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UBIA_SHEDO
ID   UBIA_SHEDO              Reviewed;         293 AA.
AC   Q12S01;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   25-MAY-2022, entry version 86.
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=Sden_0483;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
RG   US DOE Joint Genome Institute;
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   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE53775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000302; ABE53775.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041405646.1; NC_007954.1.
DR   AlphaFoldDB; Q12S01; -.
DR   SMR; Q12S01; -.
DR   STRING; 318161.Sden_0483; -.
DR   EnsemblBacteria; ABE53775; ABE53775; Sden_0483.
DR   KEGG; sdn:Sden_0483; -.
DR   eggNOG; COG0382; Bacteria.
DR   HOGENOM; CLU_034879_1_0_6; -.
DR   OrthoDB; 1472516at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000001982; 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..293
FT                   /note="4-hydroxybenzoate octaprenyltransferase"
FT                   /id="PRO_0000262837"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ   SEQUENCE   293 AA;  33001 MW;  54DF13DEABD7BEFE CRC64;
     MTAQTQQSIM AKLALYAQLS RIDRPIGTLL LLWPCLMALL FAAKGMPDIK VLLIFILGVV
     IMRACGCIIN DYADRNLDAH VERTKQRPLA SGAISSKEAL SLFALLGLLA FALVLLLNPL
     VVKLSVVGIV LTIMYPFMKR VTNMPQMFLG IVWSWSIPMA YAAQLGEVPV EAWWLFAANW
     CWTVAYDTMY AMIDRDDDLK VGIKSSAILF GRFDRQWIAV FQLMAFGCFL MAGLSAEREF
     IYALGLLGFI AFSVYQQRLI FSRERPACFK AFLNNNWVGM LLFLTLAADY LLY
 
 
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