TYRA_LACLM
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 03-AUG-2022, entry version 120.
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; Firmicutes; 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=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 -!- 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; NZ_WJVF01000007.1.
DR AlphaFoldDB; P43901; -.
DR SMR; P43901; -.
DR STRING; 416870.llmg_1927; -.
DR PRIDE; P43901; -.
DR EnsemblBacteria; CAL98496; CAL98496; llmg_1927.
DR KEGG; llm:llmg_1927; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_1_9; -.
DR OMA; MWRDICL; -.
DR PhylomeDB; P43901; -.
DR BioCyc; LLAC416870:LLMG_RS09645-MON; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000000364; Chromosome.
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 InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003099; Prephen_DH.
DR Pfam; PF02153; PDH; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 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; 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