UBIA_SACD2
ID UBIA_SACD2 Reviewed; 299 AA.
AC Q21DY7;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=Sde_3837;
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD83092.1; -; Genomic_DNA.
DR RefSeq; WP_011470307.1; NC_007912.1.
DR AlphaFoldDB; Q21DY7; -.
DR SMR; Q21DY7; -.
DR STRING; 203122.Sde_3837; -.
DR EnsemblBacteria; ABD83092; ABD83092; Sde_3837.
DR KEGG; sde:Sde_3837; -.
DR eggNOG; COG0382; Bacteria.
DR HOGENOM; CLU_034879_1_0_6; -.
DR OMA; MVVYPYG; -.
DR OrthoDB; 1472516at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000001947; 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..299
FT /note="4-hydroxybenzoate octaprenyltransferase"
FT /id="PRO_0000262832"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 105..125
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 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ SEQUENCE 299 AA; 33319 MW; 5F5B19EDD67CCA0A CRC64;
MTATRKSTRP SKPLKATLVA YAKLMRLDRP IGIYLVLWPT LWSLWIAADG LPDWDVLVIF
VLGVVLMRSA GCVINDFADR KIDGHVRRTA NRPLVTGLIT PKQAVLFFVA LLVIAFILVL
FTNPLTIKLS FGGALLAFCY PFMKRYTQLP QIVLGAAFAW SIPMAFAAQT NQLPEAIWVL
YTAVVLWTVA YDTFYAMADR EDDLKIGVKS TAILFGDQDR IITACLQLMA LVAMAMAGER
FGLGFSFKVS LLVAGGLFAY QQYLIRNREP NACFRAFLHN NWVGLVVFLG ILVDKLITN
