GenomeNet

Database: UniProt
Entry: A0AAD5K9F1_9FUNG
LinkDB: A0AAD5K9F1_9FUNG
Original site: A0AAD5K9F1_9FUNG 
ID   A0AAD5K9F1_9FUNG        Unreviewed;       439 AA.
AC   A0AAD5K9F1;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   10-JUN-2026, entry version 6.
DE   RecName: Full=Prephenate dehydrogenase [NADP(+)] {ECO:0000256|PIRNR:PIRNR036510};
DE            Short=PRDH {ECO:0000256|PIRNR:PIRNR036510};
DE            EC=1.3.1.13 {ECO:0000256|PIRNR:PIRNR036510};
GN   ORFNames=BDA99DRAFT_431004 {ECO:0000313|EMBL:KAI9275627.1};
OS   Phascolomyces articulosus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Lichtheimiaceae; Phascolomyces.
OX   NCBI_TaxID=60185 {ECO:0000313|EMBL:KAI9275627.1, ECO:0000313|Proteomes:UP001209540};
RN   [1] {ECO:0000313|EMBL:KAI9275627.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RSA 2281 {ECO:0000313|EMBL:KAI9275627.1};
RX   PubMed=35996588;
RA   Chang Y., Wang Y., Mondo S., Ahrendt S., Andreopoulos W., Barry K.,
RA   Beard J., Benny G.L., Blankenship S., Bonito G., Cuomo C., Desiro A.,
RA   Gervers K.A., Hundley H., Kuo A., LaButti K., Lang B.F., Lipzen A.,
RA   O'Donnell K., Pangilinan J., Reynolds N., Sandor L., Smith M.E., Tsang A.,
RA   Grigoriev I.V., Stajich J.E., Spatafora J.W.;
RT   "Evolution of zygomycete secretomes and the origins of terrestrial fungal
RT   ecologies.";
RL   IScience 25:0-0(2022).
RN   [2] {ECO:0000313|EMBL:KAI9275627.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=RSA 2281 {ECO:0000313|EMBL:KAI9275627.1};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Chang Y., Wang Y., Ahrendt S., Andreopoulos W., Barry K.,
RA   Beard J., Benny G.L., Blankenship S., Bonito G., Cuomo C., Desiro A.,
RA   Gervers K.A., Hundley H., Kuo A., LaButti K., Lang B.F., Lipzen A.,
RA   O'Donnell K., Pangilinan J., Reynolds N., Sandor L., Smith M.W., Tsang A.,
RA   Grigoriev I.V., Stajich J.E., Spatafora J.W.;
RL   Submitted (FEB-2023) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prephenate + NADP(+) = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC         NADPH; Xref=Rhea:RHEA:21640, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC         ChEBI:CHEBI:36242, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.13;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036510};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NADP(+) route): step 1/1.
CC       {ECO:0000256|PIRNR:PIRNR036510}.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000256|PIRNR:PIRNR036510}.
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:KAI9275627.1}.
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; JAIXMP010000003; KAI9275627.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD5K9F1; -.
DR   Proteomes; UP001209540; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006571; P:L-tyrosine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR046826; PDH_N.
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; PF02153; PDH_N; 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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036510};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036510};
KW   NADP {ECO:0000256|PIRNR:PIRNR036510};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036510};
KW   Reference proteome {ECO:0000313|Proteomes:UP001209540};
KW   Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          9..290
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   439 AA;  49778 MW;  4FDF6D7BC5E76519 CRC64;
     MSLEEKETIE LGIIGAGGMG RFYAQRLSKA GWKRVHVCDL PDKYEKLKED FQDSAINVLP
     DGFHVSRRCD WIMYAVEAEH IASVVAKYGP ATKMGAIVGG QTSVKQPEID ALTKYLPPDV
     HIVSCHSMHG PGVDPRGQPL VVIRQRATDE KYDLVLKILS CFESNFVHLS AEEHDRITAD
     TQAVTHAAFL SMGSAWKANF QFPWLIPHFV GGIENVKVNV AMRIYSNKWH VYAGLAIMNP
     IAKVQIAQYA RSVADLFKLM IQEKEQEFKA RIKAAGEYVF GGLQKDHVPI LLSDDILDEF
     SLSKMPKEQQ RQPNSHLSLL AMVDCWYTLR LSPYEHMVCQ TPLFRLWMGI TEYLFRNPTM
     LEDSIQAALY RKEIRPDDME FVTCARGWAE SVSLGSMEGY QKRFTETAEY FEDRYSESTI
     LGNNMIAMIS KNMGKATNE
//
DBGET integrated database retrieval system