(data stored in ACNUC8465 zone)

SWISSPROT: B6HF35_PENRW

ID   B6HF35_PENRW            Unreviewed;       418 AA.
AC   B6HF35;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   RecName: Full=4-hydroxybenzoate polyprenyltransferase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03189};
DE            Short=4-HB polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_03189};
DE            EC=2.5.1.39 {ECO:0000256|HAMAP-Rule:MF_03189};
DE   AltName: Full=Para-hydroxybenzoate--polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_03189};
DE            Short=PHB:PPT {ECO:0000256|HAMAP-Rule:MF_03189};
DE            Short=PHB:polyprenyltransferase {ECO:0000256|HAMAP-Rule:MF_03189};
GN   ORFNames=Pc20g00240 {ECO:0000313|EMBL:CAP85353.1}, PCH_Pc20g00240
GN   {ECO:0000313|EMBL:CAP85353.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85353.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85353.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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 coenzyme Q (CoQ) biosynthesis,
CC       which is the condensation of the polyisoprenoid side chain with
CC       PHB, generating the first membrane-bound Q intermediate.
CC       {ECO:0000256|HAMAP-Rule:MF_03189}.
CC   -!- CATALYTIC ACTIVITY: A polyprenyl diphosphate + 4-hydroxybenzoate =
CC       diphosphate + a 4-hydroxy-3-polyprenylbenzoate.
CC       {ECO:0000256|HAMAP-Rule:MF_03189}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03189};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03189}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000256|HAMAP-Rule:MF_03189}; Multi-pass membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000256|HAMAP-
CC       Rule:MF_03189}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03189}.
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DR   EMBL; AM920435; CAP85353.1; -; Genomic_DNA.
DR   RefSeq; XP_002562588.1; XM_002562542.1.
DR   STRING; 500485.XP_002562588.1; -.
DR   EnsemblFungi; CAP85353; CAP85353; PCH_Pc20g00240.
DR   GeneID; 8307682; -.
DR   KEGG; pcs:Pc20g00240; -.
DR   eggNOG; KOG1381; Eukaryota.
DR   eggNOG; COG0382; LUCA.
DR   HOGENOM; HOG000003697; -.
DR   KO; K06125; -.
DR   OMA; WSITMAS; -.
DR   OrthoDB; EOG092C2KJ8; -.
DR   BioCyc; PCHR:PC20G00240-MONOMER; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-HAMAP.
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:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01635; UbiA; 1.
DR   InterPro; IPR031103; HB_octoprenylTrfase.
DR   InterPro; IPR006370; HB_polyprenyltransferase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   Pfam; PF01040; UbiA; 1.
DR   TIGRFAMs; TIGR01474; ubiA_proteo; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6HF35.
DR   SWISS-2DPAGE; B6HF35.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Transit peptide {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03189};
KW   Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03189}.
FT   TRANSMEM    122    145       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03189}.
FT   TRANSMEM    220    236       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03189}.
FT   TRANSMEM    245    266       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03189}.
FT   TRANSMEM    272    290       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03189}.
FT   TRANSMEM    320    339       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03189}.
FT   TRANSMEM    345    363       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03189}.
FT   TRANSMEM    375    394       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_03189}.
FT   REGION      160    182       Allylic polyprenyl diphosphate-binding
FT                                site. {ECO:0000256|HAMAP-Rule:MF_03189}.
SQ   SEQUENCE   418 AA;  45094 MW;  B7ABCCE7BF8CD067 CRC64;
     MLSTSSRLLR ARLSPYRQKV NLTGLYNGRL PTFAHNAYSP TQLKDPRFLA SGSSIALRTT
     QVQVRHSSQL QSPATQPTET DSAEKNPATH YILPKTGLIA SLPSSWIPYA ELVRLDKPTG
     TYYLFFPTLF STLLAAPMAG AAPLHVLGTS ALFFSGALIM RGAGCAINDL WDRNLDPHVE
     RTKFRPIARG ALSPKNAILF TGSQLVAGLG VLLSFPTQCL WYGIPSLPIV VAYPLAKRVT
     NYPQAVLGLA FSWGAIMGFP ALGVDLLANH DALMAAGALY SSCIAWTVLY DMIYAHMDIK
     DDVKAGIKSI ALRHEHNTKA VLSGLAVTQV SLLAAAGVAA GCGPVFFVGS CGSAVLSLGL
     MIWKVQLKNV RNCWWWFRNG CLLTGGGISL GLFAEYATQY LGLYNTTEPE RVVAESTQ
//

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