ID Q7V9V5_PROMA Unreviewed; 288 AA.
AC Q7V9V5;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:AAQ00763.1};
GN Name=tyrA {ECO:0000313|EMBL:AAQ00763.1};
GN OrderedLocusNames=Pro_1719 {ECO:0000313|EMBL:AAQ00763.1};
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167539 {ECO:0000313|EMBL:AAQ00763.1, ECO:0000313|Proteomes:UP000001420};
RN [1] {ECO:0000313|EMBL:AAQ00763.1, ECO:0000313|Proteomes:UP000001420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120 {ECO:0000313|Proteomes:UP000001420};
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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DR EMBL; AE017126; AAQ00763.1; -; Genomic_DNA.
DR RefSeq; NP_876110.1; NC_005042.1.
DR RefSeq; WP_011125868.1; NC_005042.1.
DR AlphaFoldDB; Q7V9V5; -.
DR STRING; 167539.Pro_1719; -.
DR EnsemblBacteria; AAQ00763; AAQ00763; Pro_1719.
DR KEGG; pma:Pro_1719; -.
DR PATRIC; fig|167539.5.peg.1814; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_0_3; -.
DR OrthoDB; 9802008at2; -.
DR Proteomes; UP000001420; Chromosome.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0008977; F:prephenate dehydrogenase (NAD+) activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000001420}.
FT DOMAIN 4..288
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
SQ SEQUENCE 288 AA; 31174 MW; DDDE250A19FC46B6 CRC64;
MVLHRIGIVG LGLIGGSLGL DLQKLGYEVY GVVRRKQTLK KAQSRGLAQL ISTEFKILKD
CSMVIMALPL SQLIHPPEEL IHALPENAVI TDVGSVKVPV INSWQKLHPR FVGSHPMAGT
IETGVDAGKF GLFNNRPWIA TPNQATDLKA LEIVHQLAID LGSNWITTDP KMHDQAVALI
SHLPVFISAA LIQTVGNEKN AKLLKLAQAI ASSGFEDTTR IGGGNPYLGV AMAENNTSAI
LDAMTSYRSS IEALEAIIRS KDWSGLQQEL EATQSTRPNF INSKKLST
//
