ID D4ANH7_ARTBC Unreviewed; 361 AA.
AC D4ANH7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 10-JUN-2026, entry version 51.
DE RecName: Full=Prephenate/arogenate dehydrogenase domain-containing protein {ECO:0000259|PROSITE:PS51176};
GN ORFNames=ARB_05782 {ECO:0000313|EMBL:EFE35738.1};
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331 {ECO:0000313|EMBL:EFE35738.1, ECO:0000313|Proteomes:UP000008866};
RN [1] {ECO:0000313|Proteomes:UP000008866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000313|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE35738.1}.
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DR EMBL; ABSU01000003; EFE35738.1; -; Genomic_DNA.
DR RefSeq; XP_003016383.1; XM_003016337.1.
DR AlphaFoldDB; D4ANH7; -.
DR STRING; 663331.D4ANH7; -.
DR GeneID; 9521866; -.
DR KEGG; abe:ARB_05782; -.
DR eggNOG; KOG2380; Eukaryota.
DR HOGENOM; CLU_031403_0_0_1; -.
DR OMA; WRVNACD; -.
DR Proteomes; UP000008866; 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; IPR046825; PDH_C.
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; PF20463; PDH_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008866}.
FT DOMAIN 1..217
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 361 AA; 41020 MW; DFBF80307A14171F CRC64;
MIVEAKFIAS VVEEYGPSTK VGAIVGGQTS CKAPELEAFE KYLPSDVEIL SCHSLHGPNV
NPKGQPLVLI QHRASDESLK FVEEIFRSFQ STYVYLSGEM HDRITADTQA VTHAAFLSMG
TAWHANSQFP WEVPRYVGGI ENVKINITLR IYANKWHVYA GLAILNPAAK KQIRQYAESV
TELYKLMLGG HREELTKRIK TARAAVFKSN SARQDLLLQD NVLDRFSLSK GGTERMPNNH
LSLLAIVDCW WKLGIVPYDH MICSTPLFRL WLGVTEYLFQ NEELLDEVID TAIEDNTFRS
DDLEFTFAAR AWSECVSFGD FESYRDRFEK IQSYFAPRFP EAVRVGNEMM KTILEKTSKP
S
//
