位置:首页 > 蛋白库 > AURT_GIBZE
AURT_GIBZE
ID   AURT_GIBZE              Reviewed;         544 AA.
AC   I1RF56;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Rubrofusarin-specific efflux pump aurT {ECO:0000303|PubMed:16879655};
DE   AltName: Full=Aurofusarin biosynthesis cluster protein T {ECO:0000303|PubMed:16879655};
DE   AltName: Full=Gibberella pigment protein 4 {ECO:0000303|PubMed:16461721};
GN   Name=aurT {ECO:0000303|PubMed:16879655};
GN   Synonyms=GIP4 {ECO:0000303|PubMed:16461721};
GN   ORFNames=FG02322, FGRAMPH1_01T05589;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
RN   [4]
RP   FUNCTION.
RX   PubMed=15811992; DOI=10.1128/aem.71.4.1701-1708.2005;
RA   Kim J.E., Han K.H., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT   "Putative polyketide synthase and laccase genes for biosynthesis of
RT   aurofusarin in Gibberella zeae.";
RL   Appl. Environ. Microbiol. 71:1701-1708(2005).
RN   [5]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=15809006; DOI=10.1016/j.fgb.2005.01.010;
RA   Malz S., Grell M.N., Thrane C., Maier F.J., Rosager P., Felk A.,
RA   Albertsen K.S., Salomon S., Bohn L., Schaefer W., Giese H.;
RT   "Identification of a gene cluster responsible for the biosynthesis of
RT   aurofusarin in the Fusarium graminearum species complex.";
RL   Fungal Genet. Biol. 42:420-433(2005).
RN   [6]
RP   FUNCTION, INDUCTION, AND PATHWAY.
RX   PubMed=16879655; DOI=10.1111/j.1365-2958.2006.05295.x;
RA   Frandsen R.J., Nielsen N.J., Maolanon N., Soerensen J.C., Olsson S.,
RA   Nielsen J., Giese H.;
RT   "The biosynthetic pathway for aurofusarin in Fusarium graminearum reveals a
RT   close link between the naphthoquinones and naphthopyrones.";
RL   Mol. Microbiol. 61:1069-1080(2006).
RN   [7]
RP   INDUCTION.
RX   PubMed=16461721; DOI=10.1128/aem.72.2.1645-1652.2006;
RA   Kim J.E., Jin J., Kim H., Kim J.C., Yun S.H., Lee Y.W.;
RT   "GIP2, a putative transcription factor that regulates the aurofusarin
RT   biosynthetic gene cluster in Gibberella zeae.";
RL   Appl. Environ. Microbiol. 72:1645-1652(2006).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=21296881; DOI=10.1074/jbc.m110.179853;
RA   Frandsen R.J., Schuett C., Lund B.W., Staerk D., Nielsen J., Olsson S.,
RA   Giese H.;
RT   "Two novel classes of enzymes are required for the biosynthesis of
RT   aurofusarin in Fusarium graminearum.";
RL   J. Biol. Chem. 286:10419-10428(2011).
RN   [9]
RP   FUNCTION.
RX   PubMed=23557488; DOI=10.1186/1475-2859-12-31;
RA   Rugbjerg P., Naesby M., Mortensen U.H., Frandsen R.J.;
RT   "Reconstruction of the biosynthetic pathway for the core fungal polyketide
RT   scaffold rubrofusarin in Saccharomyces cerevisiae.";
RL   Microb. Cell Fact. 12:31-31(2013).
