UBID_PSE14
ID UBID_PSE14 Reviewed; 488 AA.
AC Q48PS5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, 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=PSPPH_0289;
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ36611.1; -; Genomic_DNA.
DR RefSeq; WP_011167423.1; NC_005773.3.
DR AlphaFoldDB; Q48PS5; -.
DR SMR; Q48PS5; -.
DR STRING; 264730.PSPPH_0289; -.
DR EnsemblBacteria; AAZ36611; AAZ36611; PSPPH_0289.
DR KEGG; psp:PSPPH_0289; -.
DR eggNOG; COG0043; Bacteria.
DR HOGENOM; CLU_023348_4_1_6; -.
DR OMA; SYQQFWG; -.
DR OrthoDB; 1012819at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000551; 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..488
FT /note="3-octaprenyl-4-hydroxybenzoate carboxy-lyase"
FT /id="PRO_0000267683"
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 488 AA; 54608 MW; 50329F677C77D19C CRC64;
MKFKDLRDFV QQLEQRGELK RIQMPISPVL EMTEICDRTL RAKGPALLFE KPVGFDIPVL
GNLFGTPERV AMGMGAEAVS ELREIGKLLA FLKEPEPPKG LKDAWSKLPI FRKVIAMAPK
VVKDAPCQEI VIEGDDVDLG MLPVQTCWPG DVAPLITWGL TVTKGPNKER QNLGIYRQQV
IGRNKIIMRW LSHRGGALDF RDWCAKHPGE PYPVAVALGA DPATILGAVT PVPDSLSEYA
FAGLLRGSRT ELIKCRGSNL QVPASAEIVL EGVIHPGEMA DEGPYGDHTG YYNEVDSFPV
LTVERITHRI KPIYHSTYTG RPPDEPAILG VALNEVFVPI LQKQFPEIVD FYLPPEGCSY
RMAVVTIKKQ YPGHAKRVML GVWSFLRQFM YTKFVIVTDD DINARDWNDV IWAITTRMDP
KRDTVMIDNT PIDYLDFASP VSGLGSKMGL DVTNKWPGET TREWGRAIVK DEATTRRVDE
IWTQLGID
