ID C4YA87_CLAL4 Unreviewed; 422 AA.
AC C4YA87;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 10-JUN-2026, entry version 70.
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=CLUG_05025 {ECO:0000313|EMBL:EEQ40897.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000313|EMBL:EEQ40897.1, ECO:0000313|Proteomes:UP000007703};
RN [1] {ECO:0000313|EMBL:EEQ40897.1, ECO:0000313|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720 {ECO:0000313|EMBL:EEQ40897.1,
RC ECO:0000313|Proteomes:UP000007703};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH408081; EEQ40897.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YA87; -.
DR FunCoup; C4YA87; 234.
DR STRING; 306902.C4YA87; -.
DR GeneID; 8495584; -.
DR KEGG; clu:CLUG_05025; -.
DR VEuPathDB; FungiDB:CLUG_05025; -.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; C4YA87; -.
DR OMA; WRVNACD; -.
DR OrthoDB; 119637at4891; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000007703; Unassembled WGS sequence.
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: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; IPR006115; 6PGDH_NADP-bd.
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 Pfam; PF03446; NAD_binding_2; 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:UP000007703};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498,
KW ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 2..282
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 422 AA; 46976 MW; A8E15AB09597E5D5 CRC64;
MSVIGIIGLG DMGAMYAERF SAAGWTVVGS DREDKYSETC KRFEKSNVKV LPTGHHVSRV
ADYIIYSVEA ENIGKIVQAY GPSTKVGAVV GGQTSCKQPE IAAFEAYLPQ DVDIVSVHSL
HGPKVDPTGQ PLVLVRHRAS DANFGLVQRV VACLQSKVVE LSAEEHDRIT ADTQAVTHAA
FLSMGSAWRQ SNQYPWETPR WIGGMENAKI NISLRIYANK WHVYAGLAIT NPAAHSQVLQ
YAQSATDLFT LMIQGRRDEL ESRLQTAKKY VFASRPGRLL LDDALLERFS LSKEPPGCAQ
PNSHLSLLAI VDSWHRLGIV PYDHMICSTP LFRIFLGVTE YLFCTPGLLE KCVDVALSDT
AFRHDDLEFT FAARSWADII ARGDYRLYQQ KFEETQRFFA PKFAEANAIG NEMIKTILSR
VE
//
