ID   UBIC_CUPMC              Reviewed;         214 AA.
AC   Q1LIU6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 82.
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}; OrderedLocusNames=Rmet_3058;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABF09930.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000352; ABF09930.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029307163.1; NC_007973.1.
DR   AlphaFoldDB; Q1LIU6; -.
DR   SMR; Q1LIU6; -.
DR   STRING; 266264.Rmet_3058; -.
DR   EnsemblBacteria; ABF09930; ABF09930; Rmet_3058.
DR   KEGG; rme:Rmet_3058; -.
DR   eggNOG; COG3161; Bacteria.
DR   HOGENOM; CLU_096824_2_0_4; -.
DR   OrthoDB; 1274776at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000002429; 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; Reference proteome; Ubiquinone biosynthesis.
FT   CHAIN           1..214
FT                   /note="Probable chorismate pyruvate-lyase"
FT                   /id="PRO_0000255911"
FT   REGION          183..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         74
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ   SEQUENCE   214 AA;  24061 MW;  F1EC498766F0D862 CRC64;
     MQKLRAAWHA HLPYDASIPL NQRRWITGEG SLTARLMSAS AAFRVRRLAQ APQLPLADEW
     RALGLIRPLP AITREVLLIC DETPAVFAHT IVDPRYARRD WPFLRGLGNR PLGGALFVDP
     RVRRDPFQFA RLTPCHPLRQ ALQRVLPALS SEPMLPARRS VFRRGGGAML VTEVFLPDLL
     TRAAPENTGA GGTRLPRRID THHTPSKQEE RPES