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Database: UniProt
Entry: R8BMT0_PHAM7
LinkDB: R8BMT0_PHAM7
Original site: R8BMT0_PHAM7 
ID   R8BMT0_PHAM7            Unreviewed;       377 AA.
AC   R8BMT0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   10-JUN-2026, entry version 36.
DE   SubName: Full=Putative prephenate dehydrogenase protein {ECO:0000313|EMBL:EOO00649.1};
GN   ORFNames=UCRPA7_3870 {ECO:0000313|EMBL:EOO00649.1};
OS   Phaeoacremonium minimum (strain UCR-PA7) (Esca disease fungus) (Togninia
OS   minima).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Togniniales; Togniniaceae; Phaeoacremonium.
OX   NCBI_TaxID=1286976 {ECO:0000313|EMBL:EOO00649.1, ECO:0000313|Proteomes:UP000014074};
RN   [1] {ECO:0000313|Proteomes:UP000014074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-PA7 {ECO:0000313|Proteomes:UP000014074};
RX   PubMed=23814032; DOI=10.1128/genomea.00390-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of the ascomycete Phaeoacremonium aleophilum strain
RT   UCR-PA7, a causal agent of the esca disease complex in grapevines.";
RL   Genome Announc. 1:E0039013-E0039013(2013).
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DR   EMBL; KB933063; EOO00649.1; -; Genomic_DNA.
DR   RefSeq; XP_007914624.1; XM_007916433.1.
DR   AlphaFoldDB; R8BMT0; -.
DR   GeneID; 19324262; -.
DR   KEGG; tmn:UCRPA7_3870; -.
DR   eggNOG; KOG2380; Eukaryota.
DR   HOGENOM; CLU_031403_0_0_1; -.
DR   OrthoDB; 5399569at2759; -.
DR   Proteomes; UP000014074; 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:InterPro.
DR   GO; GO:0006571; P:L-tyrosine biosynthetic process; IEA:EnsemblFungi.
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; IPR046825; PDH_C.
DR   InterPro; IPR050812; Preph/Arog_dehydrog.
DR   InterPro; IPR003099; Prephen_DH.
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   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014074}.
FT   DOMAIN          1..231
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   377 AA;  42614 MW;  211E035AA2C3B185 CRC64;
     MVSPSSKAPK GMENFVIGLI GMGDMGKMAL LRLLRLALSG GQTSCKAPEI AAFEEYLPPD
     VDIVPCHSLH GPNVDTRGQP LVLIKHRASD ESFAKVETVL SCLNSKHVYL SAQEHDRITA
     DTQAVTHAAF LSMGKAWHEM KQFPWEGARY VGGIENVKIN LMLRIYSQNW HVYAGLAILN
     PEARKQIAQY AKSTTELYKL MLEGRQDELR ERVYAAKKKV FGAEDSPKWE ERPLLKDEIL
     DRFSLGKTPD SPPLPNNHLA LLAMVDCWSA MGIVPYDHMI CSTPLFRLWL GVTEYLFRHN
     DKLDDAIRIA IEDHTFRSDD LEFTFAARGW AECVSLGHFE TWMERFKVTQ KFFEPRFKGA
     VEVGNAMIKA VLESTKD
//
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