UBIC_BARQU
ID UBIC_BARQU Reviewed; 172 AA.
AC Q6FZ67;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BQ09210;
OS Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Toulouse;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(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; BX897700; CAF26398.1; -; Genomic_DNA.
DR RefSeq; WP_011179627.1; NC_005955.1.
DR AlphaFoldDB; Q6FZ67; -.
DR SMR; Q6FZ67; -.
DR STRING; 283165.BQ09210; -.
DR EnsemblBacteria; CAF26398; CAF26398; BQ09210.
DR KEGG; bqu:BQ09210; -.
DR eggNOG; COG3161; Bacteria.
DR HOGENOM; CLU_096824_1_0_5; -.
DR OMA; ELWGRRS; -.
DR OrthoDB; 1274776at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000597; 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..172
FT /note="Probable chorismate pyruvate-lyase"
FT /id="PRO_0000240535"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ SEQUENCE 172 AA; 19685 MW; 07DB46CF279879DE CRC64;
MISDLRSSIL PPLKWLSDQD PPVPAGVSDW LMELGSMTRR FENHCTCIRI EPQRECFITR
DNLKEEAAHL PNSTCYWLRE VILMGDNQPW LLGRTVIPQE TLFEHNEALI NLGTVPLGRY
LFSSGNLTRD YIYIGRQGAL WARRSRLRLA GKPLLLTELF LAASPLYTTN SI
