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Database: UniProt
Entry: A0A0J0XI18_9TREE
LinkDB: A0A0J0XI18_9TREE
Original site: A0A0J0XI18_9TREE 
ID   A0A0J0XI18_9TREE        Unreviewed;       486 AA.
AC   A0A0J0XI18;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   03-MAY-2023, entry version 29.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:KLT40746.1};
GN   ORFNames=CC85DRAFT_287158 {ECO:0000313|EMBL:KLT40746.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT40746.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT40746.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT40746.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KQ087229; KLT40746.1; -; Genomic_DNA.
DR   RefSeq; XP_018277237.1; XM_018423759.1.
DR   AlphaFoldDB; A0A0J0XI18; -.
DR   STRING; 879819.A0A0J0XI18; -.
DR   GeneID; 28984362; -.
DR   OrthoDB; 1348131at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
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:tyrosine biosynthetic process; IEA:InterPro.
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; 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; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF036510; PDH_fung; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
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:UP000053611}.
FT   DOMAIN          15..295
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   REGION          440..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..467
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  53555 MW;  B8F0742A95CE025A CRC64;
     MSTSFDPRSA ATTGPVIGII GMGDMGRMYA RRLNDAGHTV IVCDRPEAYD RLASEYRGSG
     ITALYDGHAV SRAADFIIYS VEAAYIGDVV AEYGPSTKIG ATVAGQTSVK APEKVAFDKY
     LPADVDIVSV HSLHGPGVTT EGQPLIIIHH RGPKEKVTMV EDVFRSFKSR YVYLTYEEHD
     EVTANTQAVT HAAFLSMGMA WKAEGGYPWE KARWVSGIEV IKVNITLRIY AAKWHVYAGL
     AILNPAAQRQ IEQYARSASE LFKLMIGGHR AELEKRVWAA REAVFGWKRE QDAELDEAGG
     RQPILLSEDV LDQFSLGTHD KNAVEEPNSH LSLLAMVDCW AALGIRPFEH LEVAGTPVFM
     LWIGVAEHLF RSRDRLDKAI DAGITDRVFR PDDLEFTVAA RGWNECVNFG NFDLYERRFK
     EAAGESLAGG GGPPIGCLSR SSAAGRTRTR CTRGGMSHGD TRKKSRQSPL ARTSMRPSWC
     DARGSR
//
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