FGNC_ASPFU
ID FGNC_ASPFU Reviewed; 261 AA.
AC Q4WKX1;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Short-chain dehydrogenase/reductase AFUA_1G00990 {ECO:0000303|PubMed:32083553};
DE EC=1.-.-.- {ECO:0000305|PubMed:32083553};
DE AltName: Full=Fumigermin biosynthesis cluster protein AFUA_1G00980 {ECO:0000303|PubMed:32083553};
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.
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: Short-chain dehydrogenase/reductase; part of the gene cluster
CC that mediates the biosynthesis of fumigermin that inhibits germination
CC of 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 -!- 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 short-chain dehydrogenases/reductases (SDR)
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; AAHF01000007; EAL87811.1; -; Genomic_DNA.
DR RefSeq; XP_749849.1; XM_744756.1.
DR AlphaFoldDB; Q4WKX1; -.
DR SMR; Q4WKX1; -.
DR EnsemblFungi; EAL87811; EAL87811; AFUA_1G00990.
DR GeneID; 3507446; -.
DR KEGG; afm:AFUA_1G00990; -.
DR VEuPathDB; FungiDB:Afu1g00990; -.
DR HOGENOM; CLU_010194_9_0_1; -.
DR InParanoid; Q4WKX1; -.
DR OMA; MRATYNE; -.
DR OrthoDB; 1259665at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd05324; carb_red_PTCR-like_SDR_c; 1.
DR InterPro; IPR045313; CBR1-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..261
FT /note="Short-chain dehydrogenase/reductase AFUA_1G00990"
FT /id="PRO_0000449929"
FT BINDING 11..19
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 37..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 66..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 167..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
FT BINDING 200..202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q92506"
SQ SEQUENCE 261 AA; 28538 MW; 0B4086F55224E7E7 CRC64;
MDSNSSNKIV LVTGANQGLG FAVIEVAGVR YPSNTYILCA RDIEKGQQAV HQLRDRGVAA
IDLVELDVTN DDHIAAAVRH VEAQYGRLDV LVNNAGFVRL GHQDTNLSEM RATYNEYMNV
HITSVAVVTH AFTPLLHRSP APKVINVTSG LGSITNVLSP RRMARVPPYG ASKVGMNGLT
AHLQVSENER VAAGEAKAPR IRFFISNPGL LKTAFSNYIA WGKEPQAGAE SIVQLMGDEE
GKFDHAMQWE HEEGEMRVVP W
