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UBIA_PSYA2
ID   UBIA_PSYA2              Reviewed;         307 AA.
AC   Q4FR08;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=Psyc_1702;
OS   Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=259536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX   PubMed=20154119; DOI=10.1128/aem.02101-09;
RA   Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA   Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA   Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA   Murray A., Thomashow M., Tiedje J.M.;
RT   "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT   Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT   temperature growth.";
RL   Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19550.1; -; Genomic_DNA.
DR   RefSeq; WP_011280964.1; NC_007204.1.
DR   AlphaFoldDB; Q4FR08; -.
DR   SMR; Q4FR08; -.
DR   STRING; 259536.Psyc_1702; -.
DR   EnsemblBacteria; AAZ19550; AAZ19550; Psyc_1702.
DR   KEGG; par:Psyc_1702; -.
DR   eggNOG; COG0382; Bacteria.
DR   HOGENOM; CLU_034879_1_0_6; -.
DR   OMA; MVVYPYG; -.
DR   OrthoDB; 1472516at2; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000546; 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; 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;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubiquinone biosynthesis.
FT   CHAIN           1..307
FT                   /note="4-hydroxybenzoate octaprenyltransferase"
FT                   /id="PRO_0000262826"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        48..68
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        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01635"
SQ   SEQUENCE   307 AA;  33908 MW;  2FE215BD993FB69A CRC64;
     MTFNDKLQAY IQLTRFDKPV GIELLLWPTL WGVLFAAMGQ AQQQGEGVTA GLPSLSIFVV
     FALGAILMRA AGCAINDFAD RKVDGHVSRT KGRPLADGRL SAKEAIAAFL VLVLLSASLL
     LFLPIQVFYW SFAAVILAFI YPFMKRYTHL PQVFLAAAFG WAIPMAYVAI QGAADIWCWL
     LFLAYMCWTV AYDTQYAMAD RDDDVKIGVK STAILFGRYD VIIISLLQIL FLVIMGAVMW
     HYFVPTSLGI TPVFGLALVA MMFAKQNSAC ASRNALACFQ AFLANIWVGR YVFALIAIAC
     VWTTFNG
 
 
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