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Database: UniProt
Entry: D5CTX8_SIDLE
LinkDB: D5CTX8_SIDLE
Original site: D5CTX8_SIDLE 
ID   D5CTX8_SIDLE            Unreviewed;       289 AA.
AC   D5CTX8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:ADE12290.1};
DE            EC=1.3.1.12 {ECO:0000313|EMBL:ADE12290.1};
GN   OrderedLocusNames=Slit_2062 {ECO:0000313|EMBL:ADE12290.1};
OS   Sideroxydans lithotrophicus (strain ES-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Gallionellaceae; Sideroxydans.
OX   NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE12290.1, ECO:0000313|Proteomes:UP000001625};
RN   [1] {ECO:0000313|EMBL:ADE12290.1, ECO:0000313|Proteomes:UP000001625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ES-1 {ECO:0000313|EMBL:ADE12290.1,
RC   ECO:0000313|Proteomes:UP000001625};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT   "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001965; ADE12290.1; -; Genomic_DNA.
DR   RefSeq; WP_013030188.1; NC_013959.1.
DR   AlphaFoldDB; D5CTX8; -.
DR   STRING; 580332.Slit_2062; -.
DR   KEGG; slt:Slit_2062; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_0_1_4; -.
DR   OrthoDB; 9809920at2; -.
DR   Proteomes; UP000001625; 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:ADE12290.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001625}.
FT   DOMAIN          6..289
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   289 AA;  31395 MW;  05B69FD4B247D96F CRC64;
     MQPAFRKVVI FGVGLIGGSF ALALRKAGAV GEVVGFGRSA TTLQQAKQFG IIDRMGEDVA
     HEVADASLVL LATPVAQMAD IFMRIAPHLG AHTLVTDGGS TKSDVVVAAR TNLKDRIAHF
     VPAHPIAGAE QSGPAAALEE LYQGKKVVLT PLPENSKEAV ARVRKAWELC GAMVSELTSQ
     QHDEVFAAVS HLPHLLSFAL VHDLAQRDNR DQLLSFAASG FRDFTRIAAS SPEMWRDISL
     ANREALLQEV KRYADELYVV YQALQNNDAA KLEEIFSLAR EVRSAWTQQ
//
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