ID G2GCG9_9ACTN Unreviewed; 361 AA.
AC G2GCG9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Prephenate dehydrogenase {ECO:0000256|ARBA:ARBA00016891};
DE EC=1.3.1.12 {ECO:0000256|ARBA:ARBA00012068};
GN ORFNames=SZN_15968 {ECO:0000313|EMBL:EGX58772.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX58772.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX58772.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX58772.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) 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:EGX58772.1}.
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; AGBF01000045; EGX58772.1; -; Genomic_DNA.
DR RefSeq; WP_007496095.1; NZ_AGBF01000045.1.
DR AlphaFoldDB; G2GCG9; -.
DR PATRIC; fig|700597.3.peg.3128; -.
DR OrthoDB; 9802008at2; -.
DR UniPathway; UPA00122; UER00961.
DR Proteomes; UP000004217; 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:EGX58772.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004217};
KW Tyrosine biosynthesis {ECO:0000256|ARBA:ARBA00022498}.
FT DOMAIN 2..283
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; 37910 MW; A6A80728144986B1 CRC64;
MRTALVIGTG LIGTSAALAL SQRGVAVHLA DHDPEQARTA AALGAGTDDA PDGPVDLAIV
AAPPAHVAAV LADAVRRGAA RGYLDVASVK GGPRRELEAL GLDLSPYIGT HPMAGREKSG
PLAATGDLFE GRPWVLTPTR DTDTEVLNLA LELVSHCRAV PVVMDADAHD RAVALVSHMP
HLLSSLVAAR LENAEEAAVR LCGQGIRDVT RIAASDPGMW IDILSANPGP VADLLTDVAA
DLEETVRSLR SLQSQHEDER REGTSGIEDV LRRGNAGQVR VPGKHGAAPR RYEVVAVLID
DQPGQLARIF ADAGRAGVNI EDVRIEHATG QQAGLVQLMV EPKAAPVLSA SLRERGWAIR
Q
//
