ID   AFOG_EMENI              Reviewed;        2527 AA.
AC   Q5BEJ4; C8VTX6;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Asperfuranone polyketide synthase afoG {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000305|PubMed:19199437};
DE   AltName: Full=Asperfuranone biosynthesis protein B {ECO:0000303|PubMed:19199437};
GN   Name=afoG {ECO:0000303|PubMed:19199437}; ORFNames=AN1036;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19199437; DOI=10.1021/ja8088185;
RA   Chiang Y.M., Szewczyk E., Davidson A.D., Keller N., Oakley B.R., Wang C.C.;
RT   "A gene cluster containing two fungal polyketide synthases encodes the
RT   biosynthetic pathway for a polyketide, asperfuranone, in Aspergillus
RT   nidulans.";
RL   J. Am. Chem. Soc. 131:2965-2970(2009).
RN   [4]
RP   BIOTECHNOLOGY.
RX   PubMed=20148857; DOI=10.1111/j.1742-7843.2010.00545.x;
RA   Wang C.C., Chiang Y.M., Praseuth M.B., Kuo P.L., Liang H.L., Hsu Y.L.;
RT   "Asperfuranone from Aspergillus nidulans inhibits proliferation of human
RT   non-small cell lung cancer A549 cells via blocking cell cycle progression
RT   and inducing apoptosis.";
RL   Basic Clin. Pharmacol. Toxicol. 107:583-589(2010).
CC   -!- FUNCTION: Polyketide synthase; part of the gene cluster that mediates
CC       the biosynthesis of asperfuranone, a probable antitumor agent
CC       (PubMed:19199437). The polyketide synthase afoG is responsible for
CC       producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three
CC       malonyl-CoA, and two S-adenosyl methionines (SAM) (PubMed:19199437).
CC       The 3,5-dimethyloctadienone moiety is then loaded onto the SAT domain
CC       of afoE and extended with four malonyl-CoA and one SAM, which leads to
CC       the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-
CC       nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release
CC       and aldol condensation (PubMed:19199437). AfoD is the next enzyme in
CC       the biosynthesis sequence and hydroxylates the side chain at the
CC       benzylic position of compound 2 (PubMed:19199437). After benzylic
CC       hydroxylation, a furan ring is formed after five-member ring hemiacetal
CC       formation and water elimination (PubMed:19199437). AfoF and afoC are
CC       proposed to oxidize the R-diketone proton and to reduce the
CC       unconjugated carbonyl group, respectively, to generate asperfuranone
CC       (PubMed:19199437). Since no intermediates could be isolated from afoF
CC       and afoC deletants, the sequence of these two enzymes is not fully
CC       understood (PubMed:19199437). Moreover, since afoC deletant still
CC       produces a small amount of asperfuranone, other endogenous
CC       oxidoreductases might catalyze the same reaction with much less
CC       efficiency (PubMed:19199437). {ECO:0000269|PubMed:19199437}.
CC   -!- INDUCTION: Expression is regulated by the asperfuranone cluster
CC       transcription factor afoA (PubMed:19199437).
CC       {ECO:0000269|PubMed:19199437}.
CC   -!- DISRUPTION PHENOTYPE: Completely abolishes the production of
CC       asperfuranone (PubMed:19199437). {ECO:0000269|PubMed:19199437}.
CC   -!- BIOTECHNOLOGY: Asperfuranone provides anti-proliferative activity in
CC       human non-small cell lung cancer cells (PubMed:20148857).
CC       {ECO:0000269|PubMed:20148857}.
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DR   EMBL; BN001308; CBF88289.1; -; Genomic_DNA.
DR   EMBL; AACD01000015; EAA65604.1; -; Genomic_DNA.
DR   RefSeq; XP_658640.1; XM_653548.1.
DR   AlphaFoldDB; Q5BEJ4; -.
DR   SMR; Q5BEJ4; -.
DR   STRING; 162425.CADANIAP00001610; -.
DR   PRIDE; Q5BEJ4; -.
DR   EnsemblFungi; CBF88289; CBF88289; ANIA_01036.
DR   EnsemblFungi; EAA65604; EAA65604; AN1036.2.
DR   GeneID; 2876812; -.
DR   KEGG; ani:AN1036.2; -.
DR   VEuPathDB; FungiDB:AN1036; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q5BEJ4; -.
DR   OMA; GPGPHWD; -.
DR   OrthoDB; 19161at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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:1900554; P:asperfuranone biosynthetic process; IMP:AspGD.
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; IPR011032; GroES-like_sf.
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; IPR020843; PKS_ER.
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; 2.
