ID TYRA_STAA3 Reviewed; 363 AA. AC Q2FH71; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 24-JAN-2024, entry version 99. DE RecName: Full=Prephenate dehydrogenase; DE Short=PDH; DE EC=1.3.1.12; GN Name=tyrA; OrderedLocusNames=SAUSA300_1260; OS Staphylococcus aureus (strain USA300). OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=367830; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=USA300; RX PubMed=16517273; DOI=10.1016/s0140-6736(06)68231-7; RA Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., RA Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., RA Perdreau-Remington F.; RT "Complete genome sequence of USA300, an epidemic clone of community- RT acquired meticillin-resistant Staphylococcus aureus."; RL Lancet 367:731-739(2006). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000255; ABD20619.1; -; Genomic_DNA. DR RefSeq; WP_000214266.1; NZ_CP027476.1. DR AlphaFoldDB; Q2FH71; -. DR SMR; Q2FH71; -. DR KEGG; saa:SAUSA300_1260; -. DR HOGENOM; CLU_055968_2_1_9; -. DR OMA; MWRDICL; -. DR UniPathway; UPA00122; UER00961. DR Proteomes; UP000001939; 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; 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; Aromatic amino acid biosynthesis; NAD; KW Oxidoreductase; Tyrosine biosynthesis. FT CHAIN 1..363 FT /note="Prephenate dehydrogenase" FT /id="PRO_0000282662" FT DOMAIN 2..291 FT /note="Prephenate/arogenate dehydrogenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00522" FT DOMAIN 296..363 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 363 AA; 40395 MW; 8F16333DC3B816C6 CRC64; MTTVLFVGLG LIGGSLASNI KYHNPNTNII AYDADTSQLD KAKSIGIINE KCLNYSEAIK KADVIIYATP VAITNKYLSE LIDMPTKPGV IVSDTGSTKA MIQQHECNLL KHNIHLVSGH PMAGSHKSGV LNAKKHLFEN AYYILVYNEP RNEQAANTLK ELLSPTLAKF IVTTAEEHDY VTSVVSHLPH IVASSLVHVS QKNGQEHHLV NKLAAGGFRD ITRIASSNAQ MWKDITLSNK TYILEMIRQL KSQFQDLERL IESNDSEKLL SFFAQAKSYR DALPAKQLGG LNTAYDLYVD IPDESGMISK VTYILSLHNI SISNLRILEV REDIYGALKI SFKNPTDRER GMQALSDFDC YIQ //