MDPG_EMENI
ID MDPG_EMENI Reviewed; 1806 AA.
AC Q5BH30; C8VQ66;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Atrochrysone carboxylic acid synthase {ECO:0000303|PubMed:20139316};
DE Short=ACAS {ECO:0000303|PubMed:20139316};
DE EC=2.3.1.- {ECO:0000305|PubMed:20139316};
DE AltName: Full=Monodictyphenone synthesis protein G {ECO:0000303|PubMed:20139316};
DE AltName: Full=Non-reducing polyketide synthase mdpG {ECO:0000303|PubMed:20139316};
GN Name=mdpG {ECO:0000303|PubMed:20139316}; ORFNames=AN0150;
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, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=20139316; DOI=10.1128/aem.02187-09;
RA Chiang Y.M., Szewczyk E., Davidson A.D., Entwistle R., Keller N.P.,
RA Wang C.C., Oakley B.R.;
RT "Characterization of the Aspergillus nidulans monodictyphenone gene
RT cluster.";
RL Appl. Environ. Microbiol. 76:2067-2074(2010).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=21351751; DOI=10.1021/ja1096682;
RA Sanchez J.F., Entwistle R., Hung J.H., Yaegashi J., Jain S., Chiang Y.M.,
RA Wang C.C., Oakley B.R.;
RT "Genome-based deletion analysis reveals the prenyl xanthone biosynthesis
RT pathway in Aspergillus nidulans.";
RL J. Am. Chem. Soc. 133:4010-4017(2011).
RN [5]
RP FUNCTION.
RX PubMed=22730213; DOI=10.1002/cbic.201200014;
RA Simpson T.J.;
RT "Genetic and biosynthetic studies of the fungal prenylated xanthone
RT shamixanthone and related metabolites in Aspergillus spp. revisited.";
RL ChemBioChem 13:1680-1688(2012).
RN [6]
RP FUNCTION.
RX PubMed=22909031; DOI=10.1021/ja307151x;
RA Schaetzle M.A., Husain S.M., Ferlaino S., Mueller M.;
RT "Tautomers of anthrahydroquinones: enzymatic reduction and implications for
RT chrysophanol, monodictyphenone, and related xanthone biosyntheses.";
RL J. Am. Chem. Soc. 134:14742-14745(2012).
RN [7]
RP FUNCTION.
RX PubMed=26266881; DOI=10.1021/jacs.5b06770;
RA Conradt D., Schaetzle M.A., Haas J., Townsend C.A., Mueller M.;
RT "New Insights into the Conversion of Versicolorin A in the Biosynthesis of
RT Aflatoxin B1.";
RL J. Am. Chem. Soc. 137:10867-10869(2015).
CC -!- FUNCTION: Atrochrysone carboxylic acid synthase; part of the gene
CC cluster that mediates the biosynthesis of monodictyphenone, a prenyl
CC xanthone derivative (PubMed:20139316, PubMed:21351751). The pathway
CC begins with the synthesis of atrochrysone thioester by the polyketide
CC synthase (PKS) mdpG (PubMed:20139316). The atrochrysone carboxyl ACP
CC thioesterase mdpF then breaks the thioester bond and releases the
CC atrochrysone carboxylic acid from mdpG (PubMed:20139316). The
CC atrochrysone carboxylic acid is then converted to atrochrysone which is
CC further transformed into emodin anthrone (PubMed:20139316). The next
CC step is performed by the anthrone oxygenase mdpH that catalyzes the
CC oxidation of emodinanthrone to emodin (By similarity). Emodin is
CC further modified to yield monodictyphenone via several steps involving
CC mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751,
CC PubMed:22909031). The short chain dehydrogenase mdpC converts the
CC tautomers of emodin hydroquinone into the 3-hydroxy-3,4-dihydroan-
CC thracen-1(2H)-one derivative (PubMed:22909031, PubMed:26266881). These
CC enzymes with xptA, xptB and xptC are also proposed to be involved in
CC the synthesis of shamixanthone from emodin (PubMed:22730213).
