ID A0A140D6E3_9ENTR Unreviewed; 290 AA. AC A0A140D6E3; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 19-JAN-2022, entry version 18. DE RecName: Full=4-hydroxybenzoate octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01635}; DE EC=2.5.1.39 {ECO:0000256|HAMAP-Rule:MF_01635}; DE AltName: Full=4-HB polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01635}; GN Name=hdbP {ECO:0000313|EMBL:AMK07429.1}; GN Synonyms=ubiA {ECO:0000256|HAMAP-Rule:MF_01635}; OS Klebsiella sp. NT18-21. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=1778872 {ECO:0000313|EMBL:AMK07429.1}; RN [1] {ECO:0000313|EMBL:AMK07429.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NT18-21Contig1 {ECO:0000313|EMBL:AMK07429.1}; RX PubMed=26822785; DOI=10.1186/s12864-016-2404-0; RA Maruthamuthu M., Jimenez D.J., Stevens P., van Elsas J.D.; RT "A multi-substrate approach for functional metagenomics-based screening for RT (hemi)cellulases in two wheat straw-degrading microbial consortia unveils RT novel thermoalkaliphilic enzymes."; RL BMC Genomics 17:86-86(2016). 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:0000256|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:0000256|HAMAP-Rule:MF_01635}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_01635}; CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_01635}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP- CC Rule:MF_01635}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01635}. CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. CC {ECO:0000256|HAMAP-Rule:MF_01635}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KU505137; AMK07429.1; -; Genomic_DNA. 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 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 {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP- KW Rule:MF_01635}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01635}; Magnesium {ECO:0000256|HAMAP-Rule:MF_01635}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01635}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01635}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01635}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01635}; KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP- KW Rule:MF_01635}. FT TRANSMEM 21..40 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01635" FT TRANSMEM 46..70 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01635" FT TRANSMEM 99..132 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01635" FT TRANSMEM 152..182 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01635" FT TRANSMEM 213..233 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01635" FT TRANSMEM 239..257 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01635" FT TRANSMEM 269..288 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01635" SQ SEQUENCE 290 AA; 32602 MW; 7BCEEDE3DB05DCED CRC64; MERSLRPNKL LAYHQLMRTD KPIGALLLLW PTLWALWVAA PGVPPLWILA VFVAGVWLMR AAGCVVNDYA DRKFDGHVKR TANRPLPSGA VSEKEARILF AVLVLLSFLL VLTLNTMTIL LSVAGLALAW VYPFMKRYTH LPQVVLGAAF GWSIPMAFAA VSESLPLSCW LMLLANILWA VAYDTQYAMV DRDDDVKIGI KSTAILFGEN DRLIIGILQA CVLVLMAVIG WLNGLHWEFY WSILIAGALF VYQQKLIRNR ERGPCFQAFL NNNYVGLVLF IGLAMSYWQF //