ANRCH_VITVI
ID ANRCH_VITVI Reviewed; 338 AA.
AC Q7PCC4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Anthocyanidin reductase ((2S)-flavan-3-ol-forming) {ECO:0000303|PubMed:16806954};
DE Short=VvANR {ECO:0000303|PubMed:16806954};
DE EC=1.3.1.112 {ECO:0000250|UniProtKB:Q5FB34};
DE AltName: Full=Protein BANYULS {ECO:0000303|PubMed:12788945};
DE Short=VvBAN {ECO:0000303|PubMed:12788945};
GN Name=ANR {ECO:0000303|PubMed:16806954};
GN Synonyms=BAN {ECO:0000303|PubMed:12788945};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000312|EMBL:CAD91911.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Chardonnay; TISSUE=Leaf;
RX PubMed=12788945; DOI=10.1074/jbc.m302783200;
RA Tanner G.J., Francki K.T., Abrahams S., Watson J.M., Larkin P.J.,
RA Ashton A.R.;
RT "Proanthocyanidin biosynthesis in plants. Purification of legume
RT leucoanthocyanidin reductase and molecular cloning of its cDNA.";
RL J. Biol. Chem. 278:31647-31656(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Regent, and cv. Spaetburgunder;
RX PubMed=16806954; DOI=10.1016/j.plaphy.2006.06.001;
RA Pfeiffer J., Kuhnel C., Brandt J., Duy D., Punyasiri P.A., Forkmann G.,
RA Fischer T.C.;
RT "Biosynthesis of flavan 3-ols by leucoanthocyanidin 4-reductases and
RT anthocyanidin reductases in leaves of grape (Vitis vinifera L.), apple
RT (Malus x domestica Borkh.) and other crops.";
RL Plant Physiol. Biochem. 44:323-334(2006).
CC -!- FUNCTION: Produces the terminal flavan-3-ol monomers required for the
CC formation of proanthocyanidins or condensed tannins in leaves and
CC flowers, as well as in the skin and seeds of developing berries (By
CC similarity). Behaves as a reductase and as a C-3 epimerase (By
CC similarity). Catalyzes the double reduction of anthocyanidins,
CC producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols (By
CC similarity). The enzyme catalyzes sequential hydride transfers to C-2
CC and C-4, respectively and epimerization at C-3 is achieved by
CC tautomerization that occurs between the two hydride transfers (By
CC similarity). Converts cyanidin, pelargonidin and delphinidin into
CC catechin and epicatechin, afzelechin and epiafzelechin, and
CC gallocatechin and epigallocatechin respectively (PubMed:16806954).
CC {ECO:0000250|UniProtKB:Q5FB34, ECO:0000269|PubMed:16806954}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S,3R)-flavan-3-ol + 2 NADP(+) = an anthocyanidin with a 3-
CC hydroxy group + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:51416,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:134087, ChEBI:CHEBI:134088; EC=1.3.1.112;
CC Evidence={ECO:0000250|UniProtKB:Q5FB34};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (2S,3S)-flavan-3-ol + 2 NADP(+) = an anthocyanidin with a 3-
CC hydroxy group + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:51420,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:134087, ChEBI:CHEBI:134089; EC=1.3.1.112;
CC Evidence={ECO:0000250|UniProtKB:Q5FB34};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. {ECO:0000269|PubMed:16806954};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:16806954};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and grape berries.
CC {ECO:0000269|PubMed:16806954}.
CC -!- MISCELLANEOUS: Hyperbolic binding of NADPH and NADP(+) to the free
CC enzyme, with a single binding site each. The most likely enzymatic
CC mechanism is sequential ordered Bi-Uni-Uni-Bi, with NADPH binding first
CC and NADP(+) released last. {ECO:0000250|UniProtKB:Q5FB34}.
CC -!- MISCELLANEOUS: This enzyme is strictly pro-S stereospecific and the
CC reaction mechanism involves two hydride transfers from two distinct
CC NADPH molecules. {ECO:0000250|UniProtKB:Q5FB34}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; DQ129684; AAZ82409.1; -; mRNA.
DR EMBL; BN000166; CAD91911.1; -; mRNA.
DR RefSeq; NP_001267885.1; NM_001280956.1.
DR AlphaFoldDB; Q7PCC4; -.
DR SMR; Q7PCC4; -.
DR GeneID; 100232981; -.
DR KEGG; vvi:100232981; -.
DR OrthoDB; 992332at2759; -.
DR BioCyc; MetaCyc:MON-19875; -.
DR BRENDA; 1.3.1.112; 6671.
DR UniPathway; UPA00154; -.
DR ExpressionAtlas; Q7PCC4; baseline and differential.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; NADP; Oxidoreductase.
FT CHAIN 1..338
FT /note="Anthocyanidin reductase ((2S)-flavan-3-ol-forming)"
FT /id="PRO_0000438272"
FT BINDING 18..21
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P93799"
FT BINDING 48
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT BINDING 87..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P93799"
FT BINDING 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
SQ SEQUENCE 338 AA; 36735 MW; 72507DFF0E31775F CRC64;
MATQHPIGKK TACVVGGTGF VASLLVKLLL QKGYAVNTTV RDPDNQKKVS HLLELQELGD
LKIFRADLTD ELSFEAPIAG CDFVFHVATP VHFASEDPEN DMIKPAIQGV VNVMKACTRA
KSVKRVILTS SAAAVTINQL DGTGLVVDEK NWTDIEFLTS AKPPTWGYPA SKTLAEKAAW
KFAEENNIDL ITVIPTLMAG SSLTSDVPSS IGLAMSLITG NEFLINGMKG MQMLSGSVSI
AHVEDVCQAH IFVAEKESAS GRYICCAANT SVPELAKFLS KRYPQYKVPT DFGDFPPKSK
LIISSEKLVK EGFSFKYGIE EIYDESVEYF KAKGLLQN
