ANS1_ORYSJ
ID ANS1_ORYSJ Reviewed; 375 AA.
AC Q93VC3;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
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:0000250|UniProtKB:A2WQ39};
DE AltName: Full=Anthocyanidin synthase {ECO:0000305};
DE Short=OsANS {ECO:0000305};
DE AltName: Full=Anthocyanidin synthase 1 {ECO:0000305};
DE Short=OsANS1 {ECO:0000303|PubMed:18726614};
DE AltName: Full=Leucoanthocyanidin hydroxylase 1 {ECO:0000305};
GN Name=ANS1 {ECO:0000303|PubMed:18726614}; Synonyms=ANS {ECO:0000305};
GN OrderedLocusNames=Os01g0372500 {ECO:0000312|EMBL:BAF04979.1},
GN LOC_Os01g27490 {ECO:0000305};
GN ORFNames=B1039D07.24 {ECO:0000312|EMBL:BAB64051.1},
GN B1045D11.2 {ECO:0000312|EMBL:BAB61138.1};
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=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
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 [3]
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 [4]
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).
RN [5]
RP FUNCTION, AND INDUCTION BY LIGHT.
RX PubMed=18726614; DOI=10.1007/s00425-008-0806-1;
RA Shih C.H., Chu H., Tang L.K., Sakamoto W., Maekawa M., Chu I.K., Wang M.,
RA Lo C.;
RT "Functional characterization of key structural genes in rice flavonoid
RT biosynthesis.";
RL Planta 228:1043-1054(2008).
CC -!- FUNCTION: Involved in anthocyanin and protoanthocyanidin biosynthesis
CC by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins.
CC {ECO:0000305|PubMed:18726614}.
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 -!- INDUCTION: Induced by light. {ECO:0000269|PubMed:18726614}.
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; AP003199; BAB61138.1; -; Genomic_DNA.
DR EMBL; AP003198; BAB64051.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04979.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS72185.1; -; Genomic_DNA.
DR RefSeq; XP_015647276.1; XM_015791790.1.
DR AlphaFoldDB; Q93VC3; -.
DR SMR; Q93VC3; -.
DR STRING; 4530.OS01T0372500-00; -.
DR PaxDb; Q93VC3; -.
DR PRIDE; Q93VC3; -.
DR EnsemblPlants; Os01t0372500-00; Os01t0372500-00; Os01g0372500.
DR GeneID; 4325716; -.
DR Gramene; Os01t0372500-00; Os01t0372500-00; Os01g0372500.
DR KEGG; osa:4325716; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_2_1; -.
DR InParanoid; Q93VC3; -.
DR OMA; REDRISM; -.
DR OrthoDB; 830141at2759; -.
DR BRENDA; 1.14.20.4; 4460.
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 1.
DR Proteomes; UP000059680; Chromosome 1.
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 2: Evidence at transcript 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_0000440775"
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"
SQ SEQUENCE 375 AA; 40708 MW; D20CDC23FDA04DDE 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 SVLLQPVPEL LADGADKPLF APRTFKQHVQ RKLFEKLKDQ
QDNNAAAASN GMRTK