UBIA_YERPB
ID UBIA_YERPB Reviewed; 288 AA.
AC B2K1U4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=YPTS_0390;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) 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 ---------------------------------------------------------------------------
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; CP001048; ACC87379.1; -; Genomic_DNA.
DR RefSeq; WP_012413438.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K1U4; -.
DR SMR; B2K1U4; -.
DR KEGG; ypb:YPTS_0390; -.
DR PATRIC; fig|502801.10.peg.4068; -.
DR OMA; MVVYPYG; -.
DR BioCyc; YPSE502801:YPTS_RS02050-MON; -.
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..288
FT /note="4-hydroxybenzoate octaprenyltransferase"
FT /id="PRO_1000186701"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 141..161
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 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ SEQUENCE 288 AA; 32310 MW; 73C7ADA48EBF75BB CRC64;
MKGSTVHTKW QAYCRLMRID KPIGSLLLLW PTLWALWLAG RGIPEAKILV VFVLGVFFMR
AAGCVVNDYA DRHIDSFVKR TASRPLPSGT ISEKESKILF VVLILLSFGL VLTLNSMTIW
LSLAALALAW IYPFMKRVTH LPQVVLGAAF GWSIPMGFAA VSESLPLVCW LLLLANICWT
VAYDTQYAMV DRDDDLRIGV KSTAILFGQH DKLIIGLLQL ATLLLMVAIG WLMNLGGAFY
WSILLAGALF THQQKMIAQR EREPCFRAFL NNNYVGLVLF LGILISYW