ID A0A2S5B5U4_9BASI Unreviewed; 459 AA.
AC A0A2S5B5U4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 10-JUN-2026, entry version 17.
DE RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN ORFNames=BMF94_4785 {ECO:0000313|EMBL:POY72148.1};
OS Rhodotorula taiwanensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=741276 {ECO:0000313|EMBL:POY72148.1, ECO:0000313|Proteomes:UP000237144};
RN [1] {ECO:0000313|EMBL:POY72148.1, ECO:0000313|Proteomes:UP000237144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD1149 {ECO:0000313|EMBL:POY72148.1,
RC ECO:0000313|Proteomes:UP000237144};
RX PubMed=29375494;
RA Tkavc R., Matrosova V.Y., Grichenko O.E., Gostincar C., Volpe R.P.,
RA Klimenkova P., Gaidamakova E.K., Zhou C.E., Stewart B.J., Lyman M.G.,
RA Malfatti S.A., Rubinfeld B., Courtot M., Singh J., Dalgard C.L.,
RA Hamilton T., Frey K.G., Gunde-Cimerman N., Dugan L., Daly M.J.;
RT "Prospects for Fungal Bioremediation of Acidic Radioactive Waste Sites:
RT Characterization and Genome Sequence of Rhodotorula taiwanensis MD1149.";
RL Front. Microbiol. 8:2528-2528(2018).
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:POY72148.1}.
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DR EMBL; PJQD01000057; POY72148.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5B5U4; -.
DR STRING; 741276.A0A2S5B5U4; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000237144; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:TreeGrafter.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0006571; P:L-tyrosine biosynthetic process; IEA:InterPro.
DR FunFam; 1.10.3660.10:FF:000004; 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; IPR050812; Preph/Arog_dehydrog.
DR InterPro; IPR003099; Prephen_DH.
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 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000237144}.
FT DOMAIN 15..298
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 459 AA; 50724 MW; DB265137BBAFE489 CRC64;
MAGQQPPSPP PIEDAVIGLI GMGEMGKMYA ERLSKGGKCA RINVCDLPER FEELQEYCKG
KSKVVPMRDG HLVSRESDFI IYSVEAAYLD RVVAQYGSST KVGAVVSGQT SVKAPERAAF
ERYLPADVNV VSIHSLHGPT VPSDGQALIV IKHRATDEQV QWVKDLLSPL NSRYVDLSYD
EHDEVTANTQ AVTHAAFLSM GTAWRCMGTF PWASGRYIGG IEVVKVNIAL RIYAAKWHVY
AGLAILNPTA QKQIHQFAQS ATDLFKMMIQ SREDELRERV YAARDFVFGR SGDSSSEDSA
TPILLSDSAL DRFAIGNPSP TQPAAPPNSH LALLAMVDSW HQLRIRPFVH LALAATPVFR
FWIGVAEYLF RDEDRLKAAI KAGGSAGSEG VAFSSDDAEF VIAARGWSDT VRYGSFDAYK
QRFDETRAFF EPQFEESRVA NRDMFAFLAS EPIRTAVQK
//
