ID A0A316UFM9_9BASI Unreviewed; 497 AA.
AC A0A316UFM9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 10-JUN-2026, entry version 25.
DE RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN ORFNames=BCV69DRAFT_265510 {ECO:0000313|EMBL:PWN24062.1};
OS Microstroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromataceae; Microstroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN24062.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN24062.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN24062.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad Genomic Sampling Reveals a Smut Pathogenic Ancestry of the Fungal
RT Clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 35:1840-1854(2018).
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DR EMBL; KZ819321; PWN24062.1; -; Genomic_DNA.
DR RefSeq; XP_025351222.1; XM_025490786.1.
DR AlphaFoldDB; A0A316UFM9; -.
DR STRING; 1684307.A0A316UFM9; -.
DR GeneID; 37012520; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000245942; 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; 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; 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:UP000245942}.
FT DOMAIN 18..298
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT REGION 292..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..319
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 55008 MW; EA3EA474B8C182E4 CRC64;
MTLAGGSGRH RLEGDDKIEV GIIGIGDMGR LYAAKINAAG WIVNVCDRPE KYESLQEEYK
GTSINVYKDG HLVSRRSDLI IYSVEAALIY NVVAQYGPST KMGAIVSGQT SVKAPEQRAF
EAHLPADSYI ISCHSLHGPK VDPTGQPLVL IQHRAPDEKM RLMERIMAAF GSRIVLLSYQ
EHDVVTANTQ AVTHAAFLAM GAAWRCSGDY PWETDRWAGP IETVKINIMI RILSAKWHVY
AGLAILNPSA RIQVTQYAKS VSDLFKLMIA DRHDEMLRRV FEARRKVFGW QDDEQPAAAG
EGKDANTSAT TGTTTSSSTR QQRPILMSDA MLAQFHQAAR KVAPPPPTDG SSTDQPAAGT
TEQQTTDSSS PPVRPPNSHL SLLAIVDCWH HLGIDPYAHL ELAATPIFRI WIGVCEYLFR
SPARLRASIR AAVEDPTFRG DDTEFVVAAR GWAEAVNAGN FEHYEWRFKD TARFFEPRFE
EANKVGAEML KVVMSSR
//
