ID E8NE25_MICTS Unreviewed; 320 AA.
AC E8NE25;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:BAJ75070.1};
GN OrderedLocusNames=MTES_2106 {ECO:0000313|EMBL:BAJ75070.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ75070.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ75070.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ75070.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) 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}.
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DR EMBL; AP012052; BAJ75070.1; -; Genomic_DNA.
DR RefSeq; WP_013585195.1; NC_015125.1.
DR AlphaFoldDB; E8NE25; -.
DR STRING; 979556.MTES_2106; -.
DR KEGG; mts:MTES_2106; -.
DR eggNOG; COG0077; Bacteria.
DR HOGENOM; CLU_035008_0_0_11; -.
DR OrthoDB; 9802281at2; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000008975; Chromosome.
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 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; 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};
KW Phenylalanine biosynthesis {ECO:0000256|ARBA:ARBA00023222}.
FT DOMAIN 13..193
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000259|PROSITE:PS51171"
FT DOMAIN 208..286
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT SITE 186
FT /note="Essential for prephenate dehydratase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001500-2"
SQ SEQUENCE 320 AA; 33965 MW; 944111FA74F892CC CRC64;
MLPDTDHTPA RRTYSYLGPA GTFTEAALAQ VPEARDQIWR PVRNVGEALA DVVEGRSDAA
MIAIENSVDG GVSTAQDALA TVPGLRIVGE YLVPVNFVLV ARPGATLSDV SLVAAHPVAY
GQCLKWLSEH VPAHAHLPAE SNVASALGVL DGTSAADAAI AAPGIVAHHD VAVLAENIGD
NPNAVTRFVL VSRTVAPAPP TGADKTSLIV ELPEDHPGAL LELLEQFATR GINLSLLASR
PIGDALGRYR FVIDADGHVL DERMADALLG LRRFSPKVIF LGSYARADRA IVRYPQRYSD
DVFVEARDWL RGLLSGEPEA
//
