ID A0A0F7TR95_PENBI Unreviewed; 438 AA.
AC A0A0F7TR95;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 03-MAY-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=PMG11_07855 {ECO:0000313|EMBL:CEJ59224.1};
OS Penicillium brasilianum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=104259 {ECO:0000313|EMBL:CEJ59224.1, ECO:0000313|Proteomes:UP000042958};
RN [1] {ECO:0000313|Proteomes:UP000042958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG11 {ECO:0000313|Proteomes:UP000042958};
RX PubMed=26337871; DOI=10.1128/genomea.00724-15;
RA Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Brakhage A.A.,
RA Valiante V.;
RT "Draft genome sequence of the fungus Penicillium brasilianum MG11.";
RL Genome Announc. 3:0-0(2015).
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}.
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DR EMBL; CDHK01000007; CEJ59224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7TR95; -.
DR STRING; 104259.A0A0F7TR95; -.
DR OrthoDB; 1348131at2759; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000042958; Unassembled WGS sequence.
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; 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 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:UP000042958};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 10..293
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 438 AA; 49707 MW; A064E0D35CF449E3 CRC64;
MIFPLWEFLV PASADLVMRL EEYFLTNIKY YYLFQRINAC DRPENYESLQ QEFASQPLVT
IFPNGHLVSR ISDFILYSVE AGVIDRVVAQ YGPSTKQGAI VGGQTSCKAP ELAAFEKHLP
ADVEIVSCHS LHGPKVNPKG QPLVLIQHRA SDESLQFVDD ILSSFGSKHV YLTGELHDRI
TADTQAVTHA AFLSMGTAWQ ANNQFPWEIS RWVGGIENVK INITLRIYSN KWHVYAGLAI
LNPAAKQQIR QYADSVTELY KLMIGGHREE LKRRVKAAGA SVFKEGTEAQ DLLLSDEVLD
RFSLSNQTRE KSPPNSHLSL LAIVDCWSKL DIVPYDHMIC STPLFRLWLG VTEYLFRNPE
LLDEALDTAI DDNTFRSDDL EFTFAARAWS DCVSFGDFES YRDRFERIAQ YFAPQFPEAA
KLGNEMMKTI LEKTENKS
//
