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Atrochrysone carboxylic acid synthase (ACAS) (EC 2.3.1.-) (Monodictyphenone synthesis protein G) (Non-reducing polyketide synthase mdpG)

 MDPG_EMENI              Reviewed;        1806 AA.
Q5BH30; C8VQ66;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
25-OCT-2017, entry version 98.
RecName: Full=Atrochrysone carboxylic acid synthase {ECO:0000303|PubMed:20139316};
Short=ACAS {ECO:0000303|PubMed:20139316};
EC=2.3.1.- {ECO:0000269|PubMed:20139316};
AltName: Full=Monodictyphenone synthesis protein G {ECO:0000303|PubMed:20139316};
AltName: Full=Non-reducing polyketide synthase mdpG {ECO:0000303|PubMed:20139316};
Name=mdpG {ECO:0000303|PubMed:20139316}; ORFNames=AN0150;
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
194 / M139) (Aspergillus nidulans).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=227321;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=16372000; DOI=10.1038/nature04341;
Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
"Sequencing of Aspergillus nidulans and comparative analysis with A.
fumigatus and A. oryzae.";
Nature 438:1105-1115(2005).
[2]
GENOME REANNOTATION.
STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
"The 2008 update of the Aspergillus nidulans genome annotation: a
community effort.";
Fungal Genet. Biol. 46:S2-13(2009).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20139316; DOI=10.1128/AEM.02187-09;
Chiang Y.M., Szewczyk E., Davidson A.D., Entwistle R., Keller N.P.,
Wang C.C., Oakley B.R.;
"Characterization of the Aspergillus nidulans monodictyphenone gene
cluster.";
Appl. Environ. Microbiol. 76:2067-2074(2010).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21351751; DOI=10.1021/ja1096682;
Sanchez J.F., Entwistle R., Hung J.H., Yaegashi J., Jain S.,
Chiang Y.M., Wang C.C., Oakley B.R.;
"Genome-based deletion analysis reveals the prenyl xanthone
biosynthesis pathway in Aspergillus nidulans.";
J. Am. Chem. Soc. 133:4010-4017(2011).
-!- FUNCTION: Non-reducing polyketide synthase; part of the gene
cluster that mediates the biosynthesis of monodictyphenone, a
prenyl xanthone derivative (PubMed:20139316, PubMed:21351751). The
pathway begins with the synthesis of atrochrysone thioester by the
polyketide synthase (PKS) mdpG (PubMed:20139316). The atrochrysone
carboxyl ACP thioesterase mdpF then breaks the thioester bond and
releases the atrochrysone carboxylic acid from gedC
(PubMed:20139316). The atrochrysone carboxylic acid is then
converted to atrochrysone which is further transformed into emodin
anthrone (PubMed:20139316). The next step is performed by the
anthrone oxygenase mdpH that catalyzes the oxidation of
emodinanthrone to emodin (By similarity). Emodin is further
modified to yield monodictyphenone via several steps involving by
mdpB, mdpC mdpJ, mdpK and mdpL (PubMed:20139316, PubMed:21351751).
{ECO:0000250|UniProtKB:Q0CCY3, ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:20139316, ECO:0000269|PubMed:21351751}.
-!- DOMAIN: Multidomain protein; including a starter unit:ACP
transacylase (SAT) that selects the starter unit; a ketosynthase
(KS) that catalyzes repeated decarboxylative condensation to
elongate the polyketide backbone; a malonyl-CoA:ACP transacylase
(MAT) that selects and transfers the extender unit malonyl-CoA; a
product template (PT) domain that controls the immediate
cyclization regioselectivity of the reactive polyketide backbone;
and an acyl-carrier protein (ACP) that serves as the tether of the
growing and completed polyketide via its phosphopantetheinyl arm
(By similarity). {ECO:0000250|UniProtKB:Q5B0D0}.
-!- DISRUPTION PHENOTYPE: Impairs the production of monodictyphenone
and any of the intermediates of the pathway (PubMed:20139316,
PubMed:21351751). {ECO:0000269|PubMed:20139316,
ECO:0000269|PubMed:21351751}.
-----------------------------------------------------------------------
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EMBL; BN001308; CBF90097.1; -; Genomic_DNA.
EMBL; AACD01000005; EAA66023.1; -; Genomic_DNA.
RefSeq; XP_657754.1; XM_652662.1.
ProteinModelPortal; Q5BH30; -.
SMR; Q5BH30; -.
STRING; 162425.CADANIAP00002593; -.
EnsemblFungi; CADANIAT00002593; CADANIAP00002593; CADANIAG00002593.
EnsemblFungi; EAA66023; EAA66023; AN0150.2.
GeneID; 2875928; -.
KEGG; ani:AN0150.2; -.
HOGENOM; HOG000168774; -.
KO; K15415; -.
OMA; MQSDLMQ; -.
OrthoDB; EOG092C01G3; -.
Proteomes; UP000000560; Chromosome VIII.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:1900587; P:arugosin biosynthetic process; IMP:AspGD.
GO; GO:1900575; P:emodin biosynthetic process; IMP:AspGD.
GO; GO:1900815; P:monodictyphenone biosynthetic process; IMP:AspGD.
GO; GO:1900813; P:monodictyphenone metabolic process; IMP:AspGD.
GO; GO:1900584; P:o-orsellinic acid biosynthetic process; IMP:AspGD.
GO; GO:0055114; P:oxidation-reduction process; IEA:GOC.
GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
GO; GO:1900793; P:shamixanthone biosynthetic process; IMP:AspGD.
GO; GO:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.30.70.250; -; 1.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR030918; PT_fungal_PKS.
InterPro; IPR032088; SAT.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
Pfam; PF16073; SAT; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS50075; CARRIER; 1.
3: Inferred from homology;
Complete proteome; Multifunctional enzyme; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1806 Atrochrysone carboxylic acid synthase.
/FTId=PRO_0000437049.
DOMAIN 1728 1805 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 30 283 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255}.
REGION 419 853 Ketosynthase (KS) domain. {ECO:0000255}.
REGION 951 1270 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255}.
REGION 1340 1659 Product template (PT) domain.
{ECO:0000255}.
COMPBIAS 1675 1724 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
ACT_SITE 589 589 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 1765 1765 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
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


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