ID   A2CC19_PROM3            Unreviewed;       314 AA.
AC   A2CC19;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 89.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:ABM79029.1};
DE            EC=1.3.1.12 {ECO:0000313|EMBL:ABM79029.1};
GN   Name=tyrA {ECO:0000313|EMBL:ABM79029.1};
GN   OrderedLocusNames=P9303_22941 {ECO:0000313|EMBL:ABM79029.1};
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=59922 {ECO:0000313|EMBL:ABM79029.1, ECO:0000313|Proteomes:UP000002274};
RN   [1] {ECO:0000313|EMBL:ABM79029.1, ECO:0000313|Proteomes:UP000002274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303 {ECO:0000313|EMBL:ABM79029.1,
RC   ECO:0000313|Proteomes:UP000002274};
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
CC   -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00007964}.
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DR   EMBL; CP000554; ABM79029.1; -; Genomic_DNA.
DR   RefSeq; WP_011826897.1; NC_008820.1.
DR   AlphaFoldDB; A2CC19; -.
DR   STRING; 59922.P9303_22941; -.
DR   KEGG; pmf:P9303_22941; -.
DR   HOGENOM; CLU_055968_2_0_3; -.
DR   BioCyc; PMAR59922:G1G80-2010-MONOMER; -.
DR   Proteomes; UP000002274; 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:InterPro.
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; 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; NF005650; PRK07417.1; 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; PS51176; PDH_ADH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00522};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00522};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|PROSITE-
KW   ProRule:PRU00522}; Reference proteome {ECO:0000313|Proteomes:UP000002274};
KW   Tyrosine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00522}.
FT   DOMAIN          18..302
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   314 AA;  33344 MW;  1A9D9A66F83926B1 CRC64;
     MDCSARTEGM EQNKKTSLCA GVVGLGLIGG SLGLDLQALG WKVNGLVHRS STADRARARG
     LAHLVSTDPG ILADCDLVIL ALPLAQLLNP DPNLLKALPT AAVVTDVGSV KMPVLELWRD
     LHPRFVASHP MAGTAEAGVE AGLRGLFQQR PWVATPDNQT DLEALELVRR FAVSLGSQWF
     TADAANHDQA VALISHLPVL VSAALLRTVG EERDPAVREL ARVLSSSGFA DTTRVGGGNP
     QLGTSMAESN TAAILRGLAA YRWSLEQLEE AVLNGHWSQL KAELERSQAL RPSFLVAANN
     DLNSPPVTDD LAEP
//