ID D5WQ09_KYRT2 Unreviewed; 372 AA.
AC D5WQ09;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN OrderedLocusNames=Btus_1716 {ECO:0000313|EMBL:ADG06418.1};
OS Kyrpidia tusciae (strain DSM 2912 / NBRC 15312 / T2) (Bacillus tusciae).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae; Kyrpidia.
OX NCBI_TaxID=562970 {ECO:0000313|EMBL:ADG06418.1, ECO:0000313|Proteomes:UP000002368};
RN [1] {ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Pukall R., Schneider S., Wahrenburg C., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacillus tusciae DSM 2912.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG06418.1, ECO:0000313|Proteomes:UP000002368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2912 / NBRC 15312 / T2 {ECO:0000313|Proteomes:UP000002368};
RX PubMed=22180816; DOI=10.4056/sigs.2144922;
RA Klenk H.P., Lapidus A., Chertkov O., Copeland A., Del Rio T.G., Nolan M.,
RA Lucas S., Chen F., Tice H., Cheng J.F., Han C., Bruce D., Goodwin L.,
RA Pitluck S., Pati A., Ivanova N., Mavromatis K., Daum C., Chen A.,
RA Palaniappan K., Chang Y.J., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Rohde M., Abt B., Pukall R., Goker M., Bristow J., Markowitz V.,
RA Hugenholtz P., Eisen J.A.;
RT "Complete genome sequence of the thermophilic, hydrogen-oxidizing Bacillus
RT tusciae type strain (T2) and reclassification in the new genus, Kyrpidia
RT gen. nov. as Kyrpidia tusciae comb. nov. and emendation of the family
RT Alicyclobacillaceae da Costa and Rainey, 2010.";
RL Stand. Genomic Sci. 5:121-134(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 +
CC NADH; Xref=Rhea:RHEA:13869, ChEBI:CHEBI:16526, ChEBI:CHEBI:29934,
CC ChEBI:CHEBI:36242, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001162};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-
CC hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005067}.
CC -!- SIMILARITY: Belongs to the prephenate/arogenate dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007964}.
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DR EMBL; CP002017; ADG06418.1; -; Genomic_DNA.
DR RefSeq; WP_013075705.1; NC_014098.1.
DR AlphaFoldDB; D5WQ09; -.
DR STRING; 562970.Btus_1716; -.
DR KEGG; bts:Btus_1716; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_1_9; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000002368; 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:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.260; -; 1.
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; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
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; PF01842; ACT; 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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 9..297
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 302..372
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 372 AA; 40261 MW; 7A04E4E624FA187D CRC64;
MTDKGPALHR IAVVGCGLIG GSLALAWQRA GVAREIVGVD VSAEHLEIAL EIGAIDRALP
LRSAVQEADL VVLAAPVKES MALLREIAAF HPAAGTLITD VGSTKRAICR EATRVLPEGV
SFIGGHPMAG SEKSGIRAAS PRLYENAVYV LTPTPGEKPE MIQRIRDLVQ AAGAQVLILD
PDHHDRLVAA VSHLPHVVAA QLVHQVAELG EDDPLYAVLA AGGFRDVTRI ASGHPVMWRD
ILLTNGDRLR PLFERWKDQI EELLGWINRR DGEALETFFR QAARWRDALP VRGRGAIRPA
FQCTVDVPDQ PGIIGTVATL LGEAGINLRN IAILESREDE DGQLSLTFDT EDGRDQAARL
LADHGFKVDP RM
//
