ID H2AXZ6_KAZAF Unreviewed; 444 AA.
AC H2AXZ6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 10-JUN-2026, entry version 51.
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 Name=KAFR0G02120 {ECO:0000313|EMBL:CCF59246.1};
GN ORFNames=KAFR_0G02120 {ECO:0000313|EMBL:CCF59246.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF59246.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF59246.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., Oheigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(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; HE650827; CCF59246.1; -; Genomic_DNA.
DR AlphaFoldDB; H2AXZ6; -.
DR FunCoup; H2AXZ6; 273.
DR STRING; 1071382.H2AXZ6; -.
DR KEGG; kaf:KAFR_0G02120; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; H2AXZ6; -.
DR OrthoDB; 5399569at2759; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000005220; 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: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; 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|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:UP000005220};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 17..301
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 444 AA; 50585 MW; 2ECB3E1384F6F7FA CRC64;
MSSVASKAEI DEWKRTKTIG IIGLGDMGLL YATNFSENGW NVVACDREEI YEDVKAKYSN
SRFKVLPNGH YVSRISDYVI YSVETSNIAK IASLYGPSTK LGSIVGGQTS CKNDEIKAFE
KYLPEDIEII TIHSLHGPKI STEGQPLVLI NHKSTKPDSF RFVESLVSCL KSKHVYLTYQ
EHDRITADTQ AVTHAAFLSM GAAWAELKVY PWKLDDNKWY GGIENVKVNI SLRIYSNKWH
VYAGLAITNP HAHQQILQYA TSATELFTLF LDKDKKPELT ERIKKAKEFV FGHHKGLLLL
DDSILEKFSL SNGMTNTSKT TVPNSHLSLL SIVDSWYKLK INPYDHMICS TPLFRIFLGV
TEYLFLNDDL LNQTIDAVYD NKSFRRDDLE FIVAARKWSS IVSFQSFDLY KKQFETTQEF
FQPMFSEANK IGNEMVKTIL SHSK
//
