ID D0U604_9ACTN Unreviewed; 353 AA.
AC D0U604;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
OS uncultured Actinomycetes bacterium.
OC Bacteria; Actinomycetota; Actinomycetes; environmental samples.
OX NCBI_TaxID=152507 {ECO:0000313|EMBL:ACY25321.1};
RN [1] {ECO:0000313|EMBL:ACY25321.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19678830; DOI=10.1111/j.1462-2920.2009.02024.x;
RA Philosof A., Sabehi G., Beja O.;
RT "Comparative analyses of actinobacterial genomic fragments from Lake
RT Kinneret.";
RL Environ. Microbiol. 11:3189-3200(2009).
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; GQ387491; ACY25321.1; -; Genomic_DNA.
DR AlphaFoldDB; D0U604; -.
DR UniPathway; UPA00122; UER00961.
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 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; 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; 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 Signal {ECO:0000256|SAM:SignalP};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..353
FT /note="Prephenate dehydrogenase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039425135"
FT DOMAIN 4..278
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 282..353
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 353 AA; 37376 MW; 29911CF3259C3F56 CRC64;
MKQRRANIFG LGLIGGSLAA ALTARGWHVT GNDLHPDTEE EALRLGLVAA RGIDADAELS
FVATPVSSVA DQVRRALETT QGLVTDVGGV KAHIVREITD PRFVAGHPMA GSELVGLAGA
DASLFEGAVW VLTPSENTPD ANFAHVAQVV KELGAEFVVL SAERHDQLVA IVSHLPHLTA
ATLMSLANDH AEEHVAVLRL AAGGFRDMTR VASGHPAIWL DVCKENREAI IGALDGMISG
LQAMRVIVDE GKTDELKQRL QTARVARANL PGRVSNLLDV VEVRVPIPDR AGAAAEIFSL
AAELGVNTAN FEVAHSVEGD RGILVLVIDR ASQDVFKGGL IARGFRPSIQ QLT
//
