ID Q2H9P8_CHAGB Unreviewed; 425 AA.
AC Q2H9P8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=CHGG_03056 {ECO:0000313|EMBL:EAQ91121.1};
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ91121.1, ECO:0000313|Proteomes:UP000001056};
RN [1] {ECO:0000313|Proteomes:UP000001056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC {ECO:0000313|Proteomes:UP000001056};
RX PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(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; CH408030; EAQ91121.1; -; Genomic_DNA.
DR RefSeq; XP_001229572.1; XM_001229571.1.
DR AlphaFoldDB; Q2H9P8; -.
DR STRING; 306901.Q2H9P8; -.
DR GeneID; 4389404; -.
DR VEuPathDB; FungiDB:CHGG_03056; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; Q2H9P8; -.
DR OMA; GDMGLLY; -.
DR OrthoDB; 1348131at2759; -.
DR UniPathway; UPA00122; UER00962.
DR Proteomes; UP000001056; 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; 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; 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:UP000001056};
KW Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT DOMAIN 10..277
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 425 AA; 47760 MW; FD6D91CD615532DF CRC64;
MATFQGAEDF VIGLIGMGDM GKMIMACDRE EKYEELAAEF ADHRPPLVVL SLSTVHVCAI
RNAVVCLDII LTKCHLVATR LGAIVGGQTS CKDPEIKAFE EHLPSDVDIV SCHSLHGPSV
DPRDQPLVLI KHRASDASFN KVETALRCLG SKHVYLTARE HDRITADTQA VTHAAFLSMG
KAWHANQQFP WEGTRYVGGI ENVKINLMLR IYAQKWHVYA GLAILNPEAH KQINQFARST
TELFYLMLEG RRDELRERVY AAKEKVFGRE GSPKWEGRPL LPDGVVDRFS LNANAKSNAP
AMPNNHLSLL AMVDCWSALG IVPYDHMICS TPLFRLWLGV TEHLFRTPGL LDESLRVGIE
DNTFRRDDLQ FTIAASGWAE CVALRQFETW RERFAVTQKF FEPRFKGAVE VGQAMIRAVL
ESEKE
//