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Database: UniProt
Entry: F0RDP6_CELLC
LinkDB: F0RDP6_CELLC
Original site: F0RDP6_CELLC 
ID   F0RDP6_CELLC            Unreviewed;       286 AA.
AC   F0RDP6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:ADY29807.1};
DE            EC=1.3.1.12 {ECO:0000313|EMBL:ADY29807.1};
GN   OrderedLocusNames=Celly_1985 {ECO:0000313|EMBL:ADY29807.1};
OS   Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS   NCIMB 1423 / VKM B-1433 / Cy l20).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29807.1, ECO:0000313|Proteomes:UP000007487};
RN   [1] {ECO:0000313|EMBL:ADY29807.1, ECO:0000313|Proteomes:UP000007487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC   VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX   PubMed=21677859; DOI=10.4056/sigs.1774329;
RA   Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Ivanova N.;
RT   "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL   Stand. Genomic Sci. 4:221-232(2011).
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DR   EMBL; CP002534; ADY29807.1; -; Genomic_DNA.
DR   RefSeq; WP_013621552.1; NC_015167.1.
DR   AlphaFoldDB; F0RDP6; -.
DR   STRING; 867900.Celly_1985; -.
DR   KEGG; cly:Celly_1985; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_0_10; -.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000007487; 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:ADY29807.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007487}.
FT   DOMAIN          1..286
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   286 AA;  31931 MW;  A81A63EA3D32F228 CRC64;
     MNVFVIGIGL IGGSMAKDIK RINASAKIYG VDINDAHIEE ALSLGVIDQK ASYHDLQLAD
     VVIVSIPVDV MVVELPKILD AINDDAIVLD AGSTKGLICK QVENHPKRRN FIACHPIAGT
     EFSGPSAAIE NLFKGKTNII CEVEKTAFKL QEKALDLFRD MGMRIRYMNV DAHDKHIAYV
     SHLSHISSFM LGKTVIEKEK NERDIFDMAG SGFESTVRLA KSSPAMWTPI FKQNKTNVLE
     TLEEYIQNLK AFKEMIEEDN YTGIYNEMES TNKIKEILKG IPQNKN
//
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