UBIA_VIBC3
ID UBIA_VIBC3 Reviewed; 284 AA.
AC A5F4H4; C3M2F0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 85.
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};
GN OrderedLocusNames=VC0395_A2421, VC395_0086;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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; CP000627; ABQ20837.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP08114.1; -; Genomic_DNA.
DR RefSeq; WP_000127681.1; NZ_JAACZH010000014.1.
DR AlphaFoldDB; A5F4H4; -.
DR SMR; A5F4H4; -.
DR STRING; 345073.VC395_0086; -.
DR EnsemblBacteria; ABQ20837; ABQ20837; VC0395_A2421.
DR GeneID; 57741401; -.
DR KEGG; vco:VC0395_A2421; -.
DR KEGG; vcr:VC395_0086; -.
DR PATRIC; fig|345073.21.peg.78; -.
DR eggNOG; COG0382; Bacteria.
DR HOGENOM; CLU_034879_1_0_6; -.
DR OMA; MVVYPYG; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000000249; Chromosome 2.
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; IPR044878; UbiA_sf.
DR PANTHER; PTHR11048; PTHR11048; 1.
DR Pfam; PF01040; UbiA; 1.
DR TIGRFAMs; TIGR01474; ubiA_proteo; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Magnesium; Membrane; Transferase;
KW Transmembrane; Transmembrane helix; Ubiquinone biosynthesis.
FT CHAIN 1..284
FT /note="4-hydroxybenzoate octaprenyltransferase"
FT /id="PRO_1000073654"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ SEQUENCE 284 AA; 31820 MW; 4F9697774C36CAC6 CRC64;
MTAVKARAYW QLMRMDRPIG SLLLLWPTLW ALLLAAQGLP DLRVLVVFVL GVFLMRSAGC
VINDYADRHV DGHVKRTSQR PLPAGLVSAK EALLLFVLLA VSSFLLVLTM NTLTIQLSFI
GILLAFVYPF MKRFTHLPQL VLGLAFSWSI PMAWAAQANT LTPQVWVLFL INALWTIAYD
TQYAMVDRDD DVKIGIKSTA ILFGRWDKRI IGLLQLATLS LLVALGQGLA LGTSYYWGLL
IAAGLFAYQQ HLIRYRERMP CFQAFLNNNY VGMAITAGIL LSVW
