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Database: UniProt
Entry: E5R1N6_ARTGP
LinkDB: E5R1N6_ARTGP
Original site: E5R1N6_ARTGP 
ID   E5R1N6_ARTGP            Unreviewed;       434 AA.
AC   E5R1N6;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   10-JUN-2026, entry version 49.
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=MGYG_00774 {ECO:0000313|EMBL:EFQ97734.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; DS989822; EFQ97734.1; -; Genomic_DNA.
DR   RefSeq; XP_003176686.1; XM_003176638.1.
DR   AlphaFoldDB; E5R1N6; -.
DR   FunCoup; E5R1N6; 223.
DR   STRING; 535722.E5R1N6; -.
DR   GeneID; 10032007; -.
DR   VEuPathDB; FungiDB:MGYG_00774; -.
DR   eggNOG; KOG2380; Eukaryota.
DR   HOGENOM; CLU_031403_1_0_1; -.
DR   InParanoid; E5R1N6; -.
DR   OMA; WRVNACD; -.
DR   OrthoDB; 5399569at2759; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000002669; 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:000002; Prephenate dehydrogenase [NADP(+)]; 1.
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:UP000002669};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498,
KW   ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          9..290
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   434 AA;  49222 MW;  79F48BD050ECBBBC CRC64;
     MALPSREKRS IGIIGMGDMG KMYAQRLSEA GWRINACDKP TSYDKLRAEF ANDTNINILP
     NGHLVSRISD YIVYSVEAKF IASVVEEYGP STKVGAIVGG QTSCKAPELE AFEKYLPSDV
     EIISCHSLHG PNVNPKGQPL VLIQHRASNE SLKFVEDIFK SFQSTYVYLS GEMHDRITAD
     TQAVTHAAFL SMGTAWHANS QFPWEVPRYV GGIENVKINI TLRIYANKWH VYAGLAILNP
     AAKKQIRQYA ESVTELYKLM LGGHREELTK RIKTARAAVF KSKSARQDLL LQDSVLDRFS
     LSKRGTERMP NNHLSLLAIV DCWWKLGIVP YDHMICSTPL FRLWLGVTEY LFQNEELLDE
     VIDTAIEDNT FRSDDLEFTF AARAWSDCVS FGDFESYRDR FEKIQSYFAP RFPEAVRIGN
     EMMKTILEKT SKPS
//
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