ID   TYRA_LACLM              Reviewed;         354 AA.
AC   P43901; A2RMG6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   10-JUN-2026, entry version 134.
DE   RecName: Full=Prephenate dehydrogenase;
DE            Short=PDH;
DE            EC=1.3.1.12;
GN   Name=tyrA; OrderedLocusNames=llmg_1927;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MG1363 / F15876;
RX   PubMed=7823907; DOI=10.1007/bf00290140;
RA   Griffin H.G., Gasson M.J.;
RT   "Genetic aspects of aromatic amino acid biosynthesis in Lactococcus
RT   lactis.";
RL   Mol. Gen. Genet. 246:119-127(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=prephenate + NAD(+) = 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   -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC       hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X78413; CAA55179.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL98496.1; -; Genomic_DNA.
DR   PIR; S52579; S52579.
DR   RefSeq; WP_011835675.1; NC_009004.1.
DR   AlphaFoldDB; P43901; -.
DR   SMR; P43901; -.
DR   STRING; 416870.llmg_1927; -.
DR   PaxDb; 416870-llmg_1927; -.
DR   KEGG; llm:llmg_1927; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_1_9; -.
DR   OrthoDB; 9802008at2; -.
DR   PhylomeDB; P43901; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000000364; 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:L-tyrosine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   FunFam; 1.10.3660.10:FF:000003; Prephenate dehydrogenase; 1.
DR   FunFam; 3.40.50.720:FF:000208; Prephenate dehydrogenase; 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; IPR002912; ACT_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR046825; PDH_C.
DR   InterPro; IPR046826; PDH_N.
DR   InterPro; IPR050812; Preph/Arog_dehydrog.
DR   InterPro; IPR003099; Prephen_DH.
DR   NCBIfam; NF005105; PRK06545.1-3; 1.
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; Aromatic amino acid biosynthesis; NAD;
KW   Oxidoreductase; Reference proteome; Tyrosine biosynthesis.
FT   CHAIN           1..354
FT                   /note="Prephenate dehydrogenase"
FT                   /id="PRO_0000119194"
FT   DOMAIN          2..283
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00522"
FT   DOMAIN          287..354
FT                   /note="ACT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT   BINDING         3..33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  39531 MW;  95BA5322AD509482 CRC64;
     MKKILIIGLG LIGSSIALGI KKAHPEFEIL GSDREEVENI AQKRGIIDSK VELVKGAQEA
     DIIILAVPIS VTLELLKQIA TFDLKDGLLI TDAGSTKSEI VELANQLFSG TKVKFIGGHP
     MAGSHKSGVM AADLNLFENA YYVLTEESQE LRELLKGLHA KFIILDAKEH DKVTGQVSHF
     PHILASTLVW QSDDYAKEHP LVKHLAAGGF RDLTRIAEAD SLMWTSVLLS NPEITLERIE
     NFKKHLDEIA LKITKRDSQA IEHFFEEGKK IRQAMEIHKG ALPNFYDLFI SVPDEKGVVL
     RVLALLQDFS ITNIKINEEN REDIHGQLQI SFKRAEDLQE AREIIEKATD FTVV
//