UBIC_ECOLI
ID UBIC_ECOLI Reviewed; 165 AA.
AC P26602; P76783; Q2M6R5; Q4JHR8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Chorismate pyruvate-lyase;
DE Short=CL;
DE Short=CPL;
DE EC=4.1.3.40 {ECO:0000269|PubMed:11825618, ECO:0000269|PubMed:8012607};
GN Name=ubiC; OrderedLocusNames=b4039, JW5713;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=1644192; DOI=10.1016/0014-5793(92)80710-x;
RA Siebert M., Bechthold A., Melzer M., May U., Berger U., Schroeder G.,
RA Schroeder J., Severin K., Heide L.;
RT "Ubiquinone biosynthesis. Cloning of the genes coding for chorismate
RT pyruvate-lyase and 4-hydroxybenzoate octaprenyl transferase from
RT Escherichia coli.";
RL FEBS Lett. 307:347-350(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
RC STRAIN=K12;
RX PubMed=1644758; DOI=10.1128/jb.174.16.5309-5316.1992;
RA Nichols B.P., Green J.M.;
RT "Cloning and sequencing of Escherichia coli ubiC and purification of
RT chorismate lyase.";
RL J. Bacteriol. 174:5309-5316(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=1512213; DOI=10.1128/jb.174.17.5762.1992;
RA Nishimura K., Nakahigashi K., Inokuchi H.;
RT "Location of the ubiA gene on the physical map of Escherichia coli.";
RL J. Bacteriol. 174:5762-5762(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8409922; DOI=10.1099/00221287-139-8-1795;
RA Wu G., Williams H.D., Gibson F., Poole R.K.;
RT "Mutants of Escherichia coli affected in respiration: the cloning and
RT nucleotide sequence of ubiA, encoding the membrane-bound p-
RT hydroxybenzoate:octaprenyltransferase.";
RL J. Gen. Microbiol. 139:1795-1805(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BL21;
RA Zhang D., Shrestha B., Tan T.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLU-156.
RX PubMed=8012607; DOI=10.1099/00221287-140-4-897;
RA Siebert M., Severin K., Heide L.;
RT "Formation of 4-hydroxybenzoate in Escherichia coli: characterization of
RT the ubiC gene and its encoded enzyme chorismate pyruvate-lyase.";
RL Microbiology 140:897-904(1994).
RN [10]
RP POSSIBLE GENETIC INTERACTION WITH DNAG.
RX PubMed=9093842; DOI=10.1093/genetics/145.4.867;
RA Britton R.A., Lupski J.R.;
RT "Isolation and characterization of suppressors of two Escherichia coli dnaG
RT mutations, dnaG2903 and parB.";
RL Genetics 145:867-875(1997).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11825618; DOI=10.1016/s0167-4838(01)00302-8;
RA Holden M.J., Mayhew M.P., Gallagher D.T., Vilker V.L.;
RT "Chorismate lyase: kinetics and engineering for stability.";
RL Biochim. Biophys. Acta 1594:160-167(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
RX PubMed=10675300; DOI=10.1006/jsbi.1999.4205;
RA Stover C., Mayhew M.P., Holden M.J., Howard A., Gallagher D.T.;
RT "Crystallization and 1.1-A diffraction of chorismate lyase from Escherichia
RT coli.";
RL J. Struct. Biol. 129:96-99(2000).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PRODUCT; MUTANT
RP SER-15/SER-82 IN COMPLEX WITH PRODUCT; MUTANT SER-15 IN COMPLEX WITH
RP PRODUCT, AND SUBUNIT.
RX PubMed=11455603; DOI=10.1002/prot.1095;
RA Gallagher D.T., Mayhew M., Holden M.J., Howard A., Kim K.-J., Vilker V.L.;
RT "The crystal structure of chorismate lyase shows a new fold and a tightly
RT retained product.";
RL Proteins 44:304-311(2001).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF MUTANT SER-15/SER-82 IN COMPLEXES
RP WITH PRODUCT AND SUBSTRATE ANALOG; MUTANT SER-15/SER-82/ALA-91 IN COMPLEXES
RP WITH PRODUCT AND SUBSTRATE ANALOG, FUNCTION, MUTAGENESIS OF GLY-91,
RP ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=16343413; DOI=10.1016/j.abb.2005.10.026;
RA Smith N., Roitberg A.E., Rivera E., Howard A., Holden M.J., Mayhew M.,
RA Kaistha S., Gallagher D.T.;
RT "Structural analysis of ligand binding and catalysis in chorismate lyase.";
RL Arch. Biochem. Biophys. 445:72-80(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:0000269|PubMed:11825618,
CC ECO:0000269|PubMed:16343413, ECO:0000269|PubMed:1644758,
CC ECO:0000269|PubMed:8012607}.
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;
CC Evidence={ECO:0000269|PubMed:11825618, ECO:0000269|PubMed:8012607};
CC -!- ACTIVITY REGULATION: Inhibited by 4-hydroxybenzoate, vanillate, 4-
CC hydroxybenzaldehyde and 3-carboxymethylaminomethyl-4-hydroxybenzoic
CC acid. {ECO:0000269|PubMed:11825618, ECO:0000269|PubMed:16343413}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.1 uM for chorismate {ECO:0000269|PubMed:8012607};
CC KM=29 uM for chorismate {ECO:0000269|PubMed:11825618};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11825618,
CC ECO:0000269|PubMed:8012607};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11455603,
CC ECO:0000269|PubMed:16343413}.
