ID A0A366DR46_9NOCA Unreviewed; 326 AA.
AC A0A366DR46;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872, ECO:0000256|RuleBase:RU361254};
DE Short=PDT {ECO:0000256|RuleBase:RU361254};
DE EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147, ECO:0000256|RuleBase:RU361254};
GN Name=pheA {ECO:0000256|RuleBase:RU361254};
GN ORFNames=DFR74_104462 {ECO:0000313|EMBL:RBO91754.1};
OS Nocardia puris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=208602 {ECO:0000313|EMBL:RBO91754.1, ECO:0000313|Proteomes:UP000252586};
RN [1] {ECO:0000313|EMBL:RBO91754.1, ECO:0000313|Proteomes:UP000252586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44599 {ECO:0000313|EMBL:RBO91754.1,
RC ECO:0000313|Proteomes:UP000252586};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O;
CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00000913,
CC ECO:0000256|RuleBase:RU361254};
CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004741, ECO:0000256|RuleBase:RU361254}.
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:RBO91754.1}.
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DR EMBL; QNRE01000004; RBO91754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366DR46; -.
DR STRING; 1210090.GCA_001613185_03460; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000252586; Unassembled WGS sequence.
DR GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04905; ACT_CM-PDT; 1.
DR CDD; cd13632; PBP2_Aa-PDT_like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR008242; Chor_mutase/pphenate_deHydtase.
DR InterPro; IPR001086; Preph_deHydtase.
DR InterPro; IPR018528; Preph_deHydtase_CS.
DR PANTHER; PTHR21022; PREPHENATE DEHYDRATASE P PROTEIN; 1.
DR PANTHER; PTHR21022:SF19; PREPHENATE DEHYDRATASE-RELATED; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF00800; PDT; 1.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU361254};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU361254};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361254};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222,
KW ECO:0000256|RuleBase:RU361254};
KW Reference proteome {ECO:0000313|Proteomes:UP000252586}.
FT DOMAIN 25..207
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 221..295
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 200
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 326 AA; 33925 MW; 0A92058B380FF311 CRC64;
MNSRVGRGDV GSPLGGACNV VGVPRIAYFG PSGTFTEMAL ADLENSGTFD GPVERVPAPS
QGAALDLIRS GEVEGAVVPI ESSVEGSISA TLDSLALGPR LQIVAETELE VTFTIVARPG
TTLADVRSLA AYPVAAAQVR MWVARNLPEA RPYTSASNAA AAEDVAAGHA DAAVSTALAG
ERLGLTALAV GVADHDQAVT RFVLVTRPRV APAATGSDRT SIVLELPNEP GSLMRAFAEF
ATRGIDLTRI ESRPTRTGLG TYRFYLDCVG HIDDAAVAEA LKALHRTARI RFLGSWPATS
ATGTPPPSDE EAAQWLTQLR KGVADL
//