ID B2AW68_PODAN Unreviewed; 445 AA.
AC B2AW68;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 10-JUN-2026, entry version 77.
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};
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849 {ECO:0000313|EMBL:CDP32115.1, ECO:0000313|Proteomes:UP000001197};
RN [1] {ECO:0000313|EMBL:CDP32115.1, ECO:0000313|Proteomes:UP000001197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2] {ECO:0000313|Proteomes:UP000001197}
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC {ECO:0000313|Proteomes:UP000001197};
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; FO904942; CDP32115.1; -; Genomic_DNA.
DR RefSeq; XP_001907969.1; XM_001907934.1.
DR STRING; 515849.B2AW68; -.
DR GeneID; 6192301; -.
DR KEGG; pan:PODANSg5004; -.
DR VEuPathDB; FungiDB:PODANS_7_6130; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR OrthoDB; 5399569at2759; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000001197; Chromosome 7.
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:UP000001197};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498,
KW ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 13..295
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 445 AA; 50063 MW; 7399D944B3FC9466 CRC64;
MATASEFAWS KDFTIGLIGM GDMGRMYARR LANAGWRVMA CDREEKFEEL AKEFADNTNI
QILRNGHLVS RASNYIIYSV EAAAIGRVVE QFGPSTRLGA IVGGQTSCKD PEIKAFESYL
PSDVDIVSCH SLHGPNVDPR GQPLVLIKHR ASDESFQKVE SVLSCLNSTH VYLTAKEHDR
ITADTQAVTH AAFLSMGKAW HANRQFPWEE GSRYIGGIEN VKINLMLRIY AQKWHVYAGL
AILNPEAHKQ IGQFARSSTE LFYLMLEGRS DELRERVYKA KEKVFGAEGS PKWAERPLLK
EELLDRFSLN KPSGEKGGGR GLPNNHLSLL AMVDCWSALG IVPYDHMICS TPLFRLWLGV
AEHLFRTPGL LDECLRVGIE DKSFRRDDLQ FAIAAAGWAE CVSLRQFDTW RERFAVTQKF
FEPRFKGAVE VGQAMIKAVL ESEKE
//
