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Database: UniProt
Entry: A0A0D1DTR5_MYCMD
LinkDB: A0A0D1DTR5_MYCMD
Original site: A0A0D1DTR5_MYCMD 
ID   A0A0D1DTR5_MYCMD        Unreviewed;       467 AA.
AC   A0A0D1DTR5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   10-JUN-2026, entry version 44.
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=UMAG_04182 {ECO:0000313|EMBL:KIS67679.1};
OS   Mycosarcoma maydis (Corn smut fungus) (Ustilago maydis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginales incertae sedis;
OC   Mycosarcoma.
OX   NCBI_TaxID=5270 {ECO:0000313|EMBL:KIS67679.1, ECO:0000313|Proteomes:UP000000561};
RN   [1] {ECO:0000313|EMBL:KIS67679.1, ECO:0000313|Proteomes:UP000000561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14603 / FGSC 9021 / UM521
RC   {ECO:0000313|Proteomes:UP000000561};
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA   de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA   Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA   Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA   Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA   Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA   Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA   Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA   Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA   Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA   Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA   Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA   Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA   Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
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|ARBA:ARBA00051295,
CC         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|ARBA:ARBA00060605, ECO:0000256|PIRNR:PIRNR036510}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007964, ECO:0000256|PIRNR:PIRNR036510}.
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DR   EMBL; CM003151; KIS67679.1; -; Genomic_DNA.
DR   RefSeq; XP_011390669.1; XM_011392367.1.
DR   AlphaFoldDB; A0A0D1DTR5; -.
DR   FunCoup; A0A0D1DTR5; 87.
DR   STRING; 237631.A0A0D1DTR5; -.
DR   GeneID; 23564440; -.
DR   KEGG; uma:UMAG_04182; -.
DR   VEuPathDB; FungiDB:UMAG_04182; -.
DR   eggNOG; KOG2380; Eukaryota.
DR   InParanoid; A0A0D1DTR5; -.
DR   OMA; WRVNACD; -.
DR   OrthoDB; 5399569at2759; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000000561; Chromosome 12.
DR   GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006571; P:L-tyrosine biosynthetic process; IBA:GO_Central.
DR   FunFam; 1.10.3660.10:FF:000004; Prephenate dehydrogenase [NADP(+)]; 1.
DR   FunFam; 1.10.3660.10:FF:000006; 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; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR046825; PDH_C.
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; PF03807; F420_oxidored; 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|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036510};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498,
KW   ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          10..291
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   467 AA;  52400 MW;  D242CE94F1C69800 CRC64;
     MASSTEMDTL EIGIIGMGDM GRLYATKMRD AGWKKVNVCD RPENHEKLCK ELQGSGLNVL
     RDGHLVSRRS DFIIYSVEAA FIDKVVEQYG SSTKIGSIVA GQTSVKAPEK AAFEKHLPQD
     TYIISCHSMH GPKIDPTGQP LILIQHRAPD EKMRLVERIM ACFKSNFVYL TYEEHDTVTA
     NTQAVTHAAF LSMGTAWCCS NQYPWESERY PGGIETVKIN ICLRIYSAKW HVYAGLALLN
     PAAKTQVTQF AQSCTDLFKL MVAEREQQLM DRVFAARKKV FGWEKDEESN SVISRTGTRE
     ERKPILMSDK LLDRFHMAAR KATSFVVNGD AAADSSDAAT ALSQSPPNSH LSLLAIVDCW
     SSLGINPYDH LDLAATPIFR IWIGVCEYLF RSPERLRQAC HAAARDHSFR ADDTEFVIAS
     RGWAQAVQFG NFDSYQRRFE ETRGFFEHRF QEAGAVGAEM LKVVLAN
//
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