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Database: UniProt
Entry: D1B761_THEAS
LinkDB: D1B761_THEAS
Original site: D1B761_THEAS 
ID   D1B761_THEAS            Unreviewed;       283 AA.
AC   D1B761;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Prephenate dehydrogenase {ECO:0000313|EMBL:ACZ19852.1};
GN   OrderedLocusNames=Taci_1638 {ECO:0000313|EMBL:ACZ19852.1};
OS   Thermanaerovibrio acidaminovorans (strain ATCC 49978 / DSM 6589 / Su883)
OS   (Selenomonas acidaminovorans).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Synergistaceae;
OC   Thermanaerovibrio.
OX   NCBI_TaxID=525903 {ECO:0000313|EMBL:ACZ19852.1, ECO:0000313|Proteomes:UP000002030};
RN   [1] {ECO:0000313|EMBL:ACZ19852.1, ECO:0000313|Proteomes:UP000002030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49978 / DSM 6589 / Su883
RC   {ECO:0000313|Proteomes:UP000002030};
RX   PubMed=21304665; DOI=10.4056/sigs.40645;
RA   Chovatia M., Sikorski J., Schroder M., Lapidus A., Nolan M., Tice H.,
RA   Glavina Del Rio T., Copeland A., Cheng J.F., Lucas S., Chen F., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chain P., Saunders E., Detter J.C., Brettin T., Rohde M.,
RA   Goker M., Spring S., Bristow J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Eisen J.A.;
RT   "Complete genome sequence of Thermanaerovibrio acidaminovorans type strain
RT   (Su883).";
RL   Stand. Genomic Sci. 1:254-261(2009).
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DR   EMBL; CP001818; ACZ19852.1; -; Genomic_DNA.
DR   RefSeq; WP_012870361.1; NC_013522.1.
DR   RefSeq; YP_003318134.1; NC_013522.1.
DR   AlphaFoldDB; D1B761; -.
DR   STRING; 525903.Taci_1638; -.
DR   EnsemblBacteria; ACZ19852; ACZ19852; Taci_1638.
DR   KEGG; tai:Taci_1638; -.
DR   PATRIC; fig|525903.6.peg.1628; -.
DR   eggNOG; COG0287; Bacteria.
DR   HOGENOM; CLU_055968_2_0_0; -.
DR   OrthoDB; 9802008at2; -.
DR   Proteomes; UP000002030; 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:UP000002030}.
FT   DOMAIN          5..283
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
SQ   SEQUENCE   283 AA;  29820 MW;  2754623E018A6C92 CRC64;
     MGAGRHVGIV GLGLMGGSMA MGLSSVPGVS VWGWDLDRGT LERARSMGIL DGAARDLGEL
     AERCHLVILA VPPWEVIPLA MELSPSFRGF VMDLSSVKGP LAFQLDRLFP GRYLGFHPMA
     GKETGGLESA SGDLFKGAVC VLVPGPSSGN EALALGRELA SWLGARWILL GPGEHDRAAA
     VVSHLPMLIS LGLMELARRR DQGGGAFGMA AGSFRDATRV SMSQPWLLAQ VLSMNRGSVK
     EVLGELCSIL GELASMDQGD LEALAGELGS LRRRLGEEKG WSC
//
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