ID A0A345HK95_9ACTN Unreviewed; 361 AA.
AC A0A345HK95;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=DVK44_04830 {ECO:0000313|EMBL:AXG77119.1};
OS Streptomyces paludis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282738 {ECO:0000313|EMBL:AXG77119.1, ECO:0000313|Proteomes:UP000253868};
RN [1] {ECO:0000313|Proteomes:UP000253868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSSD-12 {ECO:0000313|Proteomes:UP000253868};
RA Zhao J.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001162};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005067}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007964}.
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DR EMBL; CP031194; AXG77119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345HK95; -.
DR KEGG; spad:DVK44_04830; -.
DR OrthoDB; 9802008at2; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000253868; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02116; ACT; 1.
DR Gene3D; 1.10.3660.10; 6-phosphogluconate dehydrogenase C-terminal like domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR046825; PDH_C.
DR InterPro; IPR046826; PDH_N.
DR InterPro; IPR003099; Prephen_DH.
DR PANTHER; PTHR21363; PREPHENATE DEHYDROGENASE; 1.
DR PANTHER; PTHR21363:SF0; PREPHENATE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF20463; PDH_C; 1.
DR Pfam; PF02153; PDH_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AXG77119.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253868};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 2..289
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 294..361
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 254..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 37217 MW; 37DC47E5159EB662 CRC64;
MRTALVIGTG LIGTSVALAL AGRGVTVHLR DHDPTRARTA AALGAGTDEE PAGPVDLAVV
AVPPTHVAAT LAAEMRAGAA RGYLDVASVK GGPRRELAAL GADLSAYIGT HPMAGKERSG
PLAGSADLFD GRPWVLTPTR DTDTEVLNLA LELVALCRAV PVVMDADAHD RAVALVSHTP
QLISSMVAAR LETADETDVR LCGQGIRDVT RIAASDPAMW VEILSANPGP VADVLSGIAA
DLAETVESLR ALQSADDEKR QGGAAGIEDV LRRGNAGRER VPGKHGAAPA AYEIVAVHVS
DQPGELARIF ADAGRAGVNV EDVRIEHATG QQAGLVQVMV DPAAAPVLAA ALRERGWSIR
Q
//