PHEA_MYCLB
ID PHEA_MYCLB Reviewed; 322 AA.
AC B8ZTU2;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Prephenate dehydratase;
DE Short=PDT;
DE EC=4.2.1.51;
GN Name=pheA; OrderedLocusNames=MLBr00078;
OS Mycobacterium leprae (strain Br4923).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=561304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Br4923;
RX PubMed=19881526; DOI=10.1038/ng.477;
RA Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A.,
RA Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C.,
RA Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H.,
RA Vera-Cabrera L., Stefani M.M., Banu S., Macdonald M., Sapkota B.R.,
RA Spencer J.S., Thomas J., Harshman K., Singh P., Busso P., Gattiker A.,
RA Rougemont J., Brennan P.J., Cole S.T.;
RT "Comparative genomic and phylogeographic analysis of Mycobacterium
RT leprae.";
RL Nat. Genet. 41:1282-1289(2009).
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; FM211192; CAR70171.1; -; Genomic_DNA.
DR RefSeq; WP_010907508.1; NC_011896.1.
DR AlphaFoldDB; B8ZTU2; -.
DR SMR; B8ZTU2; -.
DR EnsemblBacteria; CAR70171; CAR70171; MLBr00078.
DR KEGG; mlb:MLBr00078; -.
DR HOGENOM; CLU_035008_0_0_11; -.
DR OMA; PLMIYRE; -.
DR UniPathway; UPA00121; UER00345.
DR Proteomes; UP000006900; 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..322
FT /note="Prephenate dehydratase"
FT /id="PRO_0000382036"
FT DOMAIN 5..191
FT /note="Prephenate dehydratase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00517"
FT DOMAIN 205..282
FT /note="ACT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01007"
FT REGION 286..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 184
FT /note="Essential for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 33549 MW; 85C7FBB5866B8524 CRC64;
MSVARIAYLG PEGTFTEAAL LRMTAAGLVP DTGPDGLRRW PTESTPAALD AVRGGAADYA
CVPIENSIDG SVAPTLDNLA IGSPLQVFAE TTLDVEFNIV VKPGITAADI RTLAAFPVAA
AQVRQWLAAH LAGAELRPAY SNADAARQVA YGQVDAAVTS PLAATRWGLI ALAAGIVDEP
NARTRFVLVG MPGPPPARTG TDRTSAVLRI DNAPGMLVAA LAEFGIRGID LTRIESRPTR
TELGTYLFFV DCVGHIDDGV VAEALKALHR RCADVCYLGS WPAGLATGPT VSPPPPDEAS
RWLARLRAGK PDQASEPGGG KL
