PHEA_MYCUA
ID PHEA_MYCUA Reviewed; 315 AA.
AC A0PX17;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=MUL_5011;
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=362242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99;
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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 -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis;
CC phenylpyruvate from prephenate: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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DR EMBL; CP000325; ABL06886.1; -; Genomic_DNA.
DR RefSeq; WP_011742477.1; NC_008611.1.
DR AlphaFoldDB; A0PX17; -.
DR SMR; A0PX17; -.
DR STRING; 362242.MUL_5011; -.
DR EnsemblBacteria; ABL06886; ABL06886; MUL_5011.
DR KEGG; mul:MUL_5011; -.
DR eggNOG; COG0077; Bacteria.
DR HOGENOM; CLU_035008_0_0_11; -.
DR OMA; PLMIYRE; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000000765; 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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway.
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 Pfam; PF01842; ACT; 1.
DR Pfam; PF00800; PDT; 1.
DR PIRSF; PIRSF001500; Chor_mut_pdt_Ppr; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1.
DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Phenylalanine biosynthesis.
FT CHAIN 1..315
FT /note="Prephenate dehydratase"
FT /id="PRO_0000382044"
FT DOMAIN 3..189
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 203..280
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT SITE 182
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 315 AA; 32826 MW; 5378E728B3048CF5 CRC64;
MARIAYLGPE GTFTQAALLE IAAAGLVPGH DDGGAQPLPV DSTPAALDAV RTGAAEFACV
PIENSIDGSL APTLDSLAIG SPLQVFAETT LDVAFSIVVK PGVGAADVRT LAAFPVAAAQ
VRQWLTAHLP NVELHPAYSN ADGARQVAEG QVDAAVTSPL AAAHWALQSL ADGVVDESNA
RTRFLLIGVP GPPPPRTGTD RTSAVLRIAN VPGALLDALT EFGMRGIDLT RIESRPTRTG
LGTYMFFIDC VGHIADDAVA EALKALHRRC ADVRYLGSWP TGQTYAAQPP PADEAAIWLQ
QLREGKPEAS PEPPL
