ID K9FZ05_PEND2 Unreviewed; 392 AA.
AC K9FZ05;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 10-JUN-2026, entry version 38.
DE RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN ORFNames=PDIG_29790 {ECO:0000313|EMBL:EKV14900.1};
OS Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV14900.1, ECO:0000313|Proteomes:UP000009882};
RN [1] {ECO:0000313|Proteomes:UP000009882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT postharvest pathogen of citrus.";
RL BMC Genomics 13:646-646(2012).
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:EKV14900.1}.
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; AKCT01000128; EKV14900.1; -; Genomic_DNA.
DR AlphaFoldDB; K9FZ05; -.
DR FunCoup; K9FZ05; 221.
DR STRING; 1170229.K9FZ05; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_1_0_1; -.
DR InParanoid; K9FZ05; -.
DR OMA; WRVNACD; -.
DR OrthoDB; 32462at5073; -.
DR Proteomes; UP000009882; 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; 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 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:UP000009882}.
FT DOMAIN 1..247
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 392 AA; 43776 MW; B6D59C8E5E612B04 CRC64;
MGRTKEDASI GIIGMGDMGK MYAQRLSDAG WSVEAGAIDK VVAQYGLSTK VGAVVGGQTS
CKAPELAAFE KHLPSDVEIV SCHSLHGPKV NPQGQPLVLI QHRASDESLK FVESILSSFK
SKHVYLTGEM HDRITADTQA VTHAAFLSMG TAWQANNQFP WEHGRWVGGI ENVKINITLR
IYSNKWHVYA GLAILNPAAK QQIRQYAESV TDLYKLMIGG QREELKRRVK AAGASVFRPG
SEGQDLLLKD EVLDRFSLSN RPREKAPPNS HLSLLAIVDC WSKLGIVPYD HMICSTPLFR
LWLGVTEYLF RNQDLLDEAL DTAIDDNTFR SDDLEFTFAA RAWSDCVSFG DFESYRHRFE
RIAEYFAPRF PEAATLGNEM MKTILDKTTS NK
//