ID D6XUY8_BACIE Unreviewed; 366 AA.
AC D6XUY8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN OrderedLocusNames=Bsel_2120 {ECO:0000313|EMBL:ADH99624.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99624.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH99624.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001791; ADH99624.1; -; Genomic_DNA.
DR RefSeq; WP_013173046.1; NC_014219.1.
DR AlphaFoldDB; D6XUY8; -.
DR STRING; 439292.Bsel_2120; -.
DR KEGG; bse:Bsel_2120; -.
DR eggNOG; COG0287; Bacteria.
DR HOGENOM; CLU_055968_2_1_9; -.
DR OrthoDB; 9802008at2; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000000271; 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 CDD; cd04909; ACT_PDH-BS; 1.
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 ECO:0000313|EMBL:ADH99624.1};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 2..291
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 296..366
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 366 AA; 39953 MW; E44769B4C7A32BA1 CRC64;
MKRVSIIGLG LIGGSLALAI RKGQPNIVIT GYDKDPSTMK LAKSLQVIDE AAASAADAAL
NSDVIILATP VATALSLIDE LAGLPLKEGV IVTDVGSTKQ SIVKKAKKLT DLGIVFIGGH
PMAGSHKTGV EASNDRLFEN AFYVLSPNGQ QNDSERIKLQ NLLKGTRAKF IELPAEEHDR
FAGLISHLPH MIASGLVHQL AEEESHHPIV SQLAAGGFRD LTRIASASPD MWRDILMHNR
DILMKLLHDW KEQVNVMEEM LKEGDPEMIH QFFAKAKESR DQLPARKKGA MLPFYDLFVD
VPDHPGVISD VTAILARAGI SITNIQIIEA RNDMLGVLRL SFRSGEDLEL AQAKLAEHLY
DTYEAP
//