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Database: UniProt
Entry: A0A553ZZR9_9BACI
LinkDB: A0A553ZZR9_9BACI
Original site: A0A553ZZR9_9BACI 
ID   A0A553ZZR9_9BACI        Unreviewed;       364 AA.
AC   A0A553ZZR9;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE            EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN   ORFNames=FN960_07840 {ECO:0000313|EMBL:TSB46923.1};
OS   Alkalicoccobacillus porphyridii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccobacillus.
OX   NCBI_TaxID=2597270 {ECO:0000313|EMBL:TSB46923.1, ECO:0000313|Proteomes:UP000318521};
RN   [1] {ECO:0000313|EMBL:TSB46923.1, ECO:0000313|Proteomes:UP000318521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P16(2019) {ECO:0000313|Proteomes:UP000318521};
RA   Park Y.J., Jeong S.E., Jung H.S.;
RL   Submitted (JUL-2019) 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:TSB46923.1}.
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DR   EMBL; VLXZ01000004; TSB46923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A553ZZR9; -.
DR   OrthoDB; 9802008at2; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000318521; 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   ECO:0000313|EMBL:TSB46923.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000318521};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT   DOMAIN          3..290
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   DOMAIN          295..364
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   364 AA;  40564 MW;  AF2A7C85EEA18C0E CRC64;
     MKKEVLIVGL GLIGGSIALG IRKEHDVRIT GFDINEEQLR MAISLGVIDE KAGSLEDAVK
     NSDLIILAVP VAAAESLLES MKNYSFKPGA LMTDVGSTKN EICKRAKELS HKVTFIGGHP
     MAGSHKSGIT AAKVHLFENA FYVLTPDAEI QSQQIDTLKQ WLKGTSATFL EMSPKEHDEV
     TGAISHFPHI IAASLVHHVE AEEHRDANVT RLAAGGFRDI TRIASSSPEM WRDILLHNQQ
     SLLRLLNSWD REMQRVRVLL EEKNHGGILE YFQRAKDFRE GLPQRKKGAI PAFYDLYVDV
     PDHPGAISDV TSILAEAEIS LTNIRILETR EDIMGVLRLS FRSEEDRDQA KQQLGLHTFE
     SYIL
//
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