GenomeNet

Database: UniProt
Entry: A0A2S7PR60_9HELO
LinkDB: A0A2S7PR60_9HELO
Original site: A0A2S7PR60_9HELO 
ID   A0A2S7PR60_9HELO        Unreviewed;       441 AA.
AC   A0A2S7PR60;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   22-FEB-2023, entry version 13.
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=CJF30_00003447 {ECO:0000313|EMBL:PQE16753.1};
OS   Rutstroemia sp. NJR-2017a BBW.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Rutstroemiaceae; Rutstroemia.
OX   NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE16753.1, ECO:0000313|Proteomes:UP000238072};
RN   [1] {ECO:0000313|EMBL:PQE16753.1, ECO:0000313|Proteomes:UP000238072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE16753.1,
RC   ECO:0000313|Proteomes:UP000238072};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NADP(+) + prephenate = 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:PQE16753.1}.
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; NJPT01000042; PQE16753.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S7PR60; -.
DR   STRING; 2070414.A0A2S7PR60; -.
DR   UniPathway; UPA00122; UER00962.
DR   Proteomes; UP000238072; Unassembled WGS sequence.
DR   GO; GO:0050661; F:NADP 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:tyrosine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
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; PF03446; NAD_binding_2; 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   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:UP000238072};
KW   Tyrosine biosynthesis {ECO:0000256|PIRNR:PIRNR036510}.
FT   DOMAIN          15..296
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   441 AA;  50220 MW;  6FAE389DD939E626 CRC64;
     MAAIRTKFDG LKDEFVVGII GMGDMGKMYA RRLSEAGWRV NACDREEKYE ALKEEWADRN
     QVTILPNGHL VSRASDYIIY NVEAASIGKV VAQYGPSTKQ GAIVGGQTSC KAPEIDAFEK
     YLPPDVDIVS CHSLHGPAVD PRGQPLIFIK HRASQENFEK VEHVLSCLGS KHHNLSAREH
     DRITADTQAV THAAFLSMGK AWHANQQFPW EIARYIGGIE NVKINLTLRI YSQKWHVYAG
     LAILNPYAKE QIREYAQSVT DLYKLMLGGH RRELEERIKS AGRFVFGHRK GSSNEDLLLR
     DEVLDRFSLG RKPETPTPNN HLSLLAIVDC WARLNIIPYD HMICSTPLFR LWLGVTEYLF
     RNSKLLDEVI NTAIEDNTFR SDDLEFTFAA RGWSECVEFG DFESWKDRFE KTQTFFAPRF
     AEATKVGNEM MKTILQNTKK D
//
DBGET integrated database retrieval system