CC -!- INTERACTION:
CC P26602; P0AFG8: aceE; NbExp=2; IntAct=EBI-559360, EBI-542683;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: The sdgG mutation, which suppresses a conditional
CC mutation in dnaG (DNA primase), has been localized to one of the ubiA,
CC ubiC or yjbI genes. {ECO:0000305|PubMed:9093842}.
CC -!- SIMILARITY: Belongs to the UbiC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43133.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA40681.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X66619; CAA47181.1; -; Genomic_DNA.
DR EMBL; M93136; AAA24711.1; -; Genomic_DNA.
DR EMBL; M93413; AAA24716.1; -; Genomic_DNA.
DR EMBL; X57434; CAA40681.1; ALT_INIT; Genomic_DNA.
DR EMBL; M96268; AAA17027.1; -; Unassigned_DNA.
DR EMBL; DQ087228; AAY88959.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43133.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77009.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78041.1; -; Genomic_DNA.
DR PIR; S25660; S25660.
DR RefSeq; NP_418463.4; NC_000913.3.
DR RefSeq; WP_001326644.1; NZ_SSZK01000016.1.
DR PDB; 1FW9; X-ray; 1.40 A; A=2-165.
DR PDB; 1G1B; X-ray; 1.99 A; A/B=2-165.
DR PDB; 1G81; X-ray; 1.71 A; A=2-165.
DR PDB; 1JD3; X-ray; 2.03 A; A=2-165.
DR PDB; 1TT8; X-ray; 1.00 A; A=2-165.
DR PDB; 1XLR; X-ray; 1.94 A; A=2-165.
DR PDB; 2AHC; X-ray; 2.40 A; A/B/C/D=2-165.
DR PDBsum; 1FW9; -.
DR PDBsum; 1G1B; -.
DR PDBsum; 1G81; -.
DR PDBsum; 1JD3; -.
DR PDBsum; 1TT8; -.
DR PDBsum; 1XLR; -.
DR PDBsum; 2AHC; -.
DR AlphaFoldDB; P26602; -.
DR SMR; P26602; -.
DR BioGRID; 4262658; 212.
DR BioGRID; 852839; 1.
DR DIP; DIP-11066N; -.
DR IntAct; P26602; 3.
DR STRING; 511145.b4039; -.
DR DrugBank; DB04242; 4-hydroxybenzoic acid.
DR DrugBank; DB02130; Vanillic acid.
DR jPOST; P26602; -.
DR PaxDb; P26602; -.
DR PRIDE; P26602; -.
DR EnsemblBacteria; AAC77009; AAC77009; b4039.
DR EnsemblBacteria; BAE78041; BAE78041; BAE78041.
DR GeneID; 948545; -.
DR KEGG; ecj:JW5713; -.
DR KEGG; eco:b4039; -.
DR PATRIC; fig|511145.12.peg.4156; -.
DR EchoBASE; EB1343; -.
DR eggNOG; COG3161; Bacteria.
DR HOGENOM; CLU_096824_1_0_6; -.
DR InParanoid; P26602; -.
DR OMA; ELWGRRS; -.
DR PhylomeDB; P26602; -.
DR BioCyc; EcoCyc:CHORPYRLY-MON; -.
DR BioCyc; MetaCyc:CHORPYRLY-MON; -.
DR BRENDA; 4.1.3.40; 2026.
DR SABIO-RK; P26602; -.
DR UniPathway; UPA00232; -.
DR EvolutionaryTrace; P26602; -.
DR PRO; PR:P26602; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0008813; F:chorismate lyase activity; IDA:EcoCyc.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Lyase;
KW Reference proteome; Ubiquinone biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1644758"
FT CHAIN 2..165
FT /note="Chorismate pyruvate-lyase"
FT /id="PRO_0000065711"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11455603,
FT ECO:0000269|PubMed:16343413"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11455603,
FT ECO:0000269|PubMed:16343413"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11455603,
FT ECO:0000269|PubMed:16343413"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11455603,
FT ECO:0000269|PubMed:16343413"
FT MUTAGEN 91
FT /note="G->A: Increases the inhibition by product by about
FT 40%. No effect on substrate affinity."
FT /evidence="ECO:0000269|PubMed:16343413"
FT MUTAGEN 156
FT /note="E->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8012607"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1G1B"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:1TT8"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:1TT8"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 46..56
FT /evidence="ECO:0007829|PDB:1TT8"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1TT8"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1TT8"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:1TT8"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1TT8"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2AHC"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1G81"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:1TT8"
FT STRAND 150..158
FT /evidence="ECO:0007829|PDB:1TT8"
SQ SEQUENCE 165 AA; 18777 MW; 6DAACD25BC338F09 CRC64;
MSHPALTQLR ALRYCKEIPA LDPQLLDWLL LEDSMTKRFE QQGKTVSVTM IREGFVEQNE
IPEELPLLPK ESRYWLREIL LCADGEPWLA GRTVVPVSTL SGPELALQKL GKTPLGRYLF
TSSTLTRDFI EIGRDAGLWG RRSRLRLSGK PLLLTELFLP ASPLY
