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UBIC1_BURP1
ID   UBIC1_BURP1             Reviewed;         184 AA.
AC   Q3JJ81;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Probable chorismate pyruvate-lyase 1 {ECO:0000255|HAMAP-Rule:MF_01632};
DE            Short=CL 1 {ECO:0000255|HAMAP-Rule:MF_01632};
DE            Short=CPL 1 {ECO:0000255|HAMAP-Rule:MF_01632};
DE            EC=4.1.3.40 {ECO:0000255|HAMAP-Rule:MF_01632};
GN   Name=ubiC1 {ECO:0000255|HAMAP-Rule:MF_01632};
GN   OrderedLocusNames=BURPS1710b_A1215;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(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}.
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DR   EMBL; CP000125; ABA51190.1; -; Genomic_DNA.
DR   RefSeq; WP_004529335.1; NC_007435.1.
DR   AlphaFoldDB; Q3JJ81; -.
DR   SMR; Q3JJ81; -.
DR   EnsemblBacteria; ABA51190; ABA51190; BURPS1710b_A1215.
DR   KEGG; bpm:BURPS1710b_A1215; -.
DR   HOGENOM; CLU_096824_0_0_4; -.
DR   OMA; HTIVHPR; -.
DR   OrthoDB; 1274776at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000002700; Chromosome II.
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..184
FT                   /note="Probable chorismate pyruvate-lyase 1"
FT                   /id="PRO_0000240539"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ   SEQUENCE   184 AA;  19954 MW;  E99ABAFA51E3D1D5 CRC64;
     MNTSSGWSRQ PPASLSELEI HWLFAPGSLT ERLSALGEYS LEPVDQRHAA ACAADASLLG
     VEPDSPIWVR EVVMRLDAQP CVTARSIASA HALETQWKPL TGYGSLPLGH ILYDDPAIVR
     APFECALLMP DDPLDAISRR YARAAAPPRA RRSAFVRNGA TLVVSECFLP QFWSGFAQAR
     LAGA
 
 
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