ID   UBIC_XANAL              Reviewed;         202 AA.
AC   Q70C33;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Probable 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};
OS   Xanthomonas albilineans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=29447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Xa23R1;
RX   PubMed=15077674; DOI=10.1094/mpmi.2004.17.4.414;
RA   Royer M., Costet L., Vivien E., Bes M., Cousin A., Damais A., Pieretti I.,
RA   Savin A., Megessier S., Viard M., Frutos R., Gabriel D.W., Rott P.C.;
RT   "Albicidin pathotoxin produced by Xanthomonas albilineans is encoded by
RT   three large PKS and NRPS genes present in a gene cluster also containing
RT   several putative modifying, regulatory, and resistance genes.";
RL   Mol. Plant Microbe Interact. 17:414-427(2004).
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   -!- 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; AJ586576; CAE52333.1; -; Genomic_DNA.
DR   RefSeq; WP_052687933.1; NZ_MDCB01000001.1.
DR   AlphaFoldDB; Q70C33; -.
DR   SMR; Q70C33; -.
DR   UniPathway; UPA00232; -.
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..202
FT                   /note="Probable chorismate pyruvate-lyase"
FT                   /id="PRO_0000240585"
FT   REGION          181..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ   SEQUENCE   202 AA;  22557 MW;  439C97E71D57DFDC CRC64;
     MHPPSPLNTQ QKDWLTRGGS LTAHLRLLGQ VQVQVQREHK AMAWLDEYRV LGLSRCLLVW
     VREVVLVVDA KPYVYARSLT PLTASYNAWQ AVRSIGSRPL ADLLFRDRSV LRSALASRRI
     TAQHPLHRRA CNFVAQSHAT QALLARRSVF TRQGAPLLIT ECMLPALWAT LEPVAAPRQA
     SLSADGPCRH SAQIVSPESM LE