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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}.
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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
 
 
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