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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//