ID A0A0A5G9V1_9BACI Unreviewed; 366 AA.
AC A0A0A5G9V1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=N784_12745 {ECO:0000313|EMBL:KGX87958.1};
OS Pontibacillus litoralis JSM 072002.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX87958.1, ECO:0000313|Proteomes:UP000030401};
RN [1] {ECO:0000313|EMBL:KGX87958.1, ECO:0000313|Proteomes:UP000030401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX87958.1,
RC ECO:0000313|Proteomes:UP000030401};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGX87958.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AVPG01000004; KGX87958.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A5G9V1; -.
DR STRING; 1385512.N784_12745; -.
DR eggNOG; COG0287; Bacteria.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000030401; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000030401};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 1..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; 41452 MW; 2EDCAFAC96A05BD9 CRC64;
MNTTILVSGL GLIGGSIALN LMKHPNVHVI GYDQNQDTRN YAYHNRFIHQ AVDSFNKGVQ
LADIVMLAMP VQGCIQAIQE MNEMQLDRAK LVTDVASVKK PILDAAAQWT NEQLRFVGGH
PMAGSHKQGI IAAKAHLFEN AYYLFVPGIR STEQDVSQLQ HLLRETKSHY VTVDKREHDQ
MTGVISHFPH LIASSLVHQA KKWQRVYPFT HELAAGGFRD ITRIASSHPK MWNDILIQNK
ESIIPLLNDW IQEMNELKQF VEGNNHEQLH QYLKEAKVFR DDLPTKNKGA IPAFYDVFVD
IKDQPGALSE VTHILAMANI SIVNIRILEV REGITGALRL SFQTEADKNQ CQYVLKRSGY
DVMIQE
//
