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Database: UniProt
Entry: M1W610_CLAP2
LinkDB: M1W610_CLAP2
Original site: M1W610_CLAP2 
ID   M1W610_CLAP2            Unreviewed;       461 AA.
AC   M1W610;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   10-JUN-2026, entry version 36.
DE   RecName: Full=Prephenate dehydrogenase [NADP(+)] {ECO:0000256|PIRNR:PIRNR036510};
DE            Short=PRDH {ECO:0000256|PIRNR:PIRNR036510};
DE            EC=1.3.1.13 {ECO:0000256|PIRNR:PIRNR036510};
GN   ORFNames=CPUR_01027 {ECO:0000313|EMBL:CCE27553.1};
OS   Claviceps purpurea (strain 20.1) (Ergot fungus) (Sphacelia segetum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=1111077 {ECO:0000313|EMBL:CCE27553.1, ECO:0000313|Proteomes:UP000016801};
RN   [1] {ECO:0000313|EMBL:CCE27553.1, ECO:0000313|Proteomes:UP000016801}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20.1 {ECO:0000313|EMBL:CCE27553.1,
RC   ECO:0000313|Proteomes:UP000016801};
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prephenate + NADP(+) = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC         NADPH; Xref=Rhea:RHEA:21640, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00051295,
CC         ECO:0000256|PIRNR:PIRNR036510};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00060605, ECO:0000256|PIRNR:PIRNR036510}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007964, ECO:0000256|PIRNR:PIRNR036510}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCE27553.1}.
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DR   EMBL; CAGA01000004; CCE27553.1; -; Genomic_DNA.
DR   AlphaFoldDB; M1W610; -.
DR   STRING; 1111077.M1W610; -.
DR   VEuPathDB; FungiDB:CPUR_01027; -.
DR   eggNOG; KOG2380; Eukaryota.
DR   HOGENOM; CLU_031403_1_0_1; -.
DR   OrthoDB; 5399569at2759; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000016801; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:TreeGrafter.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:EnsemblFungi.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006571; P:L-tyrosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 1.10.3660.10:FF:000004; Prephenate dehydrogenase [NADP(+)]; 1.
DR   FunFam; 3.40.50.720:FF:000339; Prephenate dehydrogenase [NADP(+)]; 1.
DR   Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR050812; Preph/Arog_dehydrog.
DR   InterPro; IPR003099; Prephen_DH.
DR   InterPro; IPR012385; Prephenate_DH_fun.
DR   PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF27505; 6PGD_Tyr1_C; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF20463; PDH_C; 1.
DR   PIRSF; PIRSF036510; PDH_fung; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036510};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016801};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498,
KW   ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          15..305
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   461 AA;  51732 MW;  967620FD0C3BC316 CRC64;
     MATATKMTPN GMEDFVVGLI GMGDMGRMYA DRLAAAGWRR LIRDVRTRVL ACDREDRFDS
     LKKEYQGKKN IEICQNGHYV SRASDYVIYS VEAAVIDRVI AQFGPSTKMG AIVGGQTSCK
     SPEIAAFEKH LPADIHIISC HSLHGPGVNT LGQPLVLIQH RAPDEALRKV ETVLSCFRSK
     YVYLTAQEHD RITADTQAVT HAAFLSMGKA WHANSQFPWE LNRYVGGIEN VKINTMLRIY
     SQKWHVYAGL AILNPEAKQQ VAQYAKSVTA LYKLMLEGDL EGLRSRIYAA REKVFGGTTT
     SWESRPLIEP SILSSFSLGK PTDAPPRPNN HLSLLAMVDC WAALNIVPYD HMLCSTPLFR
     LRLGVTEHLF RDTTLLDAAL RTAVEDKMYR SDDLEFTFAA RGWAECVGLG HYETWEKRFV
     STQAFFQPRF AEAKIVCDQM MSKVLEGLKD EDAPRSTVNQ D
//
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