ID H0GRF6_SACCK Unreviewed; 451 AA.
AC H0GRF6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-MAY-2023, entry version 34.
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=VIN7_5674 {ECO:0000313|EMBL:EHN03610.1};
OS Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN03610.1, ECO:0000313|Proteomes:UP000009009};
RN [1] {ECO:0000313|EMBL:EHN03610.1, ECO:0000313|Proteomes:UP000009009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN7 {ECO:0000313|EMBL:EHN03610.1,
RC ECO:0000313|Proteomes:UP000009009};
RX PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT origins.";
RL FEMS Yeast Res. 12:88-96(2012).
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:EHN03610.1}.
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DR EMBL; AGVY01000134; EHN03610.1; -; Genomic_DNA.
DR AlphaFoldDB; H0GRF6; -.
DR HOGENOM; CLU_031403_1_0_1; -.
DR PhylomeDB; H0GRF6; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000009009; 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; 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 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 Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 14..297
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 451 AA; 50894 MW; 5AC4413A67D46FCB CRC64;
MVSEEKIQQW KATKIIGIIG LGDMGLLYAN RFSDAGWKVI CCDREELYGE LKERHAFAKF
ELVKNGHLVS RKSDYIIYSV EASNINKIVA MYGPSSKVGT IVGGQTSCKL PEIEAFEQHL
PKDCDIITVH SLHGPKVDTE GQPLVIINHR SQYSESFDFV NSVMSCLKSK QVYLTYEEHD
KITADTQAVT HAAFLSMGAA WAKIKIYPWT LGINKWYGGL ENVKVNISLR IYSNKWHVYA
GLAITNPSAH QQILQYATSA TELFSLMIDN KEQELTERLL KAKKFVFGKH TGLLLLDDTI
LEKYSLSKNT VSDDTNSKPL PNSHLSLLAI VDSWYQLGID PYDHMICSTP LFRIFLGVSE
YLFLTPGLLE QTIDAAIHDK SFIKDDLEFV VSAREWSSVV SFANFELYKK QFQSVQKFFE
PMLPEANRIG NEMIKTILSH SKGPSAGEKN I
//
