ID Q8Y5X9_LISMO Unreviewed; 367 AA.
AC Q8Y5X9;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN Name=tyrA {ECO:0000313|EMBL:CAD00002.1};
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963 {ECO:0000313|EMBL:CAD00002.1, ECO:0000313|Proteomes:UP000000817};
RN [1] {ECO:0000313|EMBL:CAD00002.1, ECO:0000313|Proteomes:UP000000817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; AL591981; CAD00002.1; -; Genomic_DNA.
DR PIR; AD1315; AD1315.
DR RefSeq; NP_465448.1; NC_003210.1.
DR RefSeq; WP_010989842.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y5X9; -.
DR STRING; 169963.gene:17594609; -.
DR PaxDb; 169963-lmo1924; -.
DR EnsemblBacteria; CAD00002; CAD00002; CAD00002.
DR GeneID; 985915; -.
DR KEGG; lmo:lmo1924; -.
DR PATRIC; fig|169963.11.peg.1970; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_1_9; -.
DR OrthoDB; 9802008at2; -.
DR PhylomeDB; Q8Y5X9; -.
DR BioCyc; LMON169963:LMO1924-MONOMER; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
DR GO; GO:0006571; P:tyrosine biosynthetic process; IBA:GO_Central.
DR CDD; cd04909; ACT_PDH-BS; 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 Reference proteome {ECO:0000313|Proteomes:UP000000817};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 3..292
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 297..367
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 367 AA; 40433 MW; CCCDA286CA729C9C CRC64;
MKGTIVIVGL GLIGGSIALA IKAKHPEAHI IGIDVSYHSL EVGKSLGVID EIGESILIDG
PKADLLIFCC PVKETEQLLM RLPGLRLKEN VIVTDTGSTK GTIMEASTAL RESGITFIGG
HPMAGSHKSG VRAAKELLFE NAYYLLTPTK DVTEDNVTDL KTWLSGTNAK FLVLSPNEHD
EITGMLSHLP HIVAAALVNQ TQSFTEEHPA AFRLAAGGFR DITRVASSDP RMWTDISISN
KKTLTKQLTI WRDSMNQALE MLESEDATSI YAFFDGAKEF RDSLPVHQGG AIPSFYDLFV
DVPDYPGVIS EVTRYLGEEE ISLTNIKILE TREDIFGVLQ ITFQSDEDRD RAKRCIETRS
NYTCHYE
//