CC Especially, direct reduction of emodin by the short chain dehydrogenase
CC mdpC followed by dehydration catalyzed by the scytalone dehydratase-
CC like protein mdpB gives loss of oxygen and formation of chrysophanol
CC intermediate in two simple steps (PubMed:22730213).
CC {ECO:0000250|UniProtKB:Q0CCY3, ECO:0000269|PubMed:20139316,
CC ECO:0000269|PubMed:21351751, ECO:0000269|PubMed:22730213,
CC ECO:0000269|PubMed:22909031, ECO:0000269|PubMed:26266881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8 H(+) + holo-[ACP] + 8 malonyl-CoA = atrochrysone carboxyl-
CC [ACP] + 8 CO2 + 8 CoA + 2 H2O; Xref=Rhea:RHEA:64232, Rhea:RHEA-
CC COMP:9685, Rhea:RHEA-COMP:16552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:64479, ChEBI:CHEBI:149712;
CC Evidence={ECO:0000305|PubMed:20139316};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64233;
CC Evidence={ECO:0000305|PubMed:20139316};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751}.
CC -!- DOMAIN: Multidomain protein; including a starter unit:ACP transacylase
CC (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes
CC repeated decarboxylative condensation to elongate the polyketide
CC backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and
CC transfers the extender unit malonyl-CoA; a product template (PT) domain
CC that controls the immediate cyclization regioselectivity of the
CC reactive polyketide backbone; and an acyl-carrier protein (ACP) that
CC serves as the tether of the growing and completed polyketide via its
CC phosphopantetheinyl arm (By similarity).
CC {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone and
CC any of the intermediates of the pathway (PubMed:20139316,
CC PubMed:21351751). {ECO:0000269|PubMed:20139316,
CC ECO:0000269|PubMed:21351751}.
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DR EMBL; BN001308; CBF90097.1; -; Genomic_DNA.
DR EMBL; AACD01000005; EAA66023.1; -; Genomic_DNA.
DR RefSeq; XP_657754.1; XM_652662.1.
DR AlphaFoldDB; Q5BH30; -.
DR SMR; Q5BH30; -.
DR STRING; 162425.CADANIAP00002593; -.
DR PRIDE; Q5BH30; -.
DR EnsemblFungi; CBF90097; CBF90097; ANIA_00150.
DR EnsemblFungi; EAA66023; EAA66023; AN0150.2.
DR GeneID; 2875928; -.
DR KEGG; ani:AN0150.2; -.
DR VEuPathDB; FungiDB:AN0150; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_6_1_1; -.
DR InParanoid; Q5BH30; -.
DR OMA; AAYGHKM; -.
DR OrthoDB; 68112at2759; -.
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:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1900587; P:arugosin biosynthetic process; IMP:AspGD.
DR GO; GO:0022900; P:electron transport chain; IEA:GOC.
DR GO; GO:1900575; P:emodin biosynthetic process; IMP:AspGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
DR GO; GO:1900813; P:monodictyphenone metabolic process; IMP:AspGD.
DR GO; GO:1900584; P:o-orsellinic acid biosynthetic process; IMP:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
DR GO; GO:1900793; P:shamixanthone biosynthetic process; IMP:AspGD.
