UBIC_IDILO
ID UBIC_IDILO Reviewed; 193 AA.
AC Q5QUP2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=IL0265;
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR;
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(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; AE017340; AAV81108.1; -; Genomic_DNA.
DR RefSeq; WP_011233527.1; NC_006512.1.
DR AlphaFoldDB; Q5QUP2; -.
DR SMR; Q5QUP2; -.
DR STRING; 283942.IL0265; -.
DR EnsemblBacteria; AAV81108; AAV81108; IL0265.
DR KEGG; ilo:IL0265; -.
DR eggNOG; COG3161; Bacteria.
DR HOGENOM; CLU_096824_1_1_6; -.
DR OMA; HTIVHPR; -.
DR OrthoDB; 1274776at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001171; 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..193
FT /note="Probable chorismate pyruvate-lyase"
FT /id="PRO_0000240548"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01632"
SQ SEQUENCE 193 AA; 21869 MW; B38D14CA3BBBCD27 CRC64;
MTTEFYATPA FPVSKALQWT PPEQLELTPT QADWLLYEGS LTERLKQIGQ QFSVKLLGQQ
LLAPNTEEKQ RLKGKDQAVI REVLLYCNEK PWVFARSLFS PSAENANTLN LQQLGNQSLG
ESLFARSDLY CGDIEVAKVA LEHPVARLNQ QWFGINQRLL SRRRIFSTGG EQLLVSEVFL
QPSPLYSSPN NRS
