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Database: UniProt
Entry: A2BTE4_PROMS
LinkDB: A2BTE4_PROMS
Original site: A2BTE4_PROMS 
ID   A2BTE4_PROMS            Unreviewed;       279 AA.
AC   A2BTE4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:ABM71055.1};
DE            EC=1.3.1.12 {ECO:0000313|EMBL:ABM71055.1};
GN   Name=tyrA {ECO:0000313|EMBL:ABM71055.1};
GN   OrderedLocusNames=A9601_17721 {ECO:0000313|EMBL:ABM71055.1};
OS   Prochlorococcus marinus (strain AS9601).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Prochlorococcus.
OX   NCBI_TaxID=146891 {ECO:0000313|EMBL:ABM71055.1, ECO:0000313|Proteomes:UP000002590};
RN   [1] {ECO:0000313|EMBL:ABM71055.1, ECO:0000313|Proteomes:UP000002590}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS9601 {ECO:0000313|EMBL:ABM71055.1,
RC   ECO:0000313|Proteomes:UP000002590};
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).
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DR   EMBL; CP000551; ABM71055.1; -; Genomic_DNA.
DR   RefSeq; WP_011819177.1; NC_008816.1.
DR   AlphaFoldDB; A2BTE4; -.
DR   STRING; 146891.A9601_17721; -.
DR   KEGG; pmb:A9601_17721; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_0_3; -.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000002590; 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: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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51176; PDH_ADH; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:ABM71055.1}.
FT   DOMAIN          1..279
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   279 AA;  30545 MW;  FEA8A3D3A5096431 CRC64;
     MKIGIVGLGL IGGSLGLKLQ SLNHTIYGIA NNEFNEKKAK DKKLANFVSC DLSLLKKCEL
     IILALPIKDL ISPSQQLVAS IPQETIITDV GSVKEPIVNT WENLHPLFIG SHPMAGTEKK
     GVDSGFEGLF KNAKWIITPT QNSDLNSVRT ISELIKSMHC EICQASPKEH DEAVSLISHL
     PIFLASALIE TAQTKNNQSL LDLTQKLAAT GFADTSRVGG GNEQLGLDLA INNQINILNS
     INNFKNKLNI LESLIKEKNW DLLSKKLAEA KENRQNFIN
//
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