CC   -!- FUNCTION: Rubrofusarin-specific efflux pump; part of the gene cluster
CC       that mediates the biosynthesis of aurofusarin, a red mycelium pigment
CC       which is acting as a mycotoxin (PubMed:15811992, PubMed:15809006,
CC       PubMed:16879655). The first step is performed by the polyketide
CC       synthase which condenses one acetyl-CoA and 6 malonyl-CoA units to form
CC       the first intermediate, the cyclic heptaketide and yellow pigment YWA1
CC       (PubMed:21296881, PubMed:23557488). The C2 hydroxyl group in the pyrone
CC       ring of YWA1 is probably formed during ring closure by an aldol-type
CC       cyclization reaction (PubMed:21296881). The dehydratase aurZ then acts
CC       as the first tailoring enzyme in the aurofusarin biosynthetic pathway
CC       by converting YWA1 to nor-rubrofusarin (PubMed:21296881,
CC       PubMed:23557488). Nor-rubrofusarin is then methylated to rubrofusarin
CC       by the O-methyltransferase aurJ (PubMed:21296881, PubMed:23557488).
CC       Rubrofusarin is then transported across the plasma membrane by the
CC       rubrofusarin-specific pump aurT for further enzymatic processing by the
CC       extracellular complex composed of GIP1, aurF, aurO and aurS to yield
CC       aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:15809006,
CC       ECO:0000269|PubMed:15811992, ECO:0000269|PubMed:16879655,
CC       ECO:0000269|PubMed:21296881, ECO:0000269|PubMed:23557488}.
CC   -!- PATHWAY: Pigment biosynthesis. {ECO:0000269|PubMed:15809006,
CC       ECO:0000269|PubMed:16879655, ECO:0000269|PubMed:21296881}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21296881};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- INDUCTION: Expression is regulated by the aurofusarin biosynthesis
CC       cluster-specific transcription factor aurR1/GIP2 (PubMed:16879655,
CC       PubMed:16461721). {ECO:0000269|PubMed:16461721,
CC       ECO:0000269|PubMed:16879655}.
CC   -!- DISRUPTION PHENOTYPE: Leads to pink mycelia in young cultures which
CC       turn red in older cultures, suggesting a delayed production of
CC       aurofusarin (PubMed:21296881). {ECO:0000269|PubMed:21296881}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. TCR/Tet
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HG970332; CEF74599.1; -; Genomic_DNA.
DR   RefSeq; XP_011318231.1; XM_011319929.1.
DR   AlphaFoldDB; I1RF56; -.
DR   SMR; I1RF56; -.
DR   STRING; 5518.FGSG_02322P0; -.
DR   GeneID; 23549704; -.
DR   KEGG; fgr:FGSG_02322; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G05589; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   HOGENOM; CLU_000960_22_1_1; -.
DR   InParanoid; I1RF56; -.
DR   Proteomes; UP000070720; 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:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..544
FT                   /note="Rubrofusarin-specific efflux pump aurT"
FT                   /id="PRO_0000441089"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        514..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   544 AA;  58460 MW;  0A6934D48CACEADB CRC64;
     MTDNTDMEKL DRATTPTPIP NEAPPTSEPS ESKPEEAEDE SKYPHGLKLA AIILSNMVAM
     FLVALDRTII ATAIPRITDD FNALGDISWY ASAYLITSSA TQLLWGRIFT FYPTKTVYLV
     AIFFFELGSL LCGVAPNSVA FIIGRAIAGA GSAGIYSGST ILITTVTPLS KRAGYVGMMG
     AVFGIASVIA PLIGGAFTDH VTWRWCFYIN LPVGGAAVAC LILLFPKFPV NEPVSVKQQI
     KQLDPWGNLV FLPGVICLIL ALQWGGEKYA WDSGRIVALL VLACVLLLVF IGIQIWQQEN
     ATVPPRLFKI RNVWLGTIFA FCLGSVLIVF LIALPIWFQG IRGTDAITSG IDTLPLVLSL
     VFGAIVSGGV INGVGWFNPV FFSSVIFMSV GGGLITTFVV DTPTRTWIGY QIILGLGIGQ
     GMQLASLGTQ VAVKQSDVPT GVSLMFFAQS LGGSVLVCVA QAVFNNELRS RLTSFDGIDV
     ARIIGTGATQ LRHVIPADRL AEVLVEYNAA LRSYFYVGLA AACFAVLPSL GIEWKNVKGQ
     EFVH
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024