ANRPN_VITVI
ID ANRPN_VITVI Reviewed; 338 AA.
AC D7U6G6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Anthocyanidin reductase ((2S)-flavan-3-ol-forming) {ECO:0000250|UniProtKB:Q5FB34};
DE Short=VvANR {ECO:0000250|UniProtKB:Q5FB34};
DE EC=1.3.1.112 {ECO:0000250|UniProtKB:Q5FB34};
GN Name=ANR {ECO:0000250|UniProtKB:Q5FB34};
GN ORFNames=VIT_00s0361g00040 {ECO:0000312|EMBL:CBI38335.3};
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|Proteomes:UP000009183};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024;
RX PubMed=17721507; DOI=10.1038/nature06148;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
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.
CC Behaves as a reductase and as a C-3 epimerase. Catalyzes the double
CC reduction of anthocyanidins, producing a mixture of (2S,3S)- and
CC (2S,3R)-flavan-3-ols. The enzyme catalyzes sequential hydride transfers
CC to C-2 and C-4, respectively and epimerization at C-3 is achieved by
CC tautomerization that occurs between the two hydride transfers. Converts
CC cyanidin, pelargonidin and delphinidin into catechin and epicatechin,
CC afzelechin and epiafzelechin, and gallocatechin and epigallocatechin
CC respectively. {ECO:0000250|UniProtKB:Q5FB34}.
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 -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
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; FN597047; CBI38335.3; -; Genomic_DNA.
DR AlphaFoldDB; D7U6G6; -.
DR SMR; D7U6G6; -.
DR STRING; 29760.VIT_00s0361g00040.t01; -.
DR EnsemblPlants; Vitvi10g02185_t001; Vitvi10g02185_P001; Vitvi10g02185.
DR Gramene; Vitvi10g02185_t001; Vitvi10g02185_P001; Vitvi10g02185.
DR eggNOG; KOG1502; Eukaryota.
DR HOGENOM; CLU_007383_9_0_1; -.
DR InParanoid; D7U6G6; -.
DR OMA; VFQLATP; -.
DR UniPathway; UPA00154; -.
DR Proteomes; UP000009183; Unassembled WGS sequence, unordered.
DR ExpressionAtlas; D7U6G6; baseline and differential.
DR GO; GO:0033729; F:anthocyanidin reductase activity; IBA:GO_Central.
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 InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 3: Inferred from homology;
KW Flavonoid biosynthesis; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..338
FT /note="Anthocyanidin reductase ((2S)-flavan-3-ol-forming)"
FT /id="PRO_0000438273"
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; 36725 MW; 6B60E33A57971D3D CRC64;
MATQHPIGKK TACVVGGTGF VASLLVKLLL QKGYAVNTTV RDPDNQKKVS HLLELQELGD
LKIFRADLTD ELSFEAPIAG CDFVFHVATP VHFASEDPEN DMIKPAVQGV VNVMKACTRA
KSVKRVILTS SAAAVTINQL DGTGLVVDEK NWTDIEFLTS AKPPTWGYPA SKTLAEKAAW
KFAEENNIDL ITVIPTLMAG SSLTSDVPSS IGLAMSLITG NEFLINGMKG MQMLSGSVSI
AHVEDVCRAH IFVAEKESAS GRYICCAANT SVPELAKFLS KRYPQYKVPT DFGDFPSKSK
LIISSDKLVK EGFSFKYGIE EIYDESVEYF KAKGLLQN