DR GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..1806
FT /note="Atrochrysone carboxylic acid synthase"
FT /id="PRO_0000437049"
FT DOMAIN 1728..1805
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 30..283
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255"
FT REGION 419..853
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 951..1270
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1340..1659
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1668..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1705..1721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 589
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 1765
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1806 AA; 196801 MW; 9FA7BAC8B1DC176F CRC64;
MPVYTPQSGS LPEYSKMKLL YFSNELPKDD LQGLFRRLYN HSKDRRYPLL ARFIHEATLA
VREEVRQLPT AVKALVPAFE TVLNLADYPE LRKGPLGGSL EGVLLCVLEI ATLIGHVPRL
YFKEAADCCS YYENASERFD LHAVSTYLAG LGLGLLSTAA VALCSALADV PVIGAEVVRV
SFRLGTLVDE ISQNLEPRDT SGSPDTWASV VPGAKVEEVQ AELDAIHARE KTPQPSKIFI
SAWNEGSVTI SGPPSRIRRV LRLSEFFRRH RVVSLPVYSG LCHAKHLYNE QHAREIISTR
SMDSINALYS PAIPVYQTST GRPFTASTAK GLFEQLVLEL LTQPILWDNV VQGVVDQAYA
TSATSCDVLV FRISVPINDL RTALGSKLQG FETSTEELIP WILQKSDMEI PRGTAQSKIA
IIGMSCRMPG GATDTEKFWE LLEQGLDVAR KIPADRFDVE THYDPKGKRV NTSHTPYGCF
IDEPGLFDAP FFNMSPREAQ QTDPMQRLAI VTAYEALERA GYVANRTPAT NLHRIGTFYG
QASDDYREVN TAQEISTYFI PGGCRAFGPG RINYFFKFSG PSFSCDTACS SSLATIQAAC
TSLWNGDTDM VVAGGMNVLT NSDAFAGLSH GHFLSKTPGA CKTWDVNADG YCRADGIGSI
VMKRLEDAEA DNDNIIGIIR AAATNHSAEA ISITHPHAGA QAYLYRQVMS SAGIDPLDVS
FVEMHGTGTQ AGDSVEITSI TDIFAPITKR RSAQQPLHIG AVKANVGHGE AVAGVTALLK
VLLMYQKNAI PPHVGIKNSL NPLFPKDLDK RNLHIPYQKV PWPRVKGKKR YAVVNNFSAA
GGNTTVCLEE PPLRETDYVD PRTAHVVNVS AKSKISFKKN LERLVAYLDA NPDTSLASLS
YTTTARRYHH NHRASVAATD IAQVKKKLLS YIDKVEAHKP IPATGPPQVA FAFTGQGASY
KSMNLELFHH SPYFRSQLLH LDALAQGQGF PSFIPAVDGS HEKDYAHSPV VTQLALVSVE
IALAKYWISL GVKPNAVVGH SLGEYAAFHV AGVLSASDAL FLVGRRAQLL EEKCQIGSHK
MLAVRAPLAD IEKALEGTNY EVACINGPKE TVLSGSQAQV EVVSEILQSV GYRCTSLDVA
FAFHSSQTEA ILDDFEEAAK DGVLFRAPNM PVISPLLGKV IFDDKTITAK YMRRATRETV
NFLSALEMAQ TFSTVDEETV WVEIGPHPVC MGFVNATLPA VNETVASMKR GEDNWVTLCN
SLTALHCAGV PIEWNEYQRP FEKGLRLLDL PTYAWNDKTY WIQYNGDWAL TKGNTFYDAE
KSLKAQQTGQ LASVPSGLRT STVQQIIEES FNGSAGKVVM QSDMMQPDFL DAAHGHKMNG
CGVVTSSIHG DIGFTLGGYL YKNLVKGGKA PDMNMANLVV LRGLVAQKNT KKPQYIRVTI
STTDINSGVA ELIWQNVLND NTADEPFASA SILYDDAALW LKSWIPSTHL VQGRIEALER
LAEDGIANRF TRNMAYLLFA NNLVDYAQKY RGMQSVVLHE LEAFADITLS TEKSGTWTIP
PYFIDSVAHL AGFVMNVSDA IDTKANYCVT PGWKSLRFAK PLVAGAKYRS YVKMIQTEED
PTVYLGDVYI MQDGAIIGMC GGIQFRRYPR ILLNRFFTAP EEAGAISHAA ASSTPAPRTK
PEPVPVATPA TAAAPVAQSP AAPASVTPAP APAPAPGPTP AAAPAAAGES DSVAAKALVL
IAKEAALELS DLTDDASFAN LGVDSLMSLV IAEKFREELG VTVTGSLFLE YPTIGDLRSW
LLEYYN
