucoanthocyanidin dioxygenase 1 {ECO:0000305};
DE Short=LDOX1 {ECO:0000305};
DE Short=Leucocyanidin oxygenase 1 {ECO:0000305};
DE EC=1.14.20.4 {ECO:0000269|PubMed:17157544};
DE AltName: Full=Anthocyanidin synthase {ECO:0000303|PubMed:17157544};
DE Short=OsANS {ECO:0000303|PubMed:17157544};
DE AltName: Full=Anthocyanidin synthase 1 {ECO:0000305};
DE Short=OsANS1 {ECO:0000305};
DE AltName: Full=Leucoanthocyanidin hydroxylase 1 {ECO:0000305};
GN Name=ANS1 {ECO:0000305}; Synonyms=ANS {ECO:0000303|PubMed:17157544};
GN ORFNames=OsI_01973 {ECO:0000312|EMBL:EAY74085.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP BIOTECHNOLOGY.
RC STRAIN=cv. Purple Puttu; TISSUE=Shoot;
RX PubMed=17157544; DOI=10.1016/j.ymben.2006.09.003;
RA Reddy A.M., Reddy V.S., Scheffler B.E., Wienanad U., Reddy A.R.;
RT "Novel transgenic rice overexpressing anthocyanidin synthase accumulates a
RT mixture of flavonoids leading to an increased antioxidant potential.";
RL Metab. Eng. 9:95-111(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Involved in anthocyanin and protoanthocyanidin biosynthesis
CC by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins.
CC Is able to synthesize anthocyanin pigments from leucoanthocyanidins in
CC aleurone tissue. Converts dihydroquercetin to quercetin in vitro.
CC {ECO:0000269|PubMed:17157544}.
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:17157544};
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 -!- BIOTECHNOLOGY: Plants over-expressing ANS1 have increased accumulation
CC of a mixture of flavonoids and anthocyanins, with a concomitant
CC decrease in proanthocyanidins, and could represent an enhanced
CC antioxidant potential. {ECO:0000269|PubMed:17157544}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; Y07955; CAA69252.1; -; mRNA.
DR EMBL; CM000126; EAY74085.1; -; Genomic_DNA.
DR PIR; T03593; T03593.
DR AlphaFoldDB; A2WQ39; -.
DR SMR; A2WQ39; -.
DR STRING; 39946.A2WQ39; -.
DR EnsemblPlants; BGIOSGA001621-TA; BGIOSGA001621-PA; BGIOSGA001621.
DR Gramene; BGIOSGA001621-TA; BGIOSGA001621-PA; BGIOSGA001621.
DR HOGENOM; CLU_010119_16_2_1; -.
DR OMA; REDRISM; -.
DR UniPathway; UPA00009; -.
DR Proteomes; UP000007015; Chromosome 1.
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 1: Evidence at protein level;
KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..375
FT /note="Leucoanthocyanidin dioxygenase 1"
FT /id="PRO_0000440776"
FT DOMAIN 218..317
FT /note="Fe2OG dioxygenase"
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 244
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 298
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 308
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 4
FT /note="V -> A (in Ref. 1; CAA69252)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="V -> A (in Ref. 1; CAA69252)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="I -> M (in Ref. 1; CAA69252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 40637 MW; 37189B03F7A0EDDD CRC64;
MTDVELRVEA LSLSGVSAIP PEYVRPEEER ADLGDALELA RAASDDDATA RIPVVDISAF
DNDGDGRHAC VEAVRAAAEE WGVIHIAGHG LPGDVLGRLR AAGEAFFALP IAEKEAYAND
PAAGRLQGYG SKLAANASGK REWEDYLFHL VHPDHLADHS LWPANPPEYV PVSRDFGGRV
RTLASKLLAI LSLGLGLPEE TLERRLRGHE LAGVDDDLLL QLKINYYPRC PRPDLAVGVE
AHTDVSALSF ILHNGVPGLQ VHHAGSWVTA RPEPGTIVVH VGDALEILTN GRYTSVLHRG
LVSRDAVRLS WVVFCEPPPE SVLLQPVQEL LADGAGKPLF APRTFKQHVQ RKLFKKLKDQ
QDNNAAAASN GMITK
