ID   PHBS_MYCTU              Reviewed;         199 AA.
AC   P9WIC5; L0TDV5; O86325; Q7D6D8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
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=Rv2949c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RC   STRAIN=Mt103;
RX   PubMed=16210318; DOI=10.1074/jbc.m508332200;
RA   Stadthagen G., Kordulakova J., Griffin R., Constant P., Bottova I.,
RA   Barilone N., Gicquel B., Daffe M., Jackson M.;
RT   "p-Hydroxybenzoic acid synthesis in Mycobacterium tuberculosis.";
RL   J. Biol. Chem. 280:40699-40706(2005).
RN   [3]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {ECO:0000269|PubMed:16210318}.
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         Evidence={ECO:0000269|PubMed:16210318};
CC   -!- ACTIVITY REGULATION: Inhibited by 4-hydroxybenzoate, but not by
CC       puruvate. {ECO:0000269|PubMed:16210318}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=19.7 uM for chorismate {ECO:0000269|PubMed:16210318};
CC         Vmax=0.048 umol/min/mg enzyme toward chorismate
CC         {ECO:0000269|PubMed:16210318};
CC       pH dependence:
CC         Optimum pH is 7.5. Active from pH 6.8 to 10.
CC         {ECO:0000269|PubMed:16210318};
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the chorismate pyruvate-lyase type 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP45753.1; -; Genomic_DNA.
DR   PIR; B70669; B70669.
DR   RefSeq; NP_217465.1; NC_000962.3.
DR   RefSeq; WP_003414887.1; NZ_NVQJ01000015.1.
DR   AlphaFoldDB; P9WIC5; -.
DR   SMR; P9WIC5; -.
DR   STRING; 83332.Rv2949c; -.
DR   PaxDb; P9WIC5; -.
DR   PRIDE; P9WIC5; -.
DR   DNASU; 887206; -.
DR   GeneID; 45426934; -.
DR   GeneID; 887206; -.
DR   KEGG; mtu:Rv2949c; -.
DR   TubercuList; Rv2949c; -.
DR   eggNOG; COG3161; Bacteria.
DR   OMA; VIIITEY; -.
DR   PhylomeDB; P9WIC5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0008813; F:chorismate lyase activity; IDA:MTBBASE.
DR   GO; GO:0046417; P:chorismate metabolic process; IMP:MTBBASE.
DR   GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IMP:MTBBASE.
DR   GO; GO:0072330; P:monocarboxylic acid biosynthetic process; IMP:MTBBASE.
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   1: Evidence at protein level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..199
FT                   /note="Chorismate pyruvate-lyase"
FT                   /id="PRO_0000240510"
SQ   SEQUENCE   199 AA;  22587 MW;  889D7554EA82A18B CRC64;
     MTECFLSDQE IRKLNRDLRI LIAANGTLTR VLNIVADDEV IVQIVKQRIH DVSPKLSEFE
     QLGQVGVGRV LQRYIILKGR NSEHLFVAAE SLIAIDRLPA AIITRLTQTN DPLGEVMAAS
     HIETFKEEAK VWVGDLPGWL ALHGYQNSRK RAVARRYRVI SGGQPIMVVT EHFLRSVFRD
     APHEEPDRWQ FSNAITLAR