ID A0A0U1QPK7_9BACL Unreviewed; 370 AA.
AC A0A0U1QPK7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=SINU_06440 {ECO:0000313|EMBL:KLI02739.1};
OS Sporolactobacillus inulinus CASD.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI02739.1, ECO:0000313|Proteomes:UP000035553};
RN [1] {ECO:0000313|EMBL:KLI02739.1, ECO:0000313|Proteomes:UP000035553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CASD {ECO:0000313|EMBL:KLI02739.1,
RC ECO:0000313|Proteomes:UP000035553};
RX PubMed=21952540; DOI=10.1128/JB.05934-11;
RA Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT efficient D-lactic acid-producing bacterium with high-concentration lactate
RT tolerance capability.";
RL J. Bacteriol. 193:5864-5865(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}.
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:KLI02739.1}.
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DR EMBL; AFVQ02000080; KLI02739.1; -; Genomic_DNA.
DR RefSeq; WP_010025187.1; NZ_AFVQ02000080.1.
DR AlphaFoldDB; A0A0U1QPK7; -.
DR STRING; 1069536.SINU_06440; -.
DR OrthoDB; 9802008at2; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000035553; 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 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; 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:UP000035553};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 1..294
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 299..370
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 370 AA; 40961 MW; 2D662E7323E45D24 CRC64;
MKTILIDGLG LIGGSIALAI RKKWPDDRIV AVDVSPAVLE HAKRSGIIDE GSLQLNAVAA
DADVIVLSAP VGIIIDHIKT LAELSLKPEV IVTDVGSTKQ EIVKHAQKLT EKKVIFIGGH
PMAGWHKTTI SAARADLFQS AYYFLIDDTL IDERHKAAAR ALQGLLSELD VKWLTVSASR
HDRIVAQISH LPHILASGLV NMSQNEFQSS PLSLKLAAGG FKSITRIASS DPTMWTDILL
SNRETLIDKI NRFHQYLERV RQALAASDRE SIRTFFEKAK VTRDNLNEQT GAHAPNFYDL
FLDLPDRIGS LARVTRILEN AKINLVNIHI LEIREDVAGV LQLSFSNQED RLLAKRELNR
HGLPTIRGDQ
//
