ANRCS_VITVI
ID ANRCS_VITVI Reviewed; 338 AA.
AC Q5FB34;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Anthocyanidin reductase ((2S)-flavan-3-ol-forming) {ECO:0000303|Ref.1};
DE Short=VvANR {ECO:0000303|Ref.1};
DE EC=1.3.1.112 {ECO:0000269|PubMed:20030585, ECO:0000269|Ref.1};
GN Name=ANR {ECO:0000303|Ref.1};
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:BAD89742.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=cv. Cabernet Sauvignon;
RA Fujita A., Soma N., Goto-Yamamoto N., Shindo H., Kakuta T., Koizumi T.,
RA Hashizume K.;
RT "Anthocyanidin reductase gene expression and accumulation of flavan-3-ols
RT in grape berry.";
RL Am. J. Enol. Vitic. 56:336-342(2005).
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Shiraz;
RX PubMed=16169968; DOI=10.1104/pp.105.064238;
RA Bogs J., Downey M.O., Harvey J.S., Ashton A.R., Tanner G.J., Robinson S.P.;
RT "Proanthocyanidin synthesis and expression of genes encoding
RT leucoanthocyanidin reductase and anthocyanidin reductase in developing
RT grape berries and grapevine leaves.";
RL Plant Physiol. 139:652-663(2005).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Cabernet Sauvignon;
RX PubMed=19772852; DOI=10.1016/j.abb.2009.09.010;
RA Gargouri M., Gallois B., Chaudiere J.;
RT "Binding-equilibrium and kinetic studies of anthocyanidin reductase from
RT Vitis vinifera.";
RL Arch. Biochem. Biophys. 491:61-68(2009).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Cabernet Sauvignon;
RX PubMed=20030585; DOI=10.1515/bc.2010.015;
RA Gargouri M., Chaudiere J., Manigand C., Mauge C., Bathany K.,
RA Schmitter J.M., Gallois B.;
RT "The epimerase activity of anthocyanidin reductase from Vitis vinifera and
RT its regiospecific hydride transfers.";
RL Biol. Chem. 391:219-227(2010).
RN [5] {ECO:0007744|PDB:2RH8, ECO:0007744|PDB:3HFS}
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS), FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=cv. Cabernet Sauvignon;
RX PubMed=19690377; DOI=10.1107/s0907444909025013;
RA Gargouri M., Manigand C., Mauge C., Granier T., Langlois d'Estaintot B.,
RA Cala O., Pianet I., Bathany K., Chaudiere J., Gallois B.;
RT "Structure and epimerase activity of anthocyanidin reductase from Vitis
RT vinifera.";
RL Acta Crystallogr. D 65:989-1000(2009).
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 (Ref.1,
CC PubMed:16169968). Behaves as a reductase and as a C-3 epimerase
CC (PubMed:20030585). Catalyzes the double reduction of anthocyanidins,
CC producing a mixture of (2S,3S)- and (2S,3R)-flavan-3-ols (Ref.1). The
CC enzyme catalyzes sequential hydride transfers to C-2 and C-4,
CC respectively and epimerization at C-3 is achieved by tautomerization
CC that occurs between the two hydride transfers (PubMed:20030585).
CC Converts cyanidin, pelargonidin and delphinidin into catechin and
CC epicatechin, afzelechin and epiafzelechin, and gallocatechin and
CC epigallocatechin respectively (PubMed:19690377).
CC {ECO:0000269|PubMed:16169968, ECO:0000269|PubMed:19690377,
CC ECO:0000269|PubMed:20030585, ECO:0000269|Ref.1}.
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:0000269|PubMed:20030585, ECO:0000269|Ref.1};
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:0000269|PubMed:20030585, ECO:0000269|Ref.1};
CC -!- ACTIVITY REGULATION: Inhibited at NaCl concentrations higher than 200
CC mM. {ECO:0000269|PubMed:19690377}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.82 uM for cyanidin (at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:19772852};
CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds, grape skins, flowers and
CC leaves. {ECO:0000269|PubMed:16169968}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the early stage of berry development
CC and then decreases toward the ripening stage (Ref.1, PubMed:16169968).
CC Up-regulated after flowering (PubMed:16169968). {ECO:0000269|Ref.1}.
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:0000305|PubMed:19772852}.
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:0000269|PubMed:19690377}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AB199315; BAD89742.1; -; Genomic_DNA.
DR PDB; 2RH8; X-ray; 2.22 A; A=1-338.
DR PDB; 3HFS; X-ray; 3.17 A; A/B=1-338.
DR PDBsum; 2RH8; -.
DR PDBsum; 3HFS; -.
DR AlphaFoldDB; Q5FB34; -.
DR SMR; Q5FB34; -.
DR BRENDA; 1.3.1.112; 6671.
DR SABIO-RK; Q5FB34; -.
DR UniPathway; UPA00154; -.
DR EvolutionaryTrace; Q5FB34; -.
DR ExpressionAtlas; Q5FB34; baseline and differential.
DR GO; GO:0033729; F:anthocyanidin reductase activity; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0016854; F:racemase and epimerase activity; IDA:UniProtKB.
DR GO; GO:0009813; P:flavonoid biosynthetic process; IDA:UniProtKB.
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 3D-structure; Flavonoid biosynthesis; NADP; Oxidoreductase.
FT CHAIN 1..338
FT /note="Anthocyanidin reductase ((2S)-flavan-3-ol-forming)"
FT /id="PRO_0000438271"
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"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:2RH8"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2RH8"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:2RH8"
FT TURN 149..153
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:2RH8"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 306..311
FT /evidence="ECO:0007829|PDB:2RH8"
FT HELIX 319..332
FT /evidence="ECO:0007829|PDB:2RH8"
SQ SEQUENCE 338 AA; 36763 MW; 5D807ECC0D01445C 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
AHVEDVCRAH IFVAEKESAS GRYICCAANT SVPELAKFLS KRYPQYKVPT DFGDFPPKSK
LIISSEKLVK EGFSFKYGIE EIYDESVEYF KAKGLLQN
