ID A0A7S9PSB4_EPIFF Unreviewed; 450 AA.
AC A0A7S9PSB4;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 13.
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=C2857_003444 {ECO:0000313|EMBL:QPG93902.1};
OS Epichloe festucae (strain Fl1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Epichloe.
OX NCBI_TaxID=877507 {ECO:0000313|EMBL:QPG93902.1, ECO:0000313|Proteomes:UP000594364};
RN [1] {ECO:0000313|EMBL:QPG93902.1, ECO:0000313|Proteomes:UP000594364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fl1 {ECO:0000313|EMBL:QPG93902.1,
RC ECO:0000313|Proteomes:UP000594364};
RX PubMed=30356280;
RA Winter D.J., Ganley A.R.D., Young C.A., Liachko I., Schardl C.L.,
RA Dupont P.Y., Berry D., Ram A., Scott B., Cox M.P.;
RT "Repeat elements organise 3D genome structure and mediate transcription in
RT the filamentous fungus Epichloe festucae.";
RL PLoS Genet. 14:0-e1007467(2018).
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; CP031385; QPG93902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7S9PSB4; -.
DR OrthoDB; 5399569at2759; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000594364; Chromosome 1.
DR GO; GO:0070403; F:NAD+ binding; IEA:TreeGrafter.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
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: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; IPR006115; 6PGDH_NADP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PF03446; NAD_binding_2; 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:UP000594364};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498,
KW ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 15..296
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 450 AA; 50419 MW; B06B15D40D1FB543 CRC64;
MATTIETVPI GMEGFVVGLI GMGDMGKMYA DRLSAAGWRV LACDREDRFD SLQETYQGKK
NIEICQNGHY VSRASDYIIY SVEAAIIDRV IAQFGPSTKM GAIVGGQTSC KCPEIAAFEK
HLPPDVHVIS CHSLHGPGVD THNQPLVLIQ HRAPDEAMRK VETVLSCFRS KYVYLTAQEH
DRITADTQAV THAAFLSMGK AWHANSQFPW ELNRYVGGIE NVKINTMLRI YGQKWHVYAG
LAILNPEAKN QVAQYAKSVT TLYKLMLEGD LEGLRSRVYA ARDKVFGTAT SWDTRPLIEP
SILSSFSLGK PTDAPPRPNN HLSLLGMVDC WAALNIVPYD HMLCSTPLFR LRLGVTEHLF
RNAALLDETL RTAVEDKTYR SDDLEFTFAA RGWAECVTLG HFETWEKRFV STQDFFQPRF
AEAKKVGDQM MKKVLESSKE DGTALDKDLK
//
