UBID_BURPS
ID UBID_BURPS Reviewed; 519 AA.
AC Q63RP1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BPSL2631;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36639.1; -; Genomic_DNA.
DR RefSeq; WP_004536419.1; NZ_CP009538.1.
DR RefSeq; YP_109227.1; NC_006350.1.
DR AlphaFoldDB; Q63RP1; -.
DR SMR; Q63RP1; -.
DR STRING; 272560.BPSL2631; -.
DR EnsemblBacteria; CAH36639; CAH36639; BPSL2631.
DR GeneID; 56528568; -.
DR KEGG; bps:BPSL2631; -.
DR PATRIC; fig|272560.51.peg.2720; -.
DR eggNOG; COG0043; Bacteria.
DR OMA; SYQQFWG; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000605; Chromosome 1.
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; 2.
DR Pfam; PF01977; UbiD; 1.
DR TIGRFAMs; TIGR00148; TIGR00148; 2.
PE 3: Inferred from homology;
KW Cell membrane; Decarboxylase; Flavoprotein; FMN; Lyase; Manganese;
KW Membrane; Metal-binding; Reference proteome; Ubiquinone biosynthesis.
FT CHAIN 1..519
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT /id="PRO_0000267654"
FT ACT_SITE 318
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 180..182
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 194..196
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 199..200
FT /ligand="prenyl-FMN"
FT /ligand_id="ChEBI:CHEBI:87746"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
FT BINDING 243
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01636"
SQ SEQUENCE 519 AA; 57359 MW; B915979D7691FC35 CRC64;
MKYKDLRDFI HGLEQRGELR RVTQPVSPVL EMTELCDRVL RAGGPALLFD APAGHRFPVL
GNLFGTPRRV ALGMGVDADD EAALASLRDI GRLLSALKEP DPPKRLKDAG KLLSLAKAVW
DMSPKTVSAP PCQEIVWEGD DVDLHKLPIQ TCWPGDAGPL LTWGLTVTRG PNKTRQNLGI
YRQQLIGRNK LIMRWLAHRG GALDFREFAL KHPGQPYPVA VVLGADPATM LGAVTPVPDS
LSEYQFAGLL RGARTELAKC VTPGVDALQV PARAEIVLEG FIHPQQGAPA PAPEGAPPRP
AAGAAAGYEH ALEGPYGDHT GYYNEQEWFP VFTVERITMR RDAIYHSTYT GKPPDEPAVL
GVALNEVFVP LLQKQFAEIT DFYLPPEGCS YRMAIVQMKK SYAGHAKRVM FGVWSFLRQF
MYTKFIVVVD EDVNVRDWKE VIWAITTRVD PARDTVLVEN TPIDYLDFAS PVAGLGSKMG
LDATNKWPGE TQREWGRPIE MDAAVKARVD RLWTEIGLS