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; SM00829; PKS_ER; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 3.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   SUPFAM; SSF55048; SSF55048; 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   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..2527
FT                   /note="Asperfuranone polyketide synthase afoG"
FT                   /id="PRO_0000436374"
FT   DOMAIN          2436..2513
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          15..414
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          534..847
FT                   /note="Malonyl-CoA:ACP transacylase (MAT)"
FT                   /evidence="ECO:0000255"
FT   REGION          946..1255
FT                   /note="Dehydratase-like"
FT                   /evidence="ECO:0000255"
FT   REGION          1526..1564
FT                   /note="Methyltransferase"
FT                   /evidence="ECO:0000255"
FT   REGION          2405..2432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2407..2423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2473
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2527 AA;  273245 MW;  7CE6C067D20FE51A CRC64;
     MGSTSSEPTY DSEPIAIIGL SCKFAGSADS PEKLWEMLAE GRNAWSEIPE SRFNHKAVYH
     PDSEKLGTTL DPQFRFQLES VYEALENEST AGLTIPSIAG TNTSVYAGVF THDYHEGLIR
     DEDKLPRFLP IGTLSAMSSN RISHFFDLKG ASVTVDTGCS TALVALHQAV LGLRTREADM
     SIVSGCNIML SPDMFKVFSS LGMLSPDGKS YAFDSRANGY GRGEGVATII VKRLADALRD
     GDPVRGVIRE SYLNQDGKTE TITSPSQEAQ EALIKECYRR AGLSPSDTQY FEAHGTGTPT
     GDPIEARSIA SVFGKNREQP LRIGSVKTNI GHTEAASGLA GLIKVVLAME KGFIPPSVNF
     EKPNPKLKLD EWRLKVADTL EKWPAPAERP WRASVNNFGY GGTNSHVIVE GVPKRLYTPA
     NGNETGQIKH ETESKVLLFS GRDEQACQRM VASTKEYLKK RREQDPPMTP EQVKTLMQNL
     AWTLTQHRTR FSWVSAHAVK YSTSLDTVID ALESPPPASR PVRIPDSPFR IGMVFTGQGA
     QWHAMGRELI AAYPVFKATL DEAEQYLRQL GAGWSLIEEL MKDAATTRVN DTGLSIPICV
     AVQIALVRLL KAWGITASAV TSHSSGEIAA AYTVGALSLR QAMAAAYYRA AMAADKTLKS
     AEGPQGAMVA VGVDKAAAQA YLDRVEKSAG RAVVACINSP SSITIAGDEA AVVAVEKLAT
     EEGVFARRLR VETGYHSHHM EPIASPYREA LRAALAQEDA ESGTKDQTDV PGFADATKPG
     SLDHTVFSSP VTGGRVTDAK VLSDPEHWVR SLLQPVRFVE AFTDMVLGST DSSNIDLILE
     VGPHTALGGP IKEILALPDF SSRNVSLPYM GCLVRKEDAR DCMLTAALNL FSKGHSIDLL
     RLSFSSGIPE LQVLTDLPSY PWNHSIRHWS ESRRNAAYRK RSQEPHELLG VLEPGTNPDA
     ASWRHIIKLS EAPWLRDHVV QGNILYPGAG FVCLAIEAIK MQSAMSGTND VTGFRLRDVE
     IHQALVIADS ADGVEVQTTL RSVGGKVIGA RGWKQFEIWS VSADSEWTEH ARGLITVDTE
     TKASTLVAST LDESGYTRRI DPQDMFASLR AKGLNHGPMF QNTLRILQDG RAKEPQCVVD
     IKIADVSSSK DSGRMSLLHP TTLDSIVLSS YAAVPSSDPS NDDSARVPRS IRSLWVSSMI
     SSAPGHTFTC NVKMPHHDAQ SYEANVTVVD EAGARAESMV EMQGLVCQSL GRSAPAEDRE
     PWTKELCANV EWAPDLSLSL GLPGSSDAID RRLNTLRDQN PDERSIEVQT VLRRVCVYFS
     HDALSSLTEN DVANLAFHHV KFYKWMQDTV NLALARRWSA DSDTWIHDSP AVREKYISLA
     GSQTVDGELI CQLGPLLLPV LRGERAPLEV MMEGRLLYKY YANAYRLEPA FEQLKSLLGA
     ILHKNPRARV LEIGAGTGAA TRHALKTLGT DEDGGPRCES WHFTDISSGF FEAARAEFAT
     WGGLLEFNKL DIEQDPEAQG FKLGSYDVVV ACQVLHATKS MHRTMTNVRS LMKPGGTLLL
     METTQDQIDL QFIFGLLPGW WLSEEPERHA SPSLSIDMWD RVLKGAGFTG VEIDLRDVNV
     DAESDLYGIS NIMSTAVGTA GSSPEKVDAA QVVIVTGNKT GFQDDWVRGL QAAIAQDSGS
     DALPEIISLE SPSLGAEAFQ SRLVVFVGEL DRPVLASLDS TELEGIKTMA LACKGLLWVT
     RGGAVECTDP DSALASGFVR VLRTEYLGRR FLTLDLDPAA HSPASDISVI VHLLSSRLQP
     AVETAAPADS EFALRDGLLL VPRLYKDVVW NALLEPEVPD WASPEKPRAY GLNFRDVMVA
     MGQLKERVMG LECAGVITRV GAEAAAQGFA VGDRVMALLL GPFSSRARVS WHGVASMPAG
     MGFADAASIP MIFTTAYVAL VQAARLSQGQ TVLIHAAAGG VGQAAVILAK EYLGAEVFAT
     VGSQEKRDLL IKEYGIPDDH IFNSRDSSFA PAALAATAGR GVDCLIEVLA PFGHFVEIGK
     RDLEQNSLLE MATFTRAVSF TSLDMMTLLR QRGDEAHRVL SELARLAGQG IVKPVHPVSV
     YPMRQVDKAF RLLQTGKHLG KLVLSTEPDE EVRVLPRPAT PKLRADASYL LVGGVGGLGR
     SLASWMVEHG AKHLILLSRS AGKQDSSAFV NGLRDAGCRV AAISCDVADR ADLDRAIAAA
     SELGFPHVRG VIQGAMVLQD SIIEQMSIAD WNAAIKPKVA GTRNLHDRFS QRNSLDFFVM
     LSSLSAILGW ASQASYAAGG TYQDALARWR CSKGLPAVSL DMGVIKDVGY VAESRSVSDR
     LRKVGQSLRL SEESILQTLA TAVLHPFGRP QLLLGLNSGP GSHWDPSSDS QMGRDARFAP
     LRYRKPASTK SAQTSSSGDG EEPLSSKLKS ADSPDAAANY VGGAIATKLA DIFMVPVADI
     DLTKPPSAYG VDSLVAVELR NMLVLQAACD VSIFSILQSV SLAALAGMVV EKSAHFEGSA
     TGTVVVA