FGNA_ASPFU
ID FGNA_ASPFU Reviewed; 2098 AA.
AC Q4WKW9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Fumigermin synthase {ECO:0000303|PubMed:32083553};
DE EC=2.3.1.- {ECO:0000269|PubMed:32083553};
DE AltName: Full=Fumigermin biosynthesis cluster protein A {ECO:0000303|PubMed:32083553};
DE AltName: Full=Partially reducing polyketide synthase fngA {ECO:0000303|PubMed:32083553};
GN Name=fgnA {ECO:0000303|PubMed:32083553}; ORFNames=AFUA_1G01010;
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, INDUCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND DOMAIN.
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: Partially reducing polyketide synthase; 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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + AH2 + 3 malonyl-CoA + 3 S-adenosyl-L-methionine =
CC A + 3 CO2 + 4 CoA + fumigermin + H2O + 3 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:64012, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:17499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:147341;
CC Evidence={ECO:0000269|PubMed:32083553};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64013;
CC Evidence={ECO:0000269|PubMed:32083553};
CC -!- INDUCTION: Expression is up-regulated during co-cultivation of
CC A.fumigatus with Streptomyces rapamycinicus that triggers the
CC production of the polyketide fumigermin during the bacterial-fungal
CC interaction. {ECO:0000269|PubMed:32083553}.
CC -!- DOMAIN: Multidomain protein; including a ketosynthase (KS) that
CC catalyzes repeated decarboxylative condensation to elongate the
CC polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects
CC and transfers the extender unit malonyl-CoA; a dehydratase (DH) domain
CC that reduces hydroxyl groups to enoyl groups; a methyltransferase
CC (CMeT) domain responsible for the incorporation of methyl groups; a
CC ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and
CC an acyl-carrier protein (ACP) that serves as the tether of the growing
CC and completed polyketide via its phosphopantetheinyl arm.
CC {ECO:0000305|PubMed:32083553}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of fumigermin triggered by
CC Streptomyces rapamycinicus during the bacterial-fungal interaction.
CC {ECO:0000269|PubMed:32083553}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=No license to kill - Issue
CC 232 of January 2021;
CC URL="https://web.expasy.org/spotlight/back_issues/232/";
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; EAL87813.1; -; Genomic_DNA.
DR RefSeq; XP_749851.1; XM_744758.1.
DR AlphaFoldDB; Q4WKW9; -.
DR SMR; Q4WKW9; -.
DR EnsemblFungi; EAL87813; EAL87813; AFUA_1G01010.
DR GeneID; 3507448; -.
DR KEGG; afm:AFUA_1G01010; -.
DR VEuPathDB; FungiDB:Afu1g01010; -.
DR HOGENOM; CLU_000022_31_1_1; -.
DR InParanoid; Q4WKW9; -.
DR OMA; WLPDFDF; -.
DR OrthoDB; 19161at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Methyltransferase; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..2098
