UBIC2_BURP1
ID UBIC2_BURP1 Reviewed; 197 AA.
AC Q3JUM4;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Probable chorismate pyruvate-lyase 2 {ECO:0000255|HAMAP-Rule:MF_01632};
DE Short=CL 2 {ECO:0000255|HAMAP-Rule:MF_01632};
DE Short=CPL 2 {ECO:0000255|HAMAP-Rule:MF_01632};
DE EC=4.1.3.40 {ECO:0000255|HAMAP-Rule:MF_01632};
GN Name=ubiC2 {ECO:0000255|HAMAP-Rule:MF_01632};
GN OrderedLocusNames=BURPS1710b_1319;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABA47638.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000124; ABA47638.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004550738.1; NC_007434.1.
DR AlphaFoldDB; Q3JUM4; -.
DR SMR; Q3JUM4; -.
DR EnsemblBacteria; ABA47638; ABA47638; BURPS1710b_1319.
DR KEGG; bpm:BURPS1710b_1319; -.
DR HOGENOM; CLU_096824_0_0_4; -.
DR OrthoDB; 1274776at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000002700; Chromosome I.
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..197
FT /note="Probable chorismate pyruvate-lyase 2"
FT /id="PRO_0000240540"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 111
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 197 AA; 21770 MW; E009ED2A861D9EA1 CRC64;
MRFDAADAHW RETPRPGASS AQKDWLTRGG SLTAHLARLG RVTVRVTRET VAAPWADEHR
ALSCASRAPV WVREVVLAVD GAPFVAAHSI APLAASKGVW QAMRRLRTRP LAELLYSDPE
VTRSALVSRR VLAGHPLFSL ASLALARAYA TEHAFAARRS VFERRGTPLM VTECMLPALW
RHLDAHGERR ARGLEQT