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PYR6_ASPFU
ID   PYR6_ASPFU              Reviewed;         320 AA.
AC   Q4WLD0;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Polyprenyl transferase pyr6 {ECO:0000303|PubMed:20861902};
DE            EC=2.5.1.- {ECO:0000269|PubMed:20861902};
DE   AltName: Full=Pyripyropene synthesis protein 6 {ECO:0000303|PubMed:20861902};
GN   Name=pyr6 {ECO:0000303|PubMed:20861902}; ORFNames=AFUA_6G13980;
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;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
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.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=8534106; DOI=10.1128/aem.61.12.4429-4435.1995;
RA   Wang H.J., Gloer J.B., Wicklow D.T., Dowd P.F.;
RT   "Aflavinines and other antiinsectan metabolites from the ascostromata of
RT   Eupenicillium crustaceum and related species.";
RL   Appl. Environ. Microbiol. 61:4429-4435(1995).
RN   [3]
RP   BIOTECHNOLOGY.
RX   PubMed=18997389; DOI=10.1038/ja.2008.67;
RA   Ohshiro T., Ohte S., Matsuda D., Ohtawa M., Nagamitsu T., Sunazuka T.,
RA   Harigaya Y., Rudel L.L., Omura S., Tomoda H.;
RT   "Selectivity of pyripyropene derivatives in inhibition toward acyl-
RT   CoA:cholesterol acyltransferase 2 isozyme.";
RL   J. Antibiot. 61:503-508(2008).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=19571395; DOI=10.1248/bpb.32.1261;
RA   Hayashi A., Arai M., Fujita M., Kobayashi M.;
RT   "Pyripyropenes, fungal sesquiterpenes conjugated with alpha-pyrone and
RT   pyridine moieties, exhibits anti-angiogenic activity against human
RT   umbilical vein endothelial cells.";
RL   Biol. Pharm. Bull. 32:1261-1265(2009).
RN   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20861902; DOI=10.1038/nchem.764;
RA   Itoh T., Tokunaga K., Matsuda Y., Fujii I., Abe I., Ebizuka Y., Kushiro T.;
RT   "Reconstitution of a fungal meroterpenoid biosynthesis reveals the
RT   involvement of a novel family of terpene cyclases.";
RL   Nat. Chem. 2:858-864(2010).
RN   [6]
RP   FUNCTION.
RX   PubMed=21224862; DOI=10.1038/ja.2010.162;
RA   Hu J., Okawa H., Yamamoto K., Oyama K., Mitomi M., Anzai H.;
RT   "Characterization of two cytochrome P450 monooxygenase genes of the
RT   pyripyropene biosynthetic gene cluster from Penicillium coprobium.";
RL   J. Antibiot. 64:221-227(2011).
RN   [7]
RP   FUNCTION.
RX   PubMed=26019565; DOI=10.1080/13102818.2014.960140;
RA   Hu J., Furutani A., Yamamoto K., Oyama K., Mitomi M., Anzai H.;
RT   "Characterization of two acetyltransferase genes in the pyripyropene
RT   biosynthetic gene cluster from Penicillium coprobium.";
RL   Biotechnol. Biotechnol. Equip. 28:818-826(2014).
CC   -!- FUNCTION: Polyprenyl transferase; part of the gene cluster that
CC       mediates the biosynthesis of pyripyropene A, a specific human acyl-
CC       coenzyme A:cholesterol acyltransferase 2 inhibitor (PubMed:20861902).
CC       The first step of the pathway is the synthesis of nicotinyl-CoA from
CC       nicotinic acid by the nicotinic acid-CoA ligase pyr1 (PubMed:20861902).
CC       Nicotinyl-CoA is then a substrate of polyketide synthase pyr2 to
CC       produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is
CC       further prenylated by the polyprenyl transferase pyr6 to yield
CC       farnesyl-HPPO (PubMed:20861902). The next steps consist of an
CC       epoxidation of farnesyl-HPPO to epoxyfarnesyl-HPPO by FAD-dependent
CC       monooxygenase pyr5 and a cyclization of the terpenoid portion by the
CC       terpene cyclase pyr4 to yield deacetyl-pyripyropene E
CC       (PubMed:20861902). The 2 cytochrome P450 monooxygenases pyr3 and pyr9,
CC       and the 2 acetyltransferases pyr7 and pyr8 are involved in the
CC       conversion of deacetyl-pyripyropene E into pyripyropene A through
CC       several cycles of oxidation and acetylation steps (PubMed:20861902).
