FGNB_ASPFU
ID FGNB_ASPFU Reviewed; 385 AA.
AC Q4WKX0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=2-oxoglutarate-dependent dioxygenase AFUA_1G01000;
DE EC=1.14.11.- {ECO:0000255|PROSITE-ProRule:PRU00805};
DE AltName: Full=Fumigermin biosynthesis cluster protein AFUA_1G01000 {ECO:0000303|PubMed:32083553};
GN ORFNames=AFUA_1G01000;
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: 2-oxoglutarate-dependent dioxygenase; part of the gene
CC cluster that mediates the biosynthesis of fumigermin that inhibits
CC germination of spores of the inducing S.rapamycinicus, and thus helps
CC the fungus to defend resources in the shared habitat against a
CC bacterial competitor (PubMed:32083553). The partially reducing
CC polyketide synthase fngA alone is sufficient for the production of
CC fumigermin (PubMed:32083553). FgnA catalyzes the condensation of 3
CC malonyl-CoA units to an acetyl-CoA starter, and 3 methylations to yield
CC fumigermin (PubMed:32083553). It is remarkable that the five cluster
CC genes including fgnA are conserved in distantly related fungi,
CC supporting the assumption of a fumigermin cluster; it is thus possible
CC that originally all five genes were functional, but that the genes
CC encoding tailoring enzymes became inactive from mutations, similar to
CC the case of the fgnA gene in strains A1163 and Af293 (Probable).
CC {ECO:0000269|PubMed:32083553, ECO:0000305|PubMed:32083553}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
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 iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AAHF01000007; EAL87812.1; -; Genomic_DNA.
DR RefSeq; XP_749850.1; XM_744757.1.
DR AlphaFoldDB; Q4WKX0; -.
DR SMR; Q4WKX0; -.
DR EnsemblFungi; EAL87812; EAL87812; AFUA_1G01000.
DR GeneID; 3507447; -.
DR KEGG; afm:AFUA_1G01000; -.
DR VEuPathDB; FungiDB:Afu1g01000; -.
DR HOGENOM; CLU_010119_4_0_1; -.
DR InParanoid; Q4WKX0; -.
DR OMA; PRYSETI; -.
DR OrthoDB; 841734at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..385
FT /note="2-oxoglutarate-dependent dioxygenase AFUA_1G01000"
FT /id="PRO_0000449928"
FT DOMAIN 203..327
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 230
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 304
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 318
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 385 AA; 42636 MW; 3A193A1650FB3110 CRC64;
MTVNGKDIDS PNAQYVAAGI DMSDLFPAPF PTNVKTVHLE TLSLAKLLQR DEDELRRIYE
NCKDPGFFQL DLTDDEQGVQ LLQDAVDCAR LMKQLLPNMS VEEKRMYKQH SRVGVYSKGY
QVYDVLPNGQ PKYNETVNFP MTEMLGYGDS TVDLPDWLSP HRELFQRTMR SGNKIANIVL
AALEVGLQVP RGALTDAHRI QDPSDDFLRL LRYPGLQPGQ PRDDLCFPAH KDFTSLGILF
TWLGGLQLLA SASAPGVTSG TMTGPLDIAE DAWRWVQPVP GTAIVNVGNA LEILTNKALT
SGLHRVVRAP GEQLPFDRYS VLVGTRPANS FPMKPLQSPQ ISPVLDPAAA EIATMTSGQW
GTHNIGSFNN WVKARTERQE VLIIP
