ID J4G712_9APHY Unreviewed; 986 AA.
AC J4G712;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 10-JUN-2026, entry version 50.
DE RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN ORFNames=FIBRA_04220 {ECO:0000313|EMBL:CCM02143.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM02143.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM02143.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM02143.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; HE797065; CCM02143.1; -; Genomic_DNA.
DR RefSeq; XP_012181426.1; XM_012326036.1.
DR AlphaFoldDB; J4G712; -.
DR STRING; 599839.J4G712; -.
DR GeneID; 24097054; -.
DR HOGENOM; CLU_302478_0_0_1; -.
DR InParanoid; J4G712; -.
DR OrthoDB; 5399569at2759; -.
DR Proteomes; UP000006352; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 1.20.1740.10:FF:000039; Neutral amino acid transporter (Eurofung); 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; IPR013057; AA_transpt_TM.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PF01490; Aa_trans; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006352};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 502..802
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT REGION 819..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..854
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 106984 MW; 34FFA25AE9DB094C CRC64;
MATKHEGSIE GSQDETLYSS HEHDFGRIGH PKEHIAVAEN DAYDVYGDEE SAEIKYRTMV
WWKAAALMLA ETVSLGILSI PSVFASLGMV AGCILVISLG AIATATGYLI GLFKLRYPHI
HNMADAGMVL AGPIGREVLG AAQIIFMVFL CGSHVLTGLI AFDTITAGAS CSVLWAGVTA
IICIILTIPR TLNGISYLSV ASFISILSAV LITMIGVGVA GHKGGVTARA NLSFASAFLS
VTDIIFAYAG HVAFFTFISE MRKPEDFPKA LYLLQIADTT LYLIVGIVVY AYAGADTVSP
ALGNTGTILR KIAYGIALPT IIVAGVINGH VCAKLVFIRI FRRDGVKSRH MTTHSWVGWL
TWIGICFAIW ALAFVIAEVI PFFNDLLGVI SSVFASWFTY GISVSATGSD VEIDVMTVGS
GYLLVPSDPT IRVVVYTTPE TEMCILGGYH SDPNPNLILL QMGAFIMVAG LYASIDSIVE
GAMVALKIRP DVTPDSPLEE QPAIGIIGMG SMGVMYVKYL EAGGWKKIYV CDIPSKYEAL
KEKYQDHSCV TVLRDGHLVS RISDFIMYAV EAEFICKVVE MYGPSTKVGA IVAGQTSVKA
PEKIAFEQYL PEDVFIVSCH SLHGPTVSPL GQPLVSVLSF ASSSLYVIFE FQVLTKHRAP
DEALTLVENI LAPLRSRYVY LSYEEHDTVT ANTQAVTHAA FLSMGTAWKD ELEYPWETGN
YVGGIETVKV NIMLRIYSNK WHVYAGLAIL NPSARVQIDQ YARSVTEIYK LMVAGDDAGL
RRRIYNARDR VFGSGMSDGR APILLSEDIL DRFSLGRRPS SASAKANGIY NGNGVPNGNG
STTPGSPGSP RTSRANSHLS LLGMVDCWAQ LGIQPFVHLD LAATPIFRML LGVSEYLFRS
PERLESAVNA ALYDTTYRAN DLEFVVAARG WSQCISFGSF ELYQRRFTDT SAFFESRFED
ATKLGSAMMQ AILDSSQTDG AHLADP
//
