ID A0A364L395_TALAM Unreviewed; 382 AA.
AC A0A364L395;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 10-JUN-2026, entry version 19.
DE RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN ORFNames=BHQ10_006203 {ECO:0000313|EMBL:RAO70191.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO70191.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO70191.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO70191.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential beta-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
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:RAO70191.1}.
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DR EMBL; MIKG01000011; RAO70191.1; -; Genomic_DNA.
DR RefSeq; XP_040734707.1; XM_040878764.1.
DR AlphaFoldDB; A0A364L395; -.
DR STRING; 1196081.A0A364L395; -.
DR GeneID; 63795419; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000249363; 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:000002; Prephenate dehydrogenase [NADP(+)]; 1.
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; 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; 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 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363}.
FT DOMAIN 1..236
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 382 AA; 43151 MW; CD1E454CD3EA88E4 CRC64;
MVLTKDNASI GIIGMGDMGK IVEAAYIDKI VAEYGPSTKV GAIVGGQTSC KSPELAAFDK
HLPSDVEIIS CHSLHGPKVN TKGQPLVLIQ HRASDESMRF IERVFESFES QYVYLSGEMH
DRITADTQAV THAAFLSMGT AWYANNQFPW EIDRWVGGIE NVKINITLRI YANKWHVYAG
LAILNPAAQK QIRQYAKSVT ELYKLMIEGK RDELKTRVKE AGAAVFKSDT EGQDLLLRDE
VLDRFSLSNK DSREEAPPNN HLSLLAIVDC WSKLGIVPYD HMICSTPLFR LWLGVTEYLF
RNPSLLDEVL DIAIDDQTFR SDDLEFTFAA RAWSDCVSFG DFESYRDRFE RIQSYFAPRF
PDAVKLGNEM MKTILEKTSD HA
//
