UBIC_PARXL
ID UBIC_PARXL Reviewed; 227 AA.
AC Q142T1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Bxeno_A1120;
GN ORFNames=Bxe_A3325;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE29658.1; -; Genomic_DNA.
DR RefSeq; WP_011487393.1; NZ_CP008760.1.
DR AlphaFoldDB; Q142T1; -.
DR SMR; Q142T1; -.
DR STRING; 266265.Bxe_A3325; -.
DR EnsemblBacteria; ABE29658; ABE29658; Bxe_A3325.
DR KEGG; bxb:DR64_1025; -.
DR KEGG; bxe:Bxe_A3325; -.
DR PATRIC; fig|266265.5.peg.1152; -.
DR eggNOG; COG3161; Bacteria.
DR OMA; ELWGRRS; -.
DR OrthoDB; 1274776at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001817; Chromosome 1.
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..227
FT /note="Probable chorismate pyruvate-lyase"
FT /id="PRO_0000255904"
FT REGION 192..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 113
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 227 AA; 24497 MW; FC184FCAA926B439 CRC64;
MSIRFVAADA HWRVAPLPGL SAAQKDWLTR GGSLTAHLRA LGAVAVRVTR EGVALPWPDE
HAALGLAPRA PVWVREVVLA VEGVPFVAAH SVAPLAASAG VWQAMRRLRT RPLAELLYSD
SSVARSSLVS RRLTARHPLY RLAACAIESL PPHALVARRS VFERHGAPLM VTECMLPALW
AHLATVSGAG GSGDWSAHPR VREHGRPLEH TASRAHPATR ASDEQRR