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Database: UniProt
Entry: A0A093ZHE6_9PEZI
LinkDB: A0A093ZHE6_9PEZI
Original site: A0A093ZHE6_9PEZI 
ID   A0A093ZHE6_9PEZI        Unreviewed;       440 AA.
AC   A0A093ZHE6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-FEB-2023, entry version 23.
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=V492_01257 {ECO:0000313|EMBL:KFY16539.1};
OS   Pseudogymnoascus sp. VKM F-4246.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY16539.1, ECO:0000313|Proteomes:UP000029299};
RN   [1] {ECO:0000313|EMBL:KFY16539.1, ECO:0000313|Proteomes:UP000029299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY16539.1,
RC   ECO:0000313|Proteomes:UP000029299};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prephenate = 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFY16539.1}.
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DR   EMBL; JPJU01000314; KFY16539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093ZHE6; -.
DR   STRING; 1420902.A0A093ZHE6; -.
DR   HOGENOM; CLU_031403_1_0_1; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000029299; Unassembled WGS sequence.
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:tyrosine biosynthetic process; IEA:UniProtKB-UniRule.
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; 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; 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|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:UP000029299};
KW   Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          17..298
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   440 AA;  49631 MW;  1D2F98AB204D7FD7 CRC64;
     MRLNNSESDN SDAMENFVIG IIGMGDMGKM YTRQLSDAGW RVNACDREEK YLDLVDEFSS
     RKQVEILPNG HLVSRASDYI IYNVEAASID KVVALYGPST KQGAVVGGQT SCKAPEIAAF
     EAHLPKDVDI VSCHSLHGPN VDPKGQPLVL IKHRASQANF DRVEKVLSCL GSQHVYLSAT
     EHDRITADTQ AVTHAAFLSM GKAWHANEQF PWEIARYVGG IENVKINLTL RIYSQKWHVY
     AGLAILNPYA KEQIRQYAQS VTDLFKLMLG GNREEFERRI KAAGAAVFDA QKSHHGILLE
     DEVLDRFSLG KKPDAPTPNN HLSLLAMVDC WSRMGIVPYD HMICSTPLFR LWLGVTEYLF
     RKPALLDDVI RIAIEDNTFR SDDLEFTFAA RGWSDCVTFG DFESYKDRFE STRKFFEPRF
     ADATKVGNEM MKTILMNTMR
//
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