FT /note="Fumigermin synthase"
FT /id="PRO_0000449927"
FT DOMAIN 2016..2092
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..477
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 531..863
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 871..1153
FT /note="Dehydrogenase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1320..1498
FT /note="Methyltransferase (CMet) domain"
FT /evidence="ECO:0000255"
FT REGION 1707..1882
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000255"
FT COMPBIAS 11..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2052
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2098 AA; 231310 MW; 622FEA5A01E8B424 CRC64;
MSFPQVDVPS LPVGSASTQD TSPVSGPFNS SDSDHDIVNG GQANGSPFTE PIAICGLGLR
LPGGIRDGDS FWDLLVNGRD ARMPIPASRY NISGFDGSLD GRDPIKTTHG YFLDEDLSSL
DASFFSMTKT ELEKCDPQQR QLLEVTRECL EDAGETDYRG RNVGCYIGNF GHDWMEISLR
EPQHSRSYNV LGYSDMILAN RVSYEYDLRG PSVVIKTACS ASLVALHEAC RALQARDIPS
AIVGGTSLIL APTLTSNFFG EGILSPEASC KTFDESADGF ARAEGVTAIY VKRLDDALRD
GNPIRAVIRG TGTNSDGKSM GIMSPSAEAH EALMRQVYDQ AGLSPRETAF VEEKRRLSNA
SKCHGTGTAT GDPIEATAVG NVFSERGVYI GSVKPNVGHS EGCSGITSLI KAVLALEHKT
IPPNIKFRNP NPKIPFVEKK LVVPIQPTPF PLDKAERISV NSFSIGGSNA HIDAYKSYAR
DHPDAISDIA YTLAVRRERL PHRAFAIWQN GELQTSSLSK ASAVPPAITM IFSGQGAQWA
EMGKKLIETE ASFRHDLASM DSILQSLRKP PCWSILEELQ KPAEDSQINR AEMAQPLCTA
LQVALFHQLK RLGIKPTAVV GHSSGEIAAA YAAGYITLEY ALAVAYYRGY ITKNADRSRG
AMAAVRLSAT EVLPFLRTGV CIACENSPSS TTISGDKEAL KEILARLKEE KPDVFARLLK
VEMAYHSRAS ETLLLVLRST HIFADHMKPL GIEYLELLRA ENNFGIPRSA DKALFLSSVI
CKPMVDTASF GPEYWVDNLN SPIWHQDSTA TFLSALGRMY QEAVPLAVKA LFPEERRALC
GLPVYPWDHS ESYWYESRLS SAWRQRPFPH HSLLGERTVD SPDFSPIWRN MLSLEDVTWI
ADHKIRRDVV FPLAGYIAMA GEAIRQTTGV DVGYRLRDVE ARKALVLTDF KATEVVTVLH
AHTGVPAEGP SWYDFSIASC HGGSWLIHCT GQVSPLAETL SLSWEPESAS QRSLPRELTP
MRFYEAMARV GVVFGPEFQR LVDITSSATD PLAEARVMSP APRENKRPFA LHPTAIDACI
QLLIVAAARG LCRNLDQLEV PVVVGNVEVV SRGSANLRAL AQDFTQGVEC VTENSKLALR
MSGLQLAPLA AEVADQIDVH AGARLQWLPD FDFVDHSGLF NKPQRPSLEI ELEEQLTLLC
VLESMDKVAH IPPCHPHLAK YREWLALQVR MAEAGQYTLV EHAKEWVGLP RVKRQKLIQD
TYAKILDLPG RHAYSVGIKR ICEHADQIFT GEADTLDLLM QDDILAELYD SVSFGYGDFV
RLLSSNRPNL RILEVSAGTG GTTEQTLRGL VDSSSLPPYS VYTFTDVSAG FFPQAKERFA
YAPNMEFRTF DISQDGLIQG FEAASYDIIL APNVVHATAS LKETLSNLEP LLKPNGFIIL
TELCSLIKSP NYIFGNFVGW WLGEADGRDW EPYVQPEQWD AELKAAGFTG VNAVVPDQDV
PSYRLAATII SQPARKADVP EIDRAVTLLY QSADADIVER LQLYLRDSGW QVDKCQLGEE
MPPKGQDIIA SVRLESDFFG EDLSPDRLAA FQALIRHLDA EKVLWLCPRF QVRCKDPQSA
QTLGVAQTVR TELNLPLFTL EIDTNETRFE ELVHRVLQKI RTTKDEASLH ADKEFVVTDG
QVCIGRYHPF DLKKELPSRA LTLDSAAAYL LVGGTGGLGR SMTTWMVEYG ATELILLSRR
AGKDRESQSL SQELEQMGCS VHLVAGSVEN PEDIARSIAS AKKPIKGVFQ LAMVLQDAPL
LEMTYSDWVN VNGPKVTGTW NLHHALKDQP LDFFWLASSI LTAVDTPGQA NYLATGTFLE
AFCQYRHSLG LPASVLNICP VEGVGFVAEN AHAKKNMKAQ GIYTLREREF LDFVELSLID
STPSAGGNTS PTATPPGPWV NRSQVVMGLR SEQGLGDPHN RASWRHNRRM RLYHNRRTQE
SESARDGKNG AKASALQAFL ERVREMGDEG LLRGEGVDFL AFEVGKKIHD LMLKPDEEVE
IGRTLAQIGL DSLMAIELRR WIKQVFGLTM SVLEIMGSGS LKQLAEDLAA KYAEKIQQ
