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Database: UniProt
Entry: C1GSD7_PARBA
LinkDB: C1GSD7_PARBA
Original site: C1GSD7_PARBA 
ID   C1GSD7_PARBA            Unreviewed;       456 AA.
AC   C1GSD7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 2.
DT   10-JUN-2026, entry version 67.
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=PAAG_01432 {ECO:0000313|EMBL:EEH38970.2};
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Paracoccidioides.
OX   NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH38970.2, ECO:0000313|Proteomes:UP000002059};
RN   [1] {ECO:0000313|EMBL:EEH38970.2, ECO:0000313|Proteomes:UP000002059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H., Longo L.V.,
RA   Ma L.J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN293994; EEH38970.2; -; Genomic_DNA.
DR   RefSeq; XP_015701254.1; XM_015844346.1.
DR   AlphaFoldDB; C1GSD7; -.
DR   STRING; 502779.C1GSD7; -.
DR   GeneID; 9099781; -.
DR   KEGG; pbl:PAAG_01432; -.
DR   VEuPathDB; FungiDB:PAAG_01432; -.
DR   eggNOG; KOG2380; Eukaryota.
DR   HOGENOM; CLU_031403_1_0_1; -.
DR   OMA; WRVNACD; -.
DR   OrthoDB; 5399569at2759; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000002059; Unassembled WGS sequence.
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; 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   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:UP000002059};
KW   Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          10..301
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   456 AA;  51563 MW;  3562C84763D817EB CRC64;
     MTWEFFTIPP FWRVMGFWVV GDFSILITYN PPAPMEPLLT PECRVNACDR PANYESLKRE
     FASNQNINIL PNGHLVSRIS DYIIYSVEAE AIDKIVAEYG PSTKVGAIVG GQTSCKAPEL
     AAFDKYLPND VEIISCHSLH GPNVNPKGQP LVLIKHRASD ESLRFVEDLF ASFQSKYVYL
     SGVMHDRITA DTQAVTHAAF LSMGTAWHAN NQFPWEVARY VGGIENVKIN ITLRIYANKW
     HVYAGLAILN PAAKMQIRQY AQSVTELFKL MLGGHREEFR ARVKAAGAAV FKSGTTQHEL
     LLQDEVLDQF SLSKGMSERM PNNHLSLLAI VDCWWKLGIV PYDHMICSTP LFRLWLGVTE
     YLFRNEDLLN EVLDIAIDDN TFRSDDLEFT FAARAWSECV SFGDFASYRD RFEKIQSYFA
     PRFPEAVRLG NEMMKTILDK TTTTTYATTV NATSSS
//
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