(data stored in SCRATCH zone)

SWISSPROT: Q751D7_ASHGO

ID   Q751D7_ASHGO            Unreviewed;       356 AA.
AC   Q751D7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 98.
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=4-hydroxybenzoate hexaprenyltransferase {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   Name=COQ2 {ECO:0000256|HAMAP-Rule:MF_03189};
GN   ORFNames=AGOS_AGL231W {ECO:0000313|EMBL:AAS54260.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54260.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54260.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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 coenzyme Q (CoQ) biosynthesis, which is the
CC       condensation of the polyisoprenoid side chain with PHB, generating the
CC       first membrane-bound Q intermediate. {ECO:0000256|HAMAP-Rule:MF_03189}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxybenzoate + an all-trans-polyprenyl diphosphate = a 4-
CC         hydroxy-3-all-trans-polyprenylbenzoate + diphosphate;
CC         Xref=Rhea:RHEA:44504, Rhea:RHEA-COMP:9514, Rhea:RHEA-COMP:9564,
CC         ChEBI:CHEBI:17879, ChEBI:CHEBI:33019, ChEBI:CHEBI:58914,
CC         ChEBI:CHEBI:78396; EC=2.5.1.39; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_03189};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03189};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03189}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03189}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03189}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03189}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000256|HAMAP-Rule:MF_03189}.
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DR   EMBL; AE016820; AAS54260.1; -; Genomic_DNA.
DR   RefSeq; NP_986436.1; NM_211498.1.
DR   STRING; 33169.AAS54260; -.
DR   EnsemblFungi; AAS54260; AAS54260; AGOS_AGL231W.
DR   GeneID; 4622729; -.
DR   KEGG; ago:AGOS_AGL231W; -.
DR   HOGENOM; HOG000003697; -.
DR   InParanoid; Q751D7; -.
DR   KO; K06125; -.
DR   OMA; WQIWTVD; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
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; Q751D7.
DR   SWISS-2DPAGE; Q751D7.
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:UP000000591};
KW   Transferase {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        150..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        294..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        336..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   REGION          118..140
FT                   /note="Allylic polyprenyl diphosphate-binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
SQ   SEQUENCE   356 AA;  38082 MW;  6386AB53F2CA8A93 CRC64;
     MLLSSGLCGL RSTGSGAGLR WGTAALSSGA ATRQAVFSAE QLAKAREDRQ RALGPYLSRL
     PARVVPYAEL MRLEKPVGTW LLYMPCSWAI TMAATQTAAP LASTAAMLGL FGAGALIMRG
     AGCTINDLLD RDLDNKVLRT VERPITSGRV SAGRAVAFLG AQTAAGIGIL ACLPAGCWWL
     GLASLPLVAT YPLFKRFTYY PQVALSACFT WGALLGFPAM GVLDWGTMVP LYLSSFLWCM
     TYDTIYAHQD KAFDIKAGIK STALRWGDRT RGICAGMATA QIGLLALAGA NSGLLLGPGF
     AAGLGIFAYR LYAMIRNVDL DSPADCWRWF QSNIRTGLYF SAALFCDYLL TIFGVM
//

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