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Database: UniProt
Entry: A0A3M2LWJ6_9ACTN
LinkDB: A0A3M2LWJ6_9ACTN
Original site: A0A3M2LWJ6_9ACTN 
ID   A0A3M2LWJ6_9ACTN        Unreviewed;       311 AA.
AC   A0A3M2LWJ6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Prephenate dehydratase {ECO:0000256|ARBA:ARBA00021872};
DE            EC=4.2.1.51 {ECO:0000256|ARBA:ARBA00013147};
GN   Name=pheA {ECO:0000313|EMBL:RMI41914.1};
GN   ORFNames=EBO15_21630 {ECO:0000313|EMBL:RMI41914.1};
OS   Actinomadura harenae.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Actinomadura.
OX   NCBI_TaxID=2483351 {ECO:0000313|EMBL:RMI41914.1, ECO:0000313|Proteomes:UP000282674};
RN   [1] {ECO:0000313|EMBL:RMI41914.1, ECO:0000313|Proteomes:UP000282674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-Ht49 {ECO:0000313|EMBL:RMI41914.1,
RC   ECO:0000313|Proteomes:UP000282674};
RA   Hu J.;
RT   "Isolation from soil.";
RL   Submitted (OCT-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   -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC       phenylpyruvate from prephenate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004741}.
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:RMI41914.1}.
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DR   EMBL; RFFG01000038; RMI41914.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M2LWJ6; -.
DR   OrthoDB; 9802281at2; -.
DR   UniPathway; UPA00121; UER00345.
DR   Proteomes; UP000282674; Unassembled WGS sequence.
DR   GO; GO:0004106; F:chorismate mutase activity; IEA:InterPro.
DR   GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC.
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; PS00857; PREPHENATE_DEHYDR_1; 1.
DR   PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:RMI41914.1};
KW   Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282674}.
FT   DOMAIN          6..184
FT                   /note="Prephenate dehydratase"
FT                   /evidence="ECO:0000259|PROSITE:PS51171"
FT   DOMAIN          199..274
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   SITE            177
FT                   /note="Essential for prephenate dehydratase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ   SEQUENCE   311 AA;  33488 MW;  8EB953EA14B9436F CRC64;
     MPEPRKWAYL GPQGTFTEAA LRSFPGAIGA EHVPFATVPA ALDALRSGEA DGAVVALENS
     VEGSVPTTLD ELATGDPVQI VGEVHLPVSF ALLVRPGTAI EDVKTVASHP HAQPQCRRWL
     AANVPDAEWR AATSNAEAAQ HVADGHYDAA LAGSFAAARY GLDVLAEDIH DVSDAVTRFI
     ALRRPCSPPT PTGMDRTSVV AFLDEDHPGA LLEILTEFSV RGINLSLIQS RPTGQGLGSY
     LFWMDFEGHV FESRVGEALM GLRRICSDVR FLGSYTRADK IRPDIRRGTH DHDFTEAAAW
     LATIRCGATE R
//
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