ID   PHBS_MYCLE              Reviewed;         210 AA.
AC   Q9CD83;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Chorismate pyruvate-lyase;
DE            EC=4.1.3.40;
DE   AltName: Full=4-HB synthase;
DE   AltName: Full=p-hydroxybenzoic acid synthase;
GN   OrderedLocusNames=ML0133;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Removes the pyruvyl group from chorismate to provide 4-
CC       hydroxybenzoate (4HB). Involved in the synthesis of glycosylated p-
CC       hydroxybenzoic acid methyl esters (p-HBADs) and phenolic glycolipids
CC       (PGL) that play important roles in the pathogenesis of mycobacterial
CC       infections (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate = 4-hydroxybenzoate + pyruvate;
CC         Xref=Rhea:RHEA:16505, ChEBI:CHEBI:15361, ChEBI:CHEBI:17879,
CC         ChEBI:CHEBI:29748; EC=4.1.3.40;
CC   -!- SIMILARITY: Belongs to the chorismate pyruvate-lyase type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AL583917; CAC29641.1; -; Genomic_DNA.
DR   PIR; E86925; E86925.
DR   RefSeq; NP_301227.1; NC_002677.1.
DR   RefSeq; WP_010907552.1; NC_002677.1.
DR   AlphaFoldDB; Q9CD83; -.
DR   SMR; Q9CD83; -.
DR   STRING; 272631.ML0133; -.
DR   EnsemblBacteria; CAC29641; CAC29641; CAC29641.
DR   KEGG; mle:ML0133; -.
DR   PATRIC; fig|272631.5.peg.201; -.
DR   Leproma; ML0133; -.
DR   eggNOG; COG3161; Bacteria.
DR   HOGENOM; CLU_107938_1_0_11; -.
DR   OMA; VIIITEY; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0008813; F:chorismate lyase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1410.10; -; 1.
DR   InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR   InterPro; IPR002800; Rv2949c-like.
DR   Pfam; PF01947; DUF98; 1.
DR   SUPFAM; SSF64288; SSF64288; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..210
FT                   /note="Chorismate pyruvate-lyase"
FT                   /id="PRO_0000240509"
SQ   SEQUENCE   210 AA;  24045 MW;  5C04B469DB61DA3F CRC64;
     MTNRTLSREE IRKLDRDLRI LVATNGTLTR VLNVVANEEI VVDIINQQLL DVAPKIPELE
     NLKIGRILQR DILLKGQKSG ILFVAAESLI VIDLLPTAIT TYLTKTHHPI GEIMAASRIE
     TYKEDAQVWI GDLPCWLADY GYWDLPKRAV GRRYRIIAGG QPVIITTEYF LRSVFQDTPR
     EELDRCQYSN DIDTRSGDRF VLHGRVFKNL