(data stored in SCRATCH zone)

SWISSPROT: A1AZP3_PARDP

ID   A1AZP3_PARDP            Unreviewed;       323 AA.
AC   A1AZP3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   RecName: Full=4-hydroxybenzoate octaprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS01075854};
DE            EC=2.5.1.- {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS00336940};
DE   AltName: Full=4-HB polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_01635};
GN   Name=ubiA {ECO:0000256|HAMAP-Rule:MF_01635};
GN   OrderedLocusNames=Pden_0625 {ECO:0000313|EMBL:ABL68737.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68737.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB)
CC       with an all-trans polyprenyl group. Mediates the second step in
CC       the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis,
CC       which is the condensation of the polyisoprenoid side chain with
CC       PHB, generating the first membrane-bound Q intermediate 3-
CC       octaprenyl-4-hydroxybenzoate. {ECO:0000256|HAMAP-Rule:MF_01635,
CC       ECO:0000256|SAAS:SAAS01075872}.
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;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01635,
CC         ECO:0000256|SAAS:SAAS01114937};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01635, ECO:0000256|SAAS:SAAS01075861};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS01075851}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01635, ECO:0000256|SAAS:SAAS01075873}; Multi-pass membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_01635,
CC       ECO:0000256|SAAS:SAAS01075873}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01635, ECO:0000256|SAAS:SAAS01159762}.
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DR   EMBL; CP000489; ABL68737.1; -; Genomic_DNA.
DR   RefSeq; WP_011746970.1; NC_008686.1.
DR   STRING; 318586.Pden_0625; -.
DR   PRIDE; A1AZP3; -.
DR   EnsemblBacteria; ABL68737; ABL68737; Pden_0625.
DR   KEGG; pde:Pden_0625; -.
DR   eggNOG; ENOG4105C4G; Bacteria.
DR   eggNOG; COG0382; LUCA.
DR   HOGENOM; HOG000003697; -.
DR   KO; K03179; -.
DR   OMA; WTLGFDT; -.
DR   BioCyc; PDEN318586:G1GW1-632-MONOMER; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000361; Chromosome 1.
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:0008412; F:4-hydroxybenzoate octaprenyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
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   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;
DR   PRODOM; A1AZP3.
DR   SWISS-2DPAGE; A1AZP3.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS01075859};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS01075855};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS01075847};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00181105};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00181134, ECO:0000313|EMBL:ABL68737.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00181127};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS00181088};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_01635,
KW   ECO:0000256|SAAS:SAAS01075866}.
FT   TRANSMEM     49     69       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    135    162       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    174    190       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    196    213       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    244    262       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
FT   TRANSMEM    268    286       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01635}.
SQ   SEQUENCE   323 AA;  34662 MW;  B5323809D23EAFE2 CRC64;
     MQTDHRTPEG PTPEGPSTVA DAPPDNWVDR YAPPDWRPWL RLSRADRPIG TWLLLLPCWW
     GIGLAMIAGS PGWRDLWIAV ACGVGAVLMR GAGCTWNDIT DRDIDDKVAR TRSRPIPSGQ
     VTVRGAMVWL VAQSLAGFAI LLTLGGAAIA LGVASLLLVA IYPFAKRFTW WPQLFLGLAF
     NWGVLLAWAA HMGNLAPAPV LAYLAGIAWT IFYDTIYAHQ DAEDDALIGV KSTARLFGRD
     TPRWLAGFGT ASVLLLGLAV MAAAPEGLGL TLGLLGVAGF AAHLAWQLRQ FDMADGAGCL
     RLFRSNRDAG LVVALFLALA GLV
//

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