(data stored in SCRATCH zone)

SWISSPROT: Q4WNJ5_ASPFU

ID   Q4WNJ5_ASPFU            Unreviewed;       419 AA.
AC   Q4WNJ5;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 81.
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=AFUA_4G05970 {ECO:0000313|EMBL:EAL90189.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90189.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90189.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL90189.1}.
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DR   EMBL; AAHF01000005; EAL90189.1; -; Genomic_DNA.
DR   RefSeq; XP_752227.1; XM_747134.1.
DR   STRING; 746128.CADAFUBP00006132; -.
DR   EnsemblFungi; EAL90189; EAL90189; AFUA_4G05970.
DR   GeneID; 3508872; -.
DR   KEGG; afm:AFUA_4G05970; -.
DR   EuPathDB; FungiDB:Afu4g05970; -.
DR   HOGENOM; HOG000003697; -.
DR   InParanoid; Q4WNJ5; -.
DR   KO; K06125; -.
DR   OMA; WQIWTVD; -.
DR   OrthoDB; 1343847at2759; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000002530; Chromosome 4.
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; Q4WNJ5.
DR   SWISS-2DPAGE; Q4WNJ5.
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:UP000002530};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03189, ECO:0000313|EMBL:EAL90189.1};
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        130..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        154..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        253..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        329..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        353..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   TRANSMEM        383..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
FT   REGION          71..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..190
FT                   /note="Allylic polyprenyl diphosphate-binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03189"
SQ   SEQUENCE   419 AA;  45658 MW;  9A93B9CCE4D469FF CRC64;
     MRLQFSYLPP VRLDQLSRRY GSGSSLLNDK RHRLLCNRNS LTTSSRVNST GRQSAYTAKP
     RSAITKRTSL MRCQPHSSQS PSSTDRPAAI TDNNPATHYI PPQKGFIASL PGSWIPYAEL
     IRLDKPTGTY YLFFPCVFST LIAAPMASAT PMQILGTTGL FFTGALIMRG AGCAINDLWD
     RNLDPYVERT KFRPIARGAL SPKKALVFTC SQLLAGLAVL LQFPSQCLWY GIPSLLLVTT
     YPLAKRVTYY PQAVLGLTFS WGAIMGFPAL GVDLFSNHAA LEAAAALYSS CVAWTVLYDM
     IYAHMDIKDD VAAGIKSIAL RHEHNTKTVL SGLAAVQVAL LATAGVAAGA GPLFYVGTCG
     SAAVSLGIMI WKVQLKNVKN CWWWFKNGCL LTGGGITLGM FFEYIAQTTG LYKSDNNLH
//

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