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UBIA_SHESR
ID   UBIA_SHESR              Reviewed;         286 AA.
AC   Q0HQR8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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};
GN   OrderedLocusNames=Shewmr7_3557;
OS   Shewanella sp. (strain MR-7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60481;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-7;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000444; ABI44537.1; -; Genomic_DNA.
DR   RefSeq; WP_011621276.1; NC_008322.1.
DR   AlphaFoldDB; Q0HQR8; -.
DR   SMR; Q0HQR8; -.
DR   PRIDE; Q0HQR8; -.
DR   EnsemblBacteria; ABI44537; ABI44537; Shewmr7_3557.
DR   KEGG; shm:Shewmr7_3557; -.
DR   HOGENOM; CLU_034879_1_0_6; -.
DR   OMA; MVVYPYG; -.
DR   OrthoDB; 1472516at2; -.
DR   UniPathway; UPA00232; -.
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; Transferase;
KW   Transmembrane; Transmembrane helix; Ubiquinone biosynthesis.
FT   CHAIN           1..286
FT                   /note="4-hydroxybenzoate octaprenyltransferase"
FT                   /id="PRO_0000262841"
FT   TRANSMEM        21..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ   SEQUENCE   286 AA;  31961 MW;  D16D1EA95173B967 CRC64;
     MNLKQKWDVY SRLTRLDRPI GTLLLLWPCL MALVLAAGGM PDIKVLIIFI IGVVIMRACG
     CIINDYADRD LDSHVERTRS RPLASGEIST KEALLLFVIL GLAAFGLVLL LNGLVVKLSV
     VGIILTIIYP FTKRVTNMPQ MFLGVVWSWS IPMAYAAQTG EVPIEAWWLF AANWFWTVAY
     DTMYAMVDRD DDLKVGIKST AILFGQYDRQ IIGLFQFAAL LCFIAAGWSA DRGLLYGLGL
     LTFVGFSTYQ QMLIFGRERA PCFKAFLNNN WAGLALFVGL GADYLF
 
 
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