FGND_ASPFU
ID FGND_ASPFU Reviewed; 496 AA.
AC Q4WKX2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=FAD-linked oxidoreductase AFUA_1G00980 {ECO:0000303|PubMed:32083553};
DE EC=1.-.-.- {ECO:0000305|PubMed:32083553};
DE AltName: Full=Fumigermin biosynthesis cluster protein AFUA_1G00980 {ECO:0000303|PubMed:32083553};
DE Flags: Precursor;
GN ORFNames=AFUA_1G00980;
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 FUNCTION, AND INDUCTION.
RX PubMed=32083553; DOI=10.7554/elife.52541;
RA Stroe M.C., Netzker T., Scherlach K., Krueger T., Hertweck C., Valiante V.,
RA Brakhage A.A.;
RT "Targeted induction of a silent fungal gene cluster encoding the bacteria-
RT specific germination inhibitor fumigermin.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: FAD-linked oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of fumigermin that inhibits germination of
CC spores of the inducing S.rapamycinicus, and thus helps the fungus to
CC defend resources in the shared habitat against a bacterial competitor
CC (PubMed:32083553). The partially reducing polyketide synthase fngA
CC alone is sufficient for the production of fumigermin (PubMed:32083553).
CC FgnA catalyzes the condensation of 3 malonyl-CoA units to an acetyl-CoA
CC starter, and 3 methylations to yield fumigermin (PubMed:32083553). It
CC is remarkable that the five cluster genes including fgnA are conserved
CC in distantly related fungi, supporting the assumption of a fumigermin
CC cluster; it is thus possible that originally all five genes were
CC functional, but that the genes encoding tailoring enzymes became
CC inactive from mutations, similar to the case of the fgnA gene in
CC strains A1163 and Af293 (Probable). {ECO:0000269|PubMed:32083553,
CC ECO:0000305|PubMed:32083553}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q5BEJ5};
CC -!- INDUCTION: Expression is up-regulated during co-cultivation of
CC A.fumigatus with Streptomyces rapamycinicus that triggersthe production
CC of the polyketide fumigermin during the bacterial-fungal interaction.
CC {ECO:0000269|PubMed:32083553}.
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AAHF01000007; EAL87810.1; -; Genomic_DNA.
DR RefSeq; XP_749848.1; XM_744755.1.
DR AlphaFoldDB; Q4WKX2; -.
DR SMR; Q4WKX2; -.
DR EnsemblFungi; EAL87810; EAL87810; AFUA_1G00980.
DR GeneID; 3507516; -.
DR KEGG; afm:AFUA_1G00980; -.
DR VEuPathDB; FungiDB:Afu1g00980; -.
DR HOGENOM; CLU_018354_0_1_1; -.
DR InParanoid; Q4WKX2; -.
DR OMA; DTINNGM; -.
DR OrthoDB; 350817at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Reference proteome;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..496
FT /note="FAD-linked oxidoreductase AFUA_1G00980"
FT /id="PRO_5004246503"
FT DOMAIN 64..243
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 496 AA; 53643 MW; F64543B20B9D8A69 CRC64;
MRRATLIPLA IWVAGAAAAA AASLPQFPSC DISLANIGLS QNSQIFFPNG SGWESETIRW
TKYMAPTYAV SVRPAHVSDV TQVRFATRCK IPFLASSGQH GFDTELAELQ NGMEIDLSAF
RNVSVDAKKN TLTVGGGVRF MDVFDPVFNA GKEIRTSETD HQVGTGSGAC VGMISPTLGG
GVGRLSGTHG IISDQLLSVQ MVTANGSLVT VSKKENSNLF WGLRGAGGNF GIVVEAVYQV
TDLTSEKVVN LDYAFSTNDT GAIIDYLALF GPNMPPKLSF IIAALYNEKL FGGVGDPGCV
DPNRGRQSAN TIPPSLFQFA VIVSGLYAGP QSEAEQLLAP LLQNATLIKQ NISVVPENKL
VYAATFGSQG NSTIACSGKG VNRSIFGGAI NTYDKATYVD FLKAFGDLVT TNTDLRGSVF
FIEHFSNYQV QKIPDHTSAY PWRDITAHLL FNYAWNDPAN QQLMLYSARK LPRLRALKKE
WDPENVFRFH HPISMS
