ID   UBIC_SALPB              Reviewed;         165 AA.
AC   A9N1L2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Chorismate pyruvate-lyase {ECO:0000255|HAMAP-Rule:MF_01632};
DE            Short=CL {ECO:0000255|HAMAP-Rule:MF_01632};
DE            Short=CPL {ECO:0000255|HAMAP-Rule:MF_01632};
DE            EC=4.1.3.40 {ECO:0000255|HAMAP-Rule:MF_01632};
GN   Name=ubiC {ECO:0000255|HAMAP-Rule:MF_01632}; OrderedLocusNames=SPAB_05216;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Removes the pyruvyl group from chorismate, with concomitant
CC       aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the
CC       ubiquinone pathway. {ECO:0000255|HAMAP-Rule:MF_01632}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01632};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01632}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01632}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01632}.
CC   -!- SIMILARITY: Belongs to the UbiC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01632}.
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DR   EMBL; CP000886; ABX70493.1; -; Genomic_DNA.
DR   RefSeq; WP_000019230.1; NC_010102.1.
DR   AlphaFoldDB; A9N1L2; -.
DR   SMR; A9N1L2; -.
DR   KEGG; spq:SPAB_05216; -.
DR   PATRIC; fig|1016998.12.peg.4885; -.
DR   HOGENOM; CLU_096824_1_0_6; -.
DR   OMA; ELWGRRS; -.
DR   BioCyc; SENT1016998:SPAB_RS21240-MON; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000008556; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008813; F:chorismate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042866; P:pyruvate biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1410.10; -; 1.
DR   HAMAP; MF_01632; UbiC; 1.
DR   InterPro; IPR007440; Chorismate--pyruvate_lyase.
DR   InterPro; IPR028978; Chorismate_lyase_/UTRA_dom_sf.
DR   PANTHER; PTHR38683; PTHR38683; 1.
DR   Pfam; PF04345; Chor_lyase; 1.
DR   SUPFAM; SSF64288; SSF64288; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Lyase; Pyruvate; Ubiquinone biosynthesis.
FT   CHAIN           1..165
FT                   /note="Chorismate pyruvate-lyase"
FT                   /id="PRO_1000088147"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         77
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ   SEQUENCE   165 AA;  18748 MW;  1A4A5AEC3BC149CE CRC64;
     MSHPALTRLR ALRYFDAIPA LEPHLLDWLL LEDSMTKRFE QQGKRVSVTL IREAFVGQSE
     VEEASGLLPS ESRYWLREIL LCADGEPWLA GRTVVPESTL CGPEQVLQHL GKTPLGRYLF
     TSSTLTRDFI EIGRDATLWG RRSRLRLSGK PLLLTELFLP ASPLY