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Database: UniProt
Entry: A0A1V6PYI9_9EURO
LinkDB: A0A1V6PYI9_9EURO
Original site: A0A1V6PYI9_9EURO 
ID   A0A1V6PYI9_9EURO        Unreviewed;       428 AA.
AC   A0A1V6PYI9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   03-MAY-2023, entry version 17.
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=PENANT_c025G10618 {ECO:0000313|EMBL:OQD81827.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD81827.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prephenate = 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|PIRNR:PIRNR036510};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR036510}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {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:OQD81827.1}.
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DR   EMBL; MDYN01000025; OQD81827.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6PYI9; -.
DR   STRING; 416450.A0A1V6PYI9; -.
DR   OrthoDB; 1348131at2759; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniRule.
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; 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; PF03807; F420_oxidored; 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|PIRNR:PIRNR036510};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036510};
KW   NADP {ECO:0000256|PIRNR:PIRNR036510};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672};
KW   Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          8..283
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   428 AA;  47826 MW;  5D871C664AB817C3 CRC64;
     MGRTKEDATI GIIGMGDMGK MYANRLSAAG WRPENYESLK QEFASQQGVT IFPNGHLVSR
     ISDFIVYSVE AGVIDKVVAQ YGPSTKLGAI VGGQTSCKAP ELAAFDKHLP ADVEIVSCHS
     LHGPKVNTQG QPLVLIQHRA SDESLKFVEE ILSSFGSKHV YLTGEMHDRI TADTQAVTHA
     AFLSMGTAWQ ANNQFPWEHG RWVGGIENVK INITLRIYSN KWHVYAGLAI LNPAAKQQIR
     QYAESVTELY KLMIGGHREE LKRRVKAAGA SVFKAGTEGQ DLLLKDEVLD QFSLSNRPRE
     KSPPNSHLSL LAIVDCWSKL GIVPYDHMIC STPLFRLWLG VTEYLFRNDD LLNEALDTAI
     DDTTFRSDDL EFTFAARAWS DCVSFGDFES YRHRFERIAE YFAPRFPEAA TLGNQMMKTI
     LEKTTSNK
//
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