ID A0A9Q8PCG2_FULFL Unreviewed; 401 AA.
AC A0A9Q8PCG2;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 10-JUN-2026, entry version 11.
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=CLAFUR5_10453 {ECO:0000313|EMBL:UJO19895.1};
OS Fulvia fulva (Tomato leaf mold) (Passalora fulva).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Fulvia.
OX NCBI_TaxID=5499 {ECO:0000313|EMBL:UJO19895.1, ECO:0000313|Proteomes:UP000756132};
RN [1] {ECO:0000313|EMBL:UJO19895.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Race5_Kim {ECO:0000313|EMBL:UJO19895.1};
RA Zaccaron A., Stergiopoulos I.;
RL Submitted (DEC-2021) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:UJO19895.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Race5_Kim {ECO:0000313|EMBL:UJO19895.1};
RX PubMed=35471194;
RA Zaccaron A.Z., Chen L.H., Samaras A., Stergiopoulos I.;
RT "A chromosome-scale genome assembly of the tomato pathogen Cladosporium
RT fulvum reveals a compartmentalized genome architecture and the presence of
RT a dispensable chromosome.";
RL Microb. Genom. 8:e000819-e000819(2022).
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|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; CP090169; UJO19895.1; -; Genomic_DNA.
DR RefSeq; XP_047764261.1; XM_047909601.1.
DR AlphaFoldDB; A0A9Q8PCG2; -.
DR GeneID; 71990331; -.
DR KEGG; ffu:CLAFUR5_10453; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000756132; Chromosome 7.
DR GO; GO:0070403; F:NAD+ binding; IEA:TreeGrafter.
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:000002; Prephenate dehydrogenase [NADP(+)]; 1.
DR FunFam; 1.10.3660.10:FF:000004; 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; 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; 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:UP000756132};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 1..252
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 401 AA; 45551 MW; 7B2C9F82B9F2A6AB CRC64;
MPDKFEALKA EFQSRPNVHI LENGHFVSRS SDWIMYSVPA ANIDSSVAKF GPSTKMGAIV
GGQTSTKAPE IEAFEKHLPR DVEIVSCHSL HGPGVNPKGQ PLVIINHRAS EKSVDLVQRM
LSSFESKFVP LTAEKHDRIT ADTQAVTHLA FLSMGTAWQA NNQFPWETER YVGGIENVKI
NLMMRIYANK WHVYAGLAIL NPAAKKQIRQ YAESVTELYK LMLAGHRKEL RERIHAAKDA
VFGAPKPDDD VLLQDELLDR FSLGDKPAQR VKNNHLSLLA MVDCWWKLGI VPYDHMICST
PLFRLWLGIT EYVYRNETLL EECITTAIED QSFRADDLEF TFATRDWSER VQLGHMDGYR
EKFEKIQAYF APRFAEANKI GNEMIKTIEE SLKATRKNGL A
//
