HPPR_PLESU
ID HPPR_PLESU Reviewed; 313 AA.
AC Q65CJ7;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Hydroxyphenylpyruvate reductase;
DE Short=HPPR;
DE EC=1.1.1.237 {ECO:0000269|PubMed:15284489};
GN Name=HPPR;
OS Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae;
OC Plectranthinae; Plectranthus.
OX NCBI_TaxID=4142;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 37-65 AND 147-162,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15284489; DOI=10.1023/b:plan.0000036367.03056.b2;
RA Kim K.H., Janiak V., Petersen M.;
RT "Purification, cloning and functional expression of hydroxyphenylpyruvate
RT reductase involved in rosmarinic acid biosynthesis in cell cultures of
RT Coleus blumei.";
RL Plant Mol. Biol. 54:311-323(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NADP.
RX PubMed=20445235; DOI=10.1107/s0907444910006360;
RA Janiak V., Petersen M., Zentgraf M., Klebe G., Heine A.;
RT "Structure and substrate docking of a hydroxy(phenyl)pyruvate reductase
RT from the higher plant Coleus blumei Benth.";
RL Acta Crystallogr. D 66:593-603(2010).
CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of 4-
CC hydroxyphenylpyruvate to 4-hydroxyphenyllactate and 3,4-
CC dihydroxyphenylpyruvate to 3,4-dihydroxyphenyllactate in the
CC biosynthesis of rosmarinic acid. Rosmarinic acid is an ester of caffeic
CC acid and 3,4-dihydroxyphenyllactic acid. NADP is the preferred
CC substrate. {ECO:0000269|PubMed:15284489}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) = 3-(4-
CC hydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:10780,
CC ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.237;
CC Evidence={ECO:0000269|PubMed:15284489};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NADP(+) = 3-(4-
CC hydroxyphenyl)pyruvate + H(+) + NADPH; Xref=Rhea:RHEA:10776,
CC ChEBI:CHEBI:10980, ChEBI:CHEBI:15378, ChEBI:CHEBI:36242,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.237;
CC Evidence={ECO:0000269|PubMed:15284489};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-(3,4-dihydroxyphenyl)lactate + NADP(+) = 3-(3,4-
CC dihydroxyphenyl)pyruvate + H(+) + NADPH; Xref=Rhea:RHEA:57704,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29055, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:71492; EC=1.1.1.237;
CC Evidence={ECO:0000269|PubMed:15284489};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-(3,4-dihydroxyphenyl)lactate + NAD(+) = 3-(3,4-
CC dihydroxyphenyl)pyruvate + H(+) + NADH; Xref=Rhea:RHEA:57408,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29055, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:71492; EC=1.1.1.237;
CC Evidence={ECO:0000269|PubMed:15284489};
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AJ507733; CAD47810.2; -; mRNA.
DR PDB; 3BA1; X-ray; 1.47 A; A=1-313.
DR PDB; 3BAZ; X-ray; 2.20 A; A=1-313.
DR PDBsum; 3BA1; -.
DR PDBsum; 3BAZ; -.
DR AlphaFoldDB; Q65CJ7; -.
DR SMR; Q65CJ7; -.
DR KEGG; ag:CAD47810; -.
DR BioCyc; MetaCyc:MON-11763; -.
DR BRENDA; 1.1.1.237; 1561.
DR EvolutionaryTrace; Q65CJ7; -.
DR GO; GO:0047995; F:hydroxyphenylpyruvate reductase activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0102742; F:R(+)-3,4-dihydroxyphenyllactate:NADP+ oxidoreductase activity; IEA:UniProtKB-EC.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Pyruvate.
FT CHAIN 1..313
FT /note="Hydroxyphenylpyruvate reductase"
FT /id="PRO_0000422581"
FT ACT_SITE 232
FT /evidence="ECO:0000250"
FT ACT_SITE 261
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 152..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20445235"
FT BINDING 174..176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20445235"
FT BINDING 230
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20445235"
FT BINDING 256
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:20445235"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 35..42
FT /evidence="ECO:0007829|PDB:3BA1"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:3BA1"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:3BA1"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:3BA1"
FT HELIX 285..303
FT /evidence="ECO:0007829|PDB:3BA1"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:3BA1"
SQ SEQUENCE 313 AA; 34128 MW; 191F25E7E3226586 CRC64;
MEAIGVLMMC PMSTYLEQEL DKRFKLFRYW TQPAQRDFLA LQAESIRAVV GNSNAGADAE
LIDALPKLEI VSSFSVGLDK VDLIKCEEKG VRVTNTPDVL TDDVADLAIG LILAVLRRIC
ECDKYVRRGA WKFGDFKLTT KFSGKRVGII GLGRIGLAVA ERAEAFDCPI SYFSRSKKPN
TNYTYYGSVV ELASNSDILV VACPLTPETT HIINREVIDA LGPKGVLINI GRGPHVDEPE
LVSALVEGRL GGAGLDVFER EPEVPEKLFG LENVVLLPHV GSGTVETRKV MADLVVGNLE
AHFSGKPLLT PVV
