ID   UBID_CUPPJ              Reviewed;         509 AA.
AC   Q474N8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   03-AUG-2022, entry version 103.
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}; OrderedLocusNames=Reut_A0765;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ60145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000090; AAZ60145.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041679503.1; NC_007347.1.
DR   AlphaFoldDB; Q474N8; -.
DR   SMR; Q474N8; -.
DR   STRING; 264198.Reut_A0765; -.
DR   EnsemblBacteria; AAZ60145; AAZ60145; Reut_A0765.
DR   KEGG; reu:Reut_A0765; -.
DR   eggNOG; COG0043; Bacteria.
DR   HOGENOM; CLU_023348_4_1_4; -.
DR   OMA; SYQQFWG; -.
DR   OrthoDB; 1012819at2; -.
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..509
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT                   /id="PRO_0000267686"
FT   ACT_SITE        304
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         179
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         182..184
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         196..198
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         201..202
FT                   /ligand="prenyl-FMN"
FT                   /ligand_id="ChEBI:CHEBI:87746"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT   BINDING         245
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
SQ   SEQUENCE   509 AA;  56525 MW;  0BD9CE2E1CF9A018 CRC64;
     MQYKDLRDFI SQLEQLGELR RVSTPVSPNL EMTEICDRLL RAGGPAVLFE RPAGFRSPEG
     TYSVPVLANL FGTTHRVALG MGAQSLEDLR DIGRVLSALK EPEPPRGLRE AGKLFTLAKS
     VWDMAPKRVS SPACQEIVWE GNDVDLARLP IQTCWPGDAA PLITWGLVVT KGPHKKRQNL
     GIYRQQVISR NQVIMRWLAH RGGALDFREH ALANPGKPFP IAVALGADPA TILGAVTPVP
     DTLSEYQFAG LLRGSRTALA GCLTPTLSEL SVPASAEIVL EGHIQPDPDH PSGYQHALEG
     PYGDHTGYYN EQDWFPVFTI DRITMRRDPI YHSTYTGKPP DEPAVLGVAL NEVFVPLLQK
     QFPEITDFYL PPEGCSYRMA LVRMKKQYAG HAKRVMFGVW SFLRQFMYTK FIVVVDDDVD
     VRDWKEVIWA ITTRVDPARD TVLVENTPID YLDFASPVSG LGSKMGIDAT DKWPGETTRE
     WGRTISMDPA VKAKVDGMMA TLFDRPAGT