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UBIA_MARMS
ID   UBIA_MARMS              Reviewed;         284 AA.
AC   A6W3L5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
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=Mmwyl1_4399;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) 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; CP000749; ABR73294.1; -; Genomic_DNA.
DR   RefSeq; WP_012072059.1; NC_009654.1.
DR   AlphaFoldDB; A6W3L5; -.
DR   SMR; A6W3L5; -.
DR   STRING; 400668.Mmwyl1_4399; -.
DR   EnsemblBacteria; ABR73294; ABR73294; Mmwyl1_4399.
DR   KEGG; mmw:Mmwyl1_4399; -.
DR   eggNOG; COG0382; Bacteria.
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; IPR044878; UbiA_sf.
DR   PANTHER; PTHR11048; PTHR11048; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01474; ubiA_proteo; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Magnesium; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix; Ubiquinone biosynthesis.
FT   CHAIN           1..284
FT                   /note="4-hydroxybenzoate octaprenyltransferase"
FT                   /id="PRO_1000088175"
FT   TRANSMEM        13..32
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        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ   SEQUENCE   284 AA;  32507 MW;  3E259AFCDAD05219 CRC64;
     MNKLKDYAEL TRFNRPIGSF LLMWPTLWAL WLAADGMPQW HLVIIFILGV FSMRSAGCVI
     NDYADRKVDG FVDRTKNRPL PSGRVSEKEA LMLFCALSIL SFILVLFTDL RTILLSFVGL
     GLAALYPFMK RYTHLPQLFL GLAFSWAIPM AYSAQGGDLT DPKLWMLFVA NCFWTIAYDT
     YYAMTDRPDD LKIGIKSTAI LFGQYDLFVI ICLQGLTLSL LTWIGLLAGL HWLYFVSLIV
     CVGLFYQQFK QAKERDRQAC FRSFLDNNRV GYCVFIGLVA SYFM
 
 
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