BAN_ARATH
ID BAN_ARATH Reviewed; 340 AA.
AC Q9SEV0; Q1PFH9; Q680A7; Q9SYA8;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Anthocyanidin reductase;
DE Short=AtANR {ECO:0000303|PubMed:14725861};
DE EC=1.3.1.77 {ECO:0000269|PubMed:12532018, ECO:0000269|PubMed:14725861};
DE AltName: Full=Anthocyanin spotted testa;
DE Short=ast;
DE AltName: Full=Protein BANYULS;
GN Name=BAN; Synonyms=ANR; OrderedLocusNames=At1g61720; ORFNames=T13M11.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND CHARACTERIZATION.
RC STRAIN=cv. En-1, and cv. Wassilewskija; TISSUE=Silique;
RX PubMed=10504561; DOI=10.1046/j.1365-313x.1999.00529.x;
RA Devic M., Guilleminot J., Debeaujon I., Bechtold N., Bensaude E.,
RA Koornneef M., Pelletier G., Delseny M.;
RT "The BANYULS gene encodes a DFR-like protein and is a marker of early seed
RT coat development.";
RL Plant J. 19:387-398(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-340.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12532018; DOI=10.1126/science.1078540;
RA Xie D.Y., Sharma S.B., Paiva N.L., Ferreira D., Dixon R.A.;
RT "Role of anthocyanidin reductase, encoded by BANYULS in plant flavonoid
RT biosynthesis.";
RL Science 299:396-399(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=14725861; DOI=10.1016/j.abb.2003.12.011;
RA Xie D.Y., Sharma S.B., Dixon R.A.;
RT "Anthocyanidin reductases from Medicago truncatula and Arabidopsis
RT thaliana.";
RL Arch. Biochem. Biophys. 422:91-102(2004).
RN [8]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Involved in the biosynthesis of condensed tannins. Converts
CC cyanidin into (-)-epicatechin as the major product.
CC {ECO:0000269|PubMed:12532018, ECO:0000269|PubMed:14725861}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2R,3R)-flavan-3-ol + 2 NAD(+) = an anthocyanidin with a 3-
CC hydroxy group + 2 H(+) + 2 NADH; Xref=Rhea:RHEA:11640,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:134086, ChEBI:CHEBI:134087; EC=1.3.1.77;
CC Evidence={ECO:0000269|PubMed:12532018, ECO:0000269|PubMed:14725861};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2R,3R)-flavan-3-ol + 2 NADP(+) = an anthocyanidin with a 3-
CC hydroxy group + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:11644,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:134086, ChEBI:CHEBI:134087; EC=1.3.1.77;
CC Evidence={ECO:0000269|PubMed:12532018, ECO:0000269|PubMed:14725861};
CC -!- ACTIVITY REGULATION: Inhibited by (+)-catechin, quercetin and (+)- and
CC (-)-dihydroquercetin. Not inhibited by salt. Positive cooperativity
CC with NADPH acting as cosubstrate and modulator.
CC {ECO:0000269|PubMed:14725861}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=73.9 uM for cyanidin {ECO:0000269|PubMed:14725861};
CC KM=52.8 uM for pelargonidin {ECO:0000269|PubMed:14725861};
CC KM=17.8 uM for delphinidin {ECO:0000269|PubMed:14725861};
CC Vmax=10.0 nmol/min/mg enzyme with cyanidin as substrate
CC {ECO:0000269|PubMed:14725861};
CC Vmax=0.9 nmol/min/mg enzyme with delphinidin as substrate
CC {ECO:0000269|PubMed:14725861};
CC Note=cannot use NADH as cosubstrate.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:14725861};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:14725861};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC -!- SUBUNIT: Homo- or heterodimer. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Flowers and young siliques. Detected specifically
CC in the endothelium of seed coat. {ECO:0000269|PubMed:10504561}.
CC -!- DEVELOPMENTAL STAGE: From fertilization until pre-globular embryo
CC stage.
CC -!- MISCELLANEOUS: Regulated by TRANSPARENT TESTA 2, TRANSPARENT TESTA 8
CC and TRANSPARENT TESTA GLABRA 1.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AF092912; AAF23859.1; -; mRNA.
DR EMBL; AC005882; AAD21417.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33879.1; -; Genomic_DNA.
DR EMBL; DQ446384; ABE65732.1; -; mRNA.
DR EMBL; AK175960; BAD43723.1; -; mRNA.
DR PIR; H96642; H96642.
DR RefSeq; NP_176365.1; NM_104854.4.
DR AlphaFoldDB; Q9SEV0; -.
DR SMR; Q9SEV0; -.
DR STRING; 3702.AT1G61720.1; -.
DR PaxDb; Q9SEV0; -.
DR PRIDE; Q9SEV0; -.
DR ProteomicsDB; 241210; -.
DR EnsemblPlants; AT1G61720.1; AT1G61720.1; AT1G61720.
DR GeneID; 842469; -.
DR Gramene; AT1G61720.1; AT1G61720.1; AT1G61720.
DR KEGG; ath:AT1G61720; -.
DR Araport; AT1G61720; -.
DR TAIR; locus:2195733; AT1G61720.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR InParanoid; Q9SEV0; -.
DR OMA; VFQLATP; -.
DR OrthoDB; 992332at2759; -.
DR PhylomeDB; Q9SEV0; -.
DR BioCyc; ARA:AT1G61720-MON; -.
DR BRENDA; 1.3.1.77; 399.
DR SABIO-RK; Q9SEV0; -.
DR UniPathway; UPA00154; -.
DR PRO; PR:Q9SEV0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SEV0; baseline and differential.
DR Genevisible; Q9SEV0; AT.
DR GO; GO:0033729; F:anthocyanidin reductase activity; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; ISS:TAIR.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009964; P:negative regulation of flavonoid biosynthetic process; IMP:TAIR.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Flavonoid biosynthesis; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..340
FT /note="Anthocyanidin reductase"
FT /id="PRO_0000215574"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 169
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT VARIANT 340
FT /note="K -> KES (in strain: cv. Wassilewskija)"
FT CONFLICT 55
FT /note="K -> Q (in Ref. 1; AAF23859)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="I -> L (in Ref. 1; AAF23859)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..157
FT /note="VE -> ID (in Ref. 1; AAF23859)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> K (in Ref. 1; AAF23859)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="K -> E (in Ref. 1; AAF23859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 37906 MW; C5C15F7359DB68FB CRC64;
MDQTLTHTGS KKACVIGGTG NLASILIKHL LQSGYKVNTT VRDPENEKKI AHLRKLQELG
DLKIFKADLT DEDSFESSFS GCEYIFHVAT PINFKSEDPE KDMIKPAIQG VINVLKSCLK
SKSVKRVIYT SSAAAVSINN LSGTGIVMNE ENWTDVEFLT EEKPFNWGYP ISKVLAEKTA
WEFAKENKIN LVTVIPALIA GNSLLSDPPS SLSLSMSFIT GKEMHVTGLK EMQKLSGSIS
FVHVDDLARA HLFLAEKETA SGRYICCAYN TSVPEIADFL IQRYPKYNVL SEFEEGLSIP
KLTLSSQKLI NEGFRFEYGI NEMYDQMIEY FESKGLIKAK
