UBIA_POLAQ
ID UBIA_POLAQ Reviewed; 287 AA.
AC A4SZT5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Pnuc_1786;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34999.1; -; Genomic_DNA.
DR RefSeq; WP_011903622.1; NC_009379.1.
DR AlphaFoldDB; A4SZT5; -.
DR SMR; A4SZT5; -.
DR STRING; 312153.Pnuc_1786; -.
DR EnsemblBacteria; ABP34999; ABP34999; Pnuc_1786.
DR GeneID; 31482175; -.
DR KEGG; pnu:Pnuc_1786; -.
DR eggNOG; COG0382; Bacteria.
DR HOGENOM; CLU_034879_1_0_4; -.
DR OMA; MVVYPYG; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000231; 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; Transferase;
KW Transmembrane; Transmembrane helix; Ubiquinone biosynthesis.
FT CHAIN 1..287
FT /note="4-hydroxybenzoate octaprenyltransferase"
FT /id="PRO_0000336982"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 118..138
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 209..229
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 263..283
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ SEQUENCE 287 AA; 31927 MW; AC399337609ABA16 CRC64;
MSLKERFTSY AYLIRLDKPI GTLLLLWPTL WALWLASSGT PSLQMLMIFI AGTFLMRSAG
CAINDYADRD FDRHVQRTKH RPVTSGKISG KEAVVVAGVL ALIAFLLIQP LNIFTKELSV
LALLVAFIYP FTKRFLAIPQ AVLGIAFGFG IPMAYAAVLD FIPLEAWVLF VGNIFWAIAY
DTAYAMVDRD DDLRLGLRTS AITFGSYEVL AIAFSYGVLF VSQLWVAHLA SLSNYFLIGW
GAALGCAIYQ LKLVSSRKRE DCFLAFRHNN WLGGFLFLGI VLGLSIQ
