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Database: UniProt
Entry: C5FBY0_ARTOC
LinkDB: C5FBY0_ARTOC
Original site: C5FBY0_ARTOC 
ID   C5FBY0_ARTOC            Unreviewed;       434 AA.
AC   C5FBY0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   10-JUN-2026, entry version 60.
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=MCYG_00202 {ECO:0000313|EMBL:EEQ27314.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ27314.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
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; DS995701; EEQ27314.1; -; Genomic_DNA.
DR   RefSeq; XP_002850098.1; XM_002850052.1.
DR   AlphaFoldDB; C5FBY0; -.
DR   STRING; 554155.C5FBY0; -.
DR   GeneID; 9230229; -.
DR   VEuPathDB; FungiDB:MCYG_00202; -.
DR   eggNOG; KOG2380; Eukaryota.
DR   HOGENOM; CLU_031403_1_0_1; -.
DR   OMA; WRVNACD; -.
DR   OrthoDB; 5399569at2759; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000002035; 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:UP000002035};
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;  49320 MW;  435F7CA5C2FFF053 CRC64;
     MATPSQENRS IGIIGMGDMG KMYAQRLSEA GWRINACDKP TSYDKLREEF ANDTSINILP
     NGHLVSRISD YIIYSVEAKL IASVVEEYGP STKLGAIVGG QTSCKAPELE AFEKYLPNDV
     EIISCHSLHG PNVNPRGQPL VLIQHRASDE SLKFIECIFK SFQSKYVYLS GEMHDRITAD
     TQAVTHAAFL SMGTAWHANS QFPWEVPRYV GGIENVKINI TLRIYANKWH VYAGLAILNP
     SAKKQIRQYA ESVTELYKLM LGGHREELTK RIKTARKAVF KSSSAKQDLL LQDNVLDRFS
     LSKGRTERMP NNHLSLLAIV DCWWKLGIVP YDHMICSTPL FRLWLGVTEY LFQNEELLDE
     VIDIAIKDNT FRSDDLEFTF AARAWSECVS FGDFESYRDR FEKIQSYFAP RFPEAVRVGN
     EMMKTILEKT SKPS
//
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