CC       Pyr7 acetylates deacetyl-pyripyropene E to pyripyropene E which is
CC       oxidized to 11-deacetyl-pyripyropene O by pyr3, which is in turn
CC       acetylated into pyripyropene O by pyr8 (PubMed:21224862,
CC       PubMed:26019565). Pyripyropene O is then oxidized to deacetyl-
CC       pyripyropene A by pyr9 (PubMed:21224862). Deacetyl-pyripyropene A is
CC       finally acetylated to pyripyropene A by pyr8 (PubMed:26019565).
CC       {ECO:0000269|PubMed:20861902, ECO:0000305|PubMed:21224862,
CC       ECO:0000305|PubMed:26019565}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 4-hydroxy-6-(pyridin-3-yl)-2H-
CC         pyran-2-one = 4-hydroxy-3-[(2E,6E)-farnesyl]-6-(pyridin-3-yl)-2H-
CC         pyran-2-one + diphosphate; Xref=Rhea:RHEA:64340, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:149707, ChEBI:CHEBI:149708, ChEBI:CHEBI:175763;
CC         Evidence={ECO:0000269|PubMed:20861902};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64341;
CC         Evidence={ECO:0000269|PubMed:20861902};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P32378};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:20861902}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: Pyripyropene A and its derivatives have very unique
CC       characteristics of selectively inhibiting the acyl-coenzyme
CC       A:cholesterol acyltransferase 2 (ACAT2) isozyme (PubMed:18997389).
CC       Therefore, pyripyropenes are expected to be developed as a new type of
CC       anti-atherosclerotic agent (PubMed:18997389). Furthermore,
CC       pyripyropenes have been shown to exhibit anti-angiogenic activity
CC       against human umbilical vein endothelial cells (PubMed:19571395).
CC       Finally, pyripyropene A also exhibits insecticidal properties
CC       (PubMed:8534106). {ECO:0000269|PubMed:18997389,
CC       ECO:0000269|PubMed:19571395, ECO:0000269|PubMed:8534106}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AAHF01000006; EAL89234.2; -; Genomic_DNA.
DR   RefSeq; XP_751272.2; XM_746179.2.
DR   AlphaFoldDB; Q4WLD0; -.
DR   SMR; Q4WLD0; -.
DR   STRING; 746128.CADAFUBP00000076; -.
DR   EnsemblFungi; EAL89234; EAL89234; AFUA_6G13980.
DR   GeneID; 3508588; -.
DR   KEGG; afm:AFUA_6G13980; -.
DR   VEuPathDB; FungiDB:Afu6g13980; -.
DR   eggNOG; KOG1381; Eukaryota.
DR   HOGENOM; CLU_075330_0_0_1; -.
DR   InParanoid; Q4WLD0; -.
DR   OMA; HENGSAW; -.
DR   OrthoDB; 1343847at2759; -.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
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:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IBA:GO_Central.
DR   CDD; cd13959; PT_UbiA_COQ2; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   InterPro; IPR039653; Prenyltransferase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR11048; PTHR11048; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..320
FT                   /note="Polyprenyl transferase pyr6"
FT                   /id="PRO_0000436759"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   320 AA;  35777 MW;  644B008280034C62 CRC64;
     MATAQSPTQL VRTLIDVSRF DKYNCLFAIF PGVWSIFLAA ASRHADGVHL PSDWVLGRAG
     LAFAYTYLLS GAGMVWNDWI DRDIDAQVAR TKNRPLASGR LATRAAIIWM LVQYAASVWL
     MDRMLSGQNL WTFMLPLTTG IILYPFGKRP TTRKLGIYPQ YILGASSALT ILPAWASVYG
     DSVAPPDLLA KCLPLCVFLF LWTIYFNTAY SYQDVKDDCR LSVNSSYVLA GQYVHGLLLL
     QAVAVVMVIP WILHENGSAW LWFSWLGVWT AALAEQLYLF DTKDPSTGGR VHRRNFALGI
     WNVLACFVEL LLVSGSLDMF
 
 
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