ID   UBID_KLEP3              Reviewed;         489 AA.
AC   B5XYH3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, 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=KPK_5336;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI10791.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XYH3; -.
DR   SMR; B5XYH3; -.
DR   EnsemblBacteria; ACI10791; ACI10791; KPK_5336.
DR   KEGG; kpe:KPK_5336; -.
DR   HOGENOM; CLU_023348_4_1_6; -.
DR   OMA; SYQQFWG; -.
DR   OrthoDB; 1012819at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001734; 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; Ubiquinone biosynthesis.
FT   CHAIN           1..489
FT                   /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT                   /id="PRO_1000186715"
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   489 AA;  54914 MW;  83EF20AB2C277689 CRC64;
     MKYHDLRDFL TLLEQQGELK RITLPVDPHL EITEIADRTL RAGGPALLFE NPKGYSMPVL
     CNLFGTPRRV ALGMGQEDVS SLREVGKLLA FLKEPEPPKG FRDLFDKLPQ FKQVLNMPTK
     RLRGAPCQQK IIQGDDVDLN KIPIMTCWPE DAAPLITWGL TVTRGPHKER QNLGIYRQQL
     IGKNKLIMRW LSHRGGALDF QEWCAAHPGE RFPVSVALGA DPATILGAVT PVPDTLSEYA
     FAGLLRGTKT EVVKCVSNDL EVPASAEIVL EGYIEAGEMA PEGPYGDHTG YYNEVDSFPV
     FTVTHITQRE DAIYHSTYTG RPPDEPAVLG VALNEVFVPI LQKQFPEIVD FYLPPEGCSY
     RLAVVTMKKQ YAGHAKRVMM GVWSFLRQFM YTKFVIVCDD DVNARDWNDV IWAITTRMDP
     ARDTVLVENT PIDYLDFASP VSGLGSKMGL DATNKWPGET QREWGRPIKK DPQVTARIDA
     IWDELAIFK