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Atrochrysone carboxylic acid synthase (ACAS) (EC 2.3.1.-) (Non-reducing polyketide synthase tpcC) (Trypacidin synthesis protein C)

 TPCC_ASPFU              Reviewed;        1782 AA.
Q4WQZ5;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
05-DEC-2018, entry version 89.
RecName: Full=Atrochrysone carboxylic acid synthase {ECO:0000305|PubMed:26242966};
Short=ACAS {ECO:0000305|PubMed:26242966};
EC=2.3.1.- {ECO:0000269|PubMed:26242966};
AltName: Full=Non-reducing polyketide synthase tpcC {ECO:0000303|PubMed:26242966};
AltName: Full=Trypacidin synthesis protein C {ECO:0000303|PubMed:26242966};
Name=tpcC {ECO:0000303|PubMed:26242966};
Synonyms=tynC {ECO:0000303|PubMed:26278536}; ORFNames=AFUA_4G14560;
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
A1100) (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=330879;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
PubMed=16372009; DOI=10.1038/nature04332;
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
Machida M., Hall N., Barrell B.G., Denning D.W.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus
Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
[2]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22319557; DOI=10.1371/journal.pone.0029906;
Gauthier T., Wang X., Sifuentes Dos Santos J., Fysikopoulos A.,
Tadrist S., Canlet C., Artigot M.P., Loiseau N., Oswald I.P., Puel O.;
"Trypacidin, a spore-borne toxin from Aspergillus fumigatus, is
cytotoxic to lung cells.";
PLoS ONE 7:E29906-E29906(2012).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26278536; DOI=10.1007/s00253-015-6898-1;
Mattern D.J., Schoeler H., Weber J., Novohradska S., Kraibooj K.,
Dahse H.M., Hillmann F., Valiante V., Figge M.T., Brakhage A.A.;
"Identification of the antiphagocytic trypacidin gene cluster in the
human-pathogenic fungus Aspergillus fumigatus.";
Appl. Microbiol. Biotechnol. 99:10151-10161(2015).
[4]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
PubMed=26242966; DOI=10.1111/1462-2920.13007;
Throckmorton K., Lim F.Y., Kontoyiannis D.P., Zheng W., Keller N.P.;
"Redundant synthesis of a conidial polyketide by two distinct
secondary metabolite clusters in Aspergillus fumigatus.";
Environ. Microbiol. 18:246-259(2016).
-!- FUNCTION: Non-reducing polyketide synthase; part of the gene
cluster that mediates the biosynthesis of trypacidin, a mycotoxin
with antiprotozoal activity and that plays a role in the infection
process (PubMed:26278536, PubMed:26242966). The pathway begins
with the synthesis of atrochrysone thioester by the polyketide
synthase (PKS) tpcC (PubMed:26242966). The atrochrysone carboxyl
ACP thioesterase tpcB then breaks the thioester bond and releases
the atrochrysone carboxylic acid from tpcC (PubMed:26242966). The
decarboxylase tpcK converts atrochrysone carboxylic acid to
atrochrysone which is further reduced into emodin anthrone
(PubMed:26242966). The next step is performed by the emodin
anthrone oxygenase tpcL that catalyzes the oxidation of
emodinanthrone to emodin (PubMed:26242966). Emodin O-
methyltransferase encoded by tpcA catalyzes methylation of the 8-
hydroxy group of emodin to form questin (PubMed:26242966). Ring
cleavage of questin by questin oxidase tpcI leads to
desmethylsulochrin via several intermediates including questin
epoxide (By similarity). Another methylation step catalyzed by
tpcM leads to the formation of sulochrin which is further
converted to monomethylsulfochrin by tpcH. Finally, the tpcJ
catalyzes the conversion of monomethylsulfochrin to trypacidin
(PubMed:26242966). Trypacidin is toxic for human pulmonary and
bronchial epithelial cells by initiating the intracellular
formation of nitric oxide (NO) and hydrogen peroxide (H(2)O(2)),
thus triggering host necrotic cell death (PubMed:22319557). The
trypacidin pathway is also able to produce endocrocin via a
distinct route from the endocrocin Enc pathway (PubMed:26242966).
{ECO:0000250|UniProtKB:Q0CCY3, ECO:0000269|PubMed:22319557,
ECO:0000269|PubMed:26242966, ECO:0000269|PubMed:26278536}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:26242966, ECO:0000269|PubMed:26278536}.
-!- TISSUE SPECIFICITY: Specifically expressed in conidia
(PubMed:22319557). {ECO:0000305|PubMed:22319557}.
-!- INDUCTION: Expression is positively regulated by the transcription
factors brlA and laeA (PubMed:26242966).
{ECO:0000269|PubMed:26242966}.
-!- 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 trypacidin and
pathway intermediates including questin (PubMed:26278536,
PubMed:26242966). Leads to enhanced phagocytosis ratio by
macrophages and amoebae (PubMed:26278536).
{ECO:0000269|PubMed:26242966, ECO:0000269|PubMed:26278536}.
