PYNF_ASPNC
ID PYNF_ASPNC Reviewed; 434 AA.
AC A5ABG1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=MFS-type transporter pynF {ECO:0000303|PubMed:24106156};
DE AltName: Full=Pyranonigrins biosynthesis cluster protein F {ECO:0000303|PubMed:24106156};
GN Name=pynF {ECO:0000303|PubMed:24106156}; ORFNames=An11g00260;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, AND INDUCTION.
RX PubMed=24106156; DOI=10.1002/cbic.201300430;
RA Awakawa T., Yang X.L., Wakimoto T., Abe I.;
RT "Pyranonigrin E: a PKS-NRPS hybrid metabolite from Aspergillus niger
RT identified by genome mining.";
RL ChemBioChem 14:2095-2099(2013).
RN [3]
RP FUNCTION.
RX PubMed=26414728; DOI=10.1021/acs.orglett.5b02435;
RA Yamamoto T., Tsunematsu Y., Noguchi H., Hotta K., Watanabe K.;
RT "Elucidation of pyranonigrin biosynthetic pathway reveals a mode of
RT tetramic acid, fused gamma-pyrone, and exo-methylene formation.";
RL Org. Lett. 17:4992-4995(2015).
CC -!- FUNCTION: MFS-type transporter; part of the gene cluster that mediates
CC the biosynthesis of pyranonigrins, a family of antioxidative compounds
CC (PubMed:24106156, PubMed:26414728). May be involved in the secretion of
CC pyranonigrins (Probable). {ECO:0000269|PubMed:24106156,
CC ECO:0000269|PubMed:26414728, ECO:0000305|PubMed:24106156}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor pynR. {ECO:0000269|PubMed:24106156}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR EMBL; AM270218; CAK48259.1; -; Genomic_DNA.
DR RefSeq; XP_001394030.1; XM_001393993.1.
DR AlphaFoldDB; A5ABG1; -.
DR SMR; A5ABG1; -.
DR PaxDb; A5ABG1; -.
DR EnsemblFungi; CAK48259; CAK48259; An11g00260.
DR GeneID; 4984232; -.
DR KEGG; ang:ANI_1_1530094; -.
DR VEuPathDB; FungiDB:An11g00260; -.
DR HOGENOM; CLU_001265_1_1_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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 GO; GO:0019748; P:secondary metabolic process; IGC:AspGD.
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; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..434
FT /note="MFS-type transporter pynF"
FT /id="PRO_0000450059"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 434 AA; 46649 MW; C814B5AEC6DCCE45 CRC64;
MSHDQRSPSE EVSRTALSKP ASESTIVGDG HHPLPAKDTS TRAWLVVVGG LLIYFPTFGF
LNAFGTFQTF YVQDLLAGTS SSKIAWIGSL QIFLLFIGGL VVGPLYDKVG ATKLLVPGSV
VYVVALMLTS VCKKYYQLIL AQGILFGCAN ALLFYPTIAA INQWFDRRRG IALGLAVSGS
SLGGIFWTEI IQLMLDHIGF GWTVRACGFI SLAFLVPSCV LIITRPPEPG ESKDMQLDFK
AIFTDTKYLL FSVGMLLVLW GMFIPFFYLP SYGETYGMSV TGANNLLAYM NAGSFVGRVL
TGLMADRLGR FNVISLAALS CGILLFCLHK ITTSGAIIAF STLYGICSGG LISLQSACIG
QITPDHSIIG VKIGLMMGFC SVGGLTGSPI AGALLSADHQ KWYGFIDFCG SILMGGAVVT
ILSRYVAAPR EWKF
