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Database: UniProt
Entry: A0A384HXZ9_9ACTN
LinkDB: A0A384HXZ9_9ACTN
Original site: A0A384HXZ9_9ACTN 
ID   A0A384HXZ9_9ACTN        Unreviewed;       361 AA.
AC   A0A384HXZ9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-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=DNK56_11895 {ECO:0000313|EMBL:PZT82695.1};
OS   Streptomyces sp. AC1-42W.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2218666 {ECO:0000313|EMBL:PZT82695.1, ECO:0000313|Proteomes:UP000249154};
RN   [1] {ECO:0000313|EMBL:PZT82695.1, ECO:0000313|Proteomes:UP000249154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC1-42W {ECO:0000313|EMBL:PZT82695.1,
RC   ECO:0000313|Proteomes:UP000249154};
RA   De Leon M.P., Montecillo A.D., Siringan M.A.T., Kim S.-G., Rosana A.R.R.;
RT   "Near complete genome sequences of Streptomyces sp. strains AC1-42W
RT   isolated from bat guano of Cabalyorisa Cave, Pangasinan, Philippines.";
RL   Submitted (JUN-2018) 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:PZT82695.1}.
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DR   EMBL; QKWY01000001; PZT82695.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A384HXZ9; -.
DR   UniPathway; UPA00122; UER00961.
DR   Proteomes; UP000249154; 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   ECO:0000313|EMBL:PZT82695.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249154};
KW   Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT   DOMAIN          2..279
FT                   /note="Prephenate/arogenate dehydrogenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51176"
FT   DOMAIN          294..361
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   361 AA;  37232 MW;  F90740F399D95D44 CRC64;
     MRSAVVIGTG LVGTSAALAL ASRGIAVHLV DHDPESARTA AALGAGTDTP PEDRVDLAVV
     AVPPAHTAAV LAAAMRDGVA RGYLDVASVK GGPRRELEAL GADLTAYIGT HPMAGKERSG
     PLAATADLFE GRPWVLTPTP DTDTEVLNLA LELVALCRAV PVVMDADAHD RAVALVSHTP
     QLISSMVAAR LEHADETAVR LCGQGIRDVT RIAASDPRMW VEILAANPGP VADVLAGVAA
     DLTETVTALR GLQSADEDER RAGTEGIRSV LSRGNAGRVR VPGKHGAAPA SYEVVAVLIS
     DRPGELAGIF ADAGRSGINI EDVRIEHATG QQAGLVQLMV EPSAAPALAA ALRERGWSLR
     Q
//
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