UBIC_PSEA6
ID UBIC_PSEA6 Reviewed; 192 AA.
AC Q15ZU0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Patl_0066;
OS Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=342610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6c / ATCC BAA-1087;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Karls A.C.,
RA Bartlett D., Higgins B.P., Richardson P.;
RT "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000388; ABG38598.1; -; Genomic_DNA.
DR RefSeq; WP_011573009.1; NC_008228.1.
DR AlphaFoldDB; Q15ZU0; -.
DR SMR; Q15ZU0; -.
DR STRING; 342610.Patl_0066; -.
DR EnsemblBacteria; ABG38598; ABG38598; Patl_0066.
DR KEGG; pat:Patl_0066; -.
DR eggNOG; COG3161; Bacteria.
DR HOGENOM; CLU_096824_3_0_6; -.
DR OMA; ELWGRRS; -.
DR OrthoDB; 1274776at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001981; 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; Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..192
FT /note="Probable chorismate pyruvate-lyase"
FT /id="PRO_0000292070"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ SEQUENCE 192 AA; 22297 MW; E8D6D7041CB88548 CRC64;
MQKTISHAFP LGDVTWSNQG RLSIPNAHLE SWLLNTGSLT QRLQTRCNDF KVQLVSQRQE
LATPAEYIQL GVSKMSQQKE NWQVREVILH GDNQPWVFAR SIIPQALCEA DFLELGDKPL
GHLIFNDDRF KRQPFQLMCL QPDEAFLHEY GLPPLTEIWG RRSVFCYQQY AMMVAELFLP
KAPAYRDSNF DR
