UBID_ACTP2
ID UBID_ACTP2 Reviewed; 487 AA.
AC A3N287;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=APL_1439;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(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; CP000569; ABN74523.1; -; Genomic_DNA.
DR RefSeq; WP_011848593.1; NC_009053.1.
DR AlphaFoldDB; A3N287; -.
DR SMR; A3N287; -.
DR STRING; 416269.APL_1439; -.
DR EnsemblBacteria; ABN74523; ABN74523; APL_1439.
DR KEGG; apl:APL_1439; -.
DR PATRIC; fig|416269.6.peg.1498; -.
DR eggNOG; COG0043; Bacteria.
DR HOGENOM; CLU_023348_4_1_6; -.
DR OMA; SYQQFWG; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001432; 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_1000069840"
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; 54948 MW; 64696E78F2B38D61 CRC64;
MKYKDLREFL TLLEGQGELV RIKQEIDPYL EMAEISDRTL RKGGPAILFE NPKGYRMPVL
CNLFGTPKRV ALGMGQEDTH ALRELGKLLA FLKEPEPPKG FKELIGQLPQ WKQVLNMPSK
VLGKADCQQV VLSGDEVELY KLPIMHCHEG DVAPLVAWGL TITQGPYKKR QNLGIYRQQL
IGKNKLIMRW LSHRGGALDF HEWKEANPDK PFPVSVAIGA DPATILAAVT PIPDTLSEYA
FAGLLRGQKT EVTKSISNDL EVPASAEIVL EGYIDPNETA LEGPYGDHTG YYNEQEYFPV
FTVTHITMRR DAIYHSTYTG RPPDEPAVLG EALNEVFIPI LQKQFPEIVD FYLPPEGCSY
RLAVVTIKKQ YAGHAKRVMM GVWSFLRQFM YTKFVIVCDD DVNARDWKDV IWAITTRCDP
SRDTTLIDHT PIDYLDFASP IAGLGSKMGI DATNKWPGET SREWGTPIKK DPNVVKRVDE
IWDQLGL
