UBIA_LEGPH
ID UBIA_LEGPH Reviewed; 282 AA.
AC Q5ZVL0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=4-hydroxybenzoate octaprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635};
DE EC=2.5.1.39 {ECO:0000255|HAMAP-Rule:MF_01635};
DE AltName: Full=4-HB polyprenyltransferase {ECO:0000255|HAMAP-Rule:MF_01635};
GN Name=ubiA {ECO:0000255|HAMAP-Rule:MF_01635}; OrderedLocusNames=lpg1430;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
CC -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with
CC an all-trans polyprenyl group. Mediates the second step in the final
CC reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the
CC condensation of the polyisoprenoid side chain with PHB, generating the
CC first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate.
CC {ECO:0000255|HAMAP-Rule:MF_01635}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + all-trans-octaprenyl diphosphate = 4-
CC hydroxy-3-all-trans-octaprenylbenzoate + diphosphate;
CC Xref=Rhea:RHEA:27782, ChEBI:CHEBI:1617, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57711; EC=2.5.1.39;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01635};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01635};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01635}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01635}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01635}.
CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_01635}.
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DR EMBL; AE017354; AAU27512.1; -; Genomic_DNA.
DR RefSeq; WP_010947159.1; NC_002942.5.
DR RefSeq; YP_095459.1; NC_002942.5.
DR AlphaFoldDB; Q5ZVL0; -.
DR SMR; Q5ZVL0; -.
DR STRING; 272624.lpg1430; -.
DR PaxDb; Q5ZVL0; -.
DR EnsemblBacteria; AAU27512; AAU27512; lpg1430.
DR GeneID; 66490562; -.
DR KEGG; lpn:lpg1430; -.
DR PATRIC; fig|272624.6.peg.1500; -.
DR eggNOG; COG0382; Bacteria.
DR HOGENOM; CLU_034879_1_0_6; -.
DR OMA; MVVYPYG; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002083; F:4-hydroxybenzoate decaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0047293; F:4-hydroxybenzoate nonaprenyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13959; PT_UbiA_COQ2; 1.
DR Gene3D; 1.10.357.140; -; 1.
DR HAMAP; MF_01635; UbiA; 1.
DR InterPro; IPR006370; HB_polyprenyltransferase-like.
DR InterPro; IPR039653; Prenyltransferase.
DR InterPro; IPR000537; UbiA_prenyltransferase.
DR InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR InterPro; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR PROSITE; PS00943; UBIA; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Magnesium; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubiquinone biosynthesis.
FT CHAIN 1..282
FT /note="4-hydroxybenzoate octaprenyltransferase"
FT /id="PRO_0000262805"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ SEQUENCE 282 AA; 32222 MW; 9BD877B978E48D89 CRC64;
MIPWNAYVRL LRLNKPIGIL LLWYPTAWAL WMANQGFPSI DLLMIFLLGT VFMRSAGCVI
NDIADRHIDR HVARTQFRPL TAGEVSLSEA FILLFILLCA SLLLLLKLPI NCFYFAVISV
LITFLYPFCK RFLNAPQLIL GLAFSMGIPM AFIASGKNLN SDFIVLFLIN FSWIIAYDTM
YAMTDKADDL KIGVKSTAIY FASYDRLIIA LLLIFLHSLW LVWAINKNAE WFFYLLWCTA
AGILTYQLKL IYARIPKNCF KAFLVSGYYG LVMWFAVGLA LI
