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Database: UniProt
Entry: Q65CJ7
LinkDB: Q65CJ7
Original site: Q65CJ7 
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   16-JAN-2019, entry version 72.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae;
OC   Ocimeae; 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
RT   hydroxyphenylpyruvate reductase involved in rosmarinic acid
RT   biosynthesis in cell cultures of 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
RT   reductase 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
CC       caffeic acid and 3,4-dihydroxyphenyllactic acid. NADP is the
CC       preferred substrate. {ECO:0000269|PubMed:15284489}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD(+) =
CC         3-(4-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(+) =
CC         3-(4-hydroxyphenyl)pyruvate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10776, ChEBI:CHEBI:10980, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.237; 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}.
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   ProteinModelPortal; Q65CJ7; -.
DR   SMR; Q65CJ7; -.
DR   PRIDE; Q65CJ7; -.
DR   BioCyc; MetaCyc:MONOMER-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   GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
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;
KW   Nucleotide-binding; Oxidoreductase; Pyruvate.
FT   CHAIN         1    313       Hydroxyphenylpyruvate reductase.
FT                                /FTId=PRO_0000422581.
FT   NP_BIND     152    155       NADP. {ECO:0000269|PubMed:20445235}.
FT   NP_BIND     174    176       NADP. {ECO:0000269|PubMed:20445235}.
FT   ACT_SITE    232    232       {ECO:0000250}.
FT   ACT_SITE    261    261       {ECO:0000250}.
FT   ACT_SITE    279    279       Proton donor. {ECO:0000250}.
FT   BINDING     230    230       NADP; via carbonyl oxygen.
FT                                {ECO:0000269|PubMed:20445235}.
FT   BINDING     256    256       NADP. {ECO:0000269|PubMed:20445235}.
FT   STRAND        5      8       {ECO:0000244|PDB:3BA1}.
FT   HELIX        14     23       {ECO:0000244|PDB:3BA1}.
FT   STRAND       24     28       {ECO:0000244|PDB:3BA1}.
FT   HELIX        29     31       {ECO:0000244|PDB:3BA1}.
FT   HELIX        35     42       {ECO:0000244|PDB:3BA1}.
FT   TURN         43     45       {ECO:0000244|PDB:3BA1}.
FT   STRAND       46     51       {ECO:0000244|PDB:3BA1}.
FT   STRAND       53     55       {ECO:0000244|PDB:3BA1}.
FT   HELIX        59     64       {ECO:0000244|PDB:3BA1}.
FT   STRAND       70     76       {ECO:0000244|PDB:3BA1}.
FT   HELIX        83     89       {ECO:0000244|PDB:3BA1}.
FT   STRAND       92     94       {ECO:0000244|PDB:3BA1}.
FT   HELIX       101    116       {ECO:0000244|PDB:3BA1}.
FT   HELIX       119    127       {ECO:0000244|PDB:3BA1}.
FT   HELIX       130    133       {ECO:0000244|PDB:3BA1}.
FT   STRAND      147    150       {ECO:0000244|PDB:3BA1}.
FT   HELIX       154    164       {ECO:0000244|PDB:3BA1}.
FT   TURN        165    167       {ECO:0000244|PDB:3BA1}.
FT   STRAND      170    173       {ECO:0000244|PDB:3BA1}.
FT   STRAND      183    187       {ECO:0000244|PDB:3BA1}.
FT   HELIX       189    194       {ECO:0000244|PDB:3BA1}.
FT   STRAND      197    201       {ECO:0000244|PDB:3BA1}.
FT   HELIX       207    209       {ECO:0000244|PDB:3BA1}.
FT   HELIX       215    221       {ECO:0000244|PDB:3BA1}.
FT   STRAND      226    229       {ECO:0000244|PDB:3BA1}.
FT   HELIX       233    235       {ECO:0000244|PDB:3BA1}.
FT   HELIX       238    246       {ECO:0000244|PDB:3BA1}.
FT   STRAND      252    256       {ECO:0000244|PDB:3BA1}.
FT   TURN        259    262       {ECO:0000244|PDB:3BA1}.
FT   HELIX       266    270       {ECO:0000244|PDB:3BA1}.
FT   STRAND      274    276       {ECO:0000244|PDB:3BA1}.
FT   HELIX       285    303       {ECO:0000244|PDB:3BA1}.
FT   STRAND      309    311       {ECO:0000244|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
//
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