ID   UBID_THISH              Reviewed;         487 AA.
AC   B8GSS8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=Tgr7_0008;
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584; DOI=10.4056/sigs.1483693;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71113.1; -; Genomic_DNA.
DR   RefSeq; WP_012636602.1; NC_011901.1.
DR   AlphaFoldDB; B8GSS8; -.
DR   SMR; B8GSS8; -.
DR   STRING; 396588.Tgr7_0008; -.
DR   EnsemblBacteria; ACL71113; ACL71113; Tgr7_0008.
DR   KEGG; tgr:Tgr7_0008; -.
DR   eggNOG; COG0043; Bacteria.
DR   HOGENOM; CLU_023348_4_1_6; -.
DR   OMA; SYQQFWG; -.
DR   OrthoDB; 1012819at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000002383; Chromosome.
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; Reference proteome; Ubiquinone biosynthesis.
FT   CHAIN           1..487
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT                   /id="PRO_1000186725"
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   487 AA;  54197 MW;  97E33F6315212C81 CRC64;
     MKYRDLRDFI AQLEALGELK RIGVEVDPHL EMTEICDRTL RAGGPALLFE KPKGHTMPVL
     GNLFGTPRRV ALGMGEDSVE ALREVGKLLA FLKEPDPPKG LKEAWKTLPI FKKVLDMAPK
     KVGSASCQDL VREGADVDLS SIPVQTCWPG DAGPLITWGL VVTKGPHKER QNMGIYRQQV
     IGPNRVIMRW LSHRGGALDF RDWCEKYPGE PFPVAVALGA DPATILGAVT PVPDSLSEHA
     FAGLLRGSRT ELVKCLGSDL LVPASAEIVL EGVIHPGDTA PEGPFGDHTG YYNEVDQFPV
     FTIERITSRR DPIYHSTYTG RPPDEPAILG VALNEVFIPI LQKQFPEIVD FYLPPEGCSY
     RLAVVTMRKQ YPGHAKRVMM GVWSFLRQFM YTKFVIVTDA DVNARDWQDV IWAMTTRMDP
     ARDTVMIENT PIDYLDFASP VSGLGSKIGF DATNKWPGET TREWGTPIVM DEAVKRRVDE
     MWETLGL