ID   UBID_YERPG              Reviewed;         495 AA.
AC   A9R751;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=3-octaprenyl-4-hydroxybenzoate carboxy-lyase {ECO:0000255|HAMAP-Rule:MF_01636};
DE            EC=4.1.1.98 {ECO:0000255|HAMAP-Rule:MF_01636};
DE   AltName: Full=Polyprenyl p-hydroxybenzoate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01636};
GN   Name=ubiD {ECO:0000255|HAMAP-Rule:MF_01636};
GN   OrderedLocusNames=YpAngola_A1909;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
CC   -!- FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy
CC       benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-hydroxy-3-all-trans-polyprenylbenzoate + H(+) = a 2-all-
CC         trans-polyprenylphenol + CO2; Xref=Rhea:RHEA:41680, Rhea:RHEA-
CC         COMP:9514, Rhea:RHEA-COMP:9516, ChEBI:CHEBI:1269, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:78396; EC=4.1.1.98;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01636};
CC   -!- COFACTOR:
CC       Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01636};
CC       Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01636};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01636};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01636};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01636}.
CC   -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01636}.
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DR   EMBL; CP000901; ABX85206.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9R751; -.
DR   SMR; A9R751; -.
DR   KEGG; ypg:YpAngola_A1909; -.
DR   OMA; SYQQFWG; -.
DR   UniPathway; UPA00232; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008694; F:3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01636; UbiD; 1.
DR   InterPro; IPR002830; UbiD.
DR   InterPro; IPR023677; UbiD_bacteria.
DR   PANTHER; PTHR30108; PTHR30108; 1.
DR   Pfam; PF01977; UbiD; 1.
DR   TIGRFAMs; TIGR00148; TIGR00148; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Decarboxylase; Flavoprotein; FMN; Lyase; Manganese;
KW   Membrane; Metal-binding; Ubiquinone biosynthesis.
FT   CHAIN           1..495
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT                   /id="PRO_1000186726"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         172
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         175..177
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         189..191
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         194..195
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         238
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
SQ   SEQUENCE   495 AA;  55979 MW;  97F15A97D1E46E32 CRC64;
     MKYRDLRDFL SLLEQRGELK RISQPIDPYL EMTEIADRTL RAGGPALLFE NPKGYSMPVL
     CNLFGTAKRV AMGMGQEDVS ALRDVGKLLA FLKEPDPPKG FRDLFDKLPK FKQVLNMPTK
     RLNSAPCQEQ VWQGEDVDLS RIPVMHCWPE DAAPLVSWGL TITRGPHKER QNLGIYRQQV
     LGKNKLIMRW LSHRGGALDY QEWCEAHPGE RFPVAVALGA DPATILAAVT PVPDTLSEYA
     FAGLLRGHKT EVVKCLSNDL EVPASAEIVL EGYIEQGDMA PEGPYGDHTG YYNEIDNFPV
     FTVTHITQRQ DAIYHSTYTG RPPDEPAVMG VALNEVFVPI LQKQFPEIVD FYLPPEGCSY
     RLAVVTIKKQ YAGHAKRVMM GIWSFLRQFM YTKFVIVCDD DINARDWNDV IWAITTRMDP
     SRDTVLIENT PIDYLDFASP VSGLGSKMGL DATNKWPAET PREWGRPIKM DEDVRARIDA
     LWDELAIFSD KDAKR