UBIC_YERPG
ID UBIC_YERPG Reviewed; 174 AA.
AC A9QYL0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
GN OrderedLocusNames=YpAngola_A0678;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(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 -!- 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; CP000901; ABX86341.1; -; Genomic_DNA.
DR RefSeq; WP_002209087.1; NZ_CP009935.1.
DR AlphaFoldDB; A9QYL0; -.
DR SMR; A9QYL0; -.
DR GeneID; 66843219; -.
DR KEGG; ypg:YpAngola_A0678; -.
DR PATRIC; fig|349746.12.peg.1625; -.
DR OMA; ELWGRRS; -.
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..174
FT /note="Chorismate pyruvate-lyase"
FT /id="PRO_1000186542"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ SEQUENCE 174 AA; 19916 MW; 51A02866228B3ED2 CRC64;
MFIGDASILK PIQWCATEHP ELPADIADWL MELGSMTRRF EQHCQRVHVE PQRECFITRD
ALGEEAEHLP VSQRYWLREI VLFGDNVPWL LGRTVIPEET LSGPDRALVD LGTLPLGRYL
FSGDALTRDY IHVGRQDNLW ARRSLLRLSG NPLLLTEVFL PASPLYTHCD SIPK