-----------------------------------------------------------------------
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EMBL; AAHF01000005; EAL89339.1; -; Genomic_DNA.
RefSeq; XP_751377.1; XM_746284.1.
ProteinModelPortal; Q4WQZ5; -.
SMR; Q4WQZ5; -.
STRING; 5085.CADAFUBP00006997; -.
EnsemblFungi; EAL89339; EAL89339; AFUA_4G14560.
GeneID; 3509595; -.
KEGG; afm:AFUA_4G14560; -.
EuPathDB; FungiDB:Afu4g14560; -.
HOGENOM; HOG000168774; -.
InParanoid; Q4WQZ5; -.
KO; K15415; -.
OMA; MQSDLMQ; -.
OrthoDB; EOG092C01G3; -.
Proteomes; UP000002530; Chromosome 4.
Proteomes; UP000002530; Unassembled WGS sequence.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
GO; GO:0044550; P:secondary metabolite biosynthetic process; IMP:AspGD.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.40.366.10; -; 1.
Gene3D; 3.40.47.10; -; 1.
InterPro; IPR001227; Ac_transferase_dom_sf.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR018201; Ketoacyl_synth_AS.
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; 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; 1.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
2: Evidence at transcript level;
Complete proteome; Multifunctional enzyme; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1782 Atrochrysone carboxylic acid synthase.
/FTId=PRO_0000437050.
DOMAIN 1704 1781 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 41 270 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255}.
REGION 410 844 Ketosynthase (KS) domain. {ECO:0000255}.
REGION 946 1266 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255}.
REGION 1331 1648 Product template (PT) domain.
{ECO:0000255}.
ACT_SITE 580 580 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 1741 1741 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 1782 AA; 194340 MW; 40ADDE88312785DE CRC64;
MRPVDFTPSS ESPTAEKGMK VVYFGNELPQ DGIQGICRRL HTYTKDRRYP LLARFIEEST
WAVHDEVRQL HAAQKALVSP FESVLHLAEQ PELCRGPLCG SIEGVLLCVI QLGTFIGYYE
DSPNEYTFDS ANTYLTGLGL GLLASTAVSL SPTLADLPLA GAEVVRVAFR LGVLVADVSQ
NLQPADATGE RDSWAYVIPN VAPKEAEEEL AVIHTRENTP EASRIFISAI SRTSVTISGP
PARLRRLFRM SDFFRDRTFV ALPVYGGLCH AKHIYNSQHA RSVVQGPSIA ALDTRFIARY
PILSTGSGEP FPTATTATEL FEHVMTEILT QAIEWENVIQ GVVERAKLLS VSEVQVQVFR
NSHPVHDLLS ALETSLREGV EVAIKDLGPW ITRTRDEERP PPRGTAQSKI AIVGMSCRMP
SGATDTEKFW DILEQGLDVH RKIPPDRFDV DSHYDPAGKR VNASHTPYGC FIDEPGLFDA
PFFNMSPREA QQTDPMQRLA IVTAYEALER AGYVANRTRS SNKHRMGTFY GQASDDYREV
NSAQEISTYF IPGGCRAFGP GRINYFFKLW GPSFSIDTAC SSSLATIQAA CTALWNGDTD
TVVAGGMNVL TNSDAFAGLS HGHFLTKTPN ACKTWDCEAD GYCRADGVAS IVMKRLEDAE
ADNDNILGVI LGAATNHSAE AISITHPHAG AQSCLSRQVL RSAGIDPMDV SYVEMHGTGT
QAGDAEEIKS VSDVFAPAVK RRSSQQPVFI GAVKANVGHG EAVAGVTALV KVLLMFQKEA
IPPHVGIKNS INPGFPKDLD QRNLRIPYEK KPWPRRPGRK RIAMVNNFSA AGGNSTLAIE
EGPLRPKPAG AIDPRSSHLV TVSAKSKISL KGNLERLLSF LDAHPDVALS DLAYTTTARR
HHHNHRVAVA TSDIADLKAQ LCKTLESDSV NTLQPISATG PPPIAFAFTG QGSSYKSWDL
QLFQHSPYFR SQILHLDTLA QGQGFPSFVP AIDGSYPRDH AHCPVITQLA LVCTEIALAK
YWVSLGVTPD VVVGHSLGEY AALHIAGVLS ASDAIFLVGQ RACLLQERCQ PSSHQMMAVR
ASLEQIEQFA GSLPYEIACV NGPREMVLSG TREEMAAVAR LLEAEGFKCI VLEVAFAFHS
AQMDPILDEF EALAASGVVF QAPNLPVISP LLSKVVFDEH TIDSVYMRRA TRETVHFLSA
MKMAHKISTI DDATVWVEIG PHPVCVNFVR SSLPSTSVTV PSFRRGEDNW VTLTSSLGIL
HCAGVPVDWN EFHQPFERAL RLLDLPTYSW NEKTYWIQYQ GNWALTKGNT FYDDEAPQTK
ALAGLASELR TSTVQQIIHE QYDGAAGSVV MQSDLMQPDF LAAAