ID A0A0G1T7Z4_9BACT Unreviewed; 559 AA.
AC A0A0G1T7Z4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=UY03_C0007G0018 {ECO:0000313|EMBL:KKU77867.1};
OS Parcubacteria group bacterium GW2011_GWA2_47_64.
OC Bacteria.
OX NCBI_TaxID=1618845 {ECO:0000313|EMBL:KKU77867.1, ECO:0000313|Proteomes:UP000034132};
RN [1] {ECO:0000313|EMBL:KKU77867.1, ECO:0000313|Proteomes:UP000034132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU77867.1}.
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DR EMBL; LCOL01000007; KKU77867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1T7Z4; -.
DR UniPathway; UPA00121; UER00345.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000034132; Unassembled WGS sequence.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
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:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR001086; Preph_deHydtase.
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 Pfam; PF00800; PDT; 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 SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51176; PDH_ADH; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 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 3..194
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 201..467
FT /note="Prephenate/arogenate dehydrogenase"
FT /evidence="ECO:0000259|PROSITE:PS51176"
FT DOMAIN 486..559
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 559 AA; 62150 MW; A5F42E24FD617B19 CRC64;
MKKKILVLDA FTNGHEAARD FAQRQGWSEM DCEIVFCGTH PNVFKRLTEG PAYAVVPIRN
SIAGEVTEVT KHLAGFRETG YDLQERDRLD LQINHYLLAP QHVGRAEELE RVMSHEKAIQ
QCGKYLDSIG ITPDRRSRRD STGNAAKAVA KLGPNVKIGA IAPKAAAEEY GLKILAEGIQ
DVPDNKTTFV LLQNEATVRQ VVVGIIGING RFGQMLKGFF DQLGCSVIGS DKKKPTGLSN
IQVVERADVV IFSILPIEDT PAAIRSVLPY TREDRLLMDV TSVKGPTVDA MLESKSQVIG
LHPMSAPEVG FDGQTVVACP VRLTLPHWKT WAVNMLAATG AKIKWSTPSA HDGYMLYVQG
NPQFGNLASA LLIAESEVSV SESLEFTSPF YGIMFALMGR LLNGDPRLYA SILMENPQTL
TMLERRVEIE QRLIELIRKK DRKAFDELFV KTRGYFGLQV IKDANELFMR LIGVLKTLYG
KNSVTLEFGK AQSRPGLLER ISRVFSQQQI NLTGINSVAL DGQRLQFTLS FEQSRASDEV
RRALEEIEDW SEPKVKVLD
//
