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Database: UniProt
Entry: A0A0D2EQQ0_9EURO
LinkDB: A0A0D2EQQ0_9EURO
Original site: A0A0D2EQQ0_9EURO 
ID   A0A0D2EQQ0_9EURO        Unreviewed;       427 AA.
AC   A0A0D2EQQ0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-FEB-2023, entry version 23.
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=PV05_05664 {ECO:0000313|EMBL:KIW57060.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW57060.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW57060.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW57060.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KN847319; KIW57060.1; -; Genomic_DNA.
DR   RefSeq; XP_013317644.1; XM_013462190.1.
DR   AlphaFoldDB; A0A0D2EQQ0; -.
DR   STRING; 348802.A0A0D2EQQ0; -.
DR   GeneID; 25327572; -.
DR   HOGENOM; CLU_031403_1_0_1; -.
DR   OrthoDB; 1348131at2759; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000054342; 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; IPR046825; PDH_C.
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   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|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:UP000054342};
KW   Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          4..285
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   427 AA;  48078 MW;  1FB62D509330DFE6 CRC64;
     MEDAAVGIIG MGDMGRMYAR RFSQAGWRVN ACDRPDKFQT LRTEFENEKR INILPNGHLV
     SRASDWIIYS VEAEVIAKVV AEYGPSTKVG AIVGGQTSCK APELAAFEKY LPEDVEIVSC
     HSLHGPAVDP TGQPLVVIQH RASQKSVDLC VRILSCLNSK MVFLSGEKHD RITADTQAVT
     HAAFLSMGTA WAANQQFPWE IDRYVGGIEN VKINITLRIY ANKWHVYAGL AILNPAAKEQ
     IRQYAQSVTE LYKLMLGGHR EELAQRIKTA GAAVFSTDTV HHNLLLGDEV LDKFSLSKRP
     NERTPNNHLS LLGIVDCWWK LGIVPYDHMI CSTPLFRIWL GVTEYLFRNE TLLDEVIKTA
     VGDNTFRSDD LEFTFAARAW SECVSFGAFD AYRARFENIQ QYFAPRFPEA VRLGNEMIKE
     IMTRTKQ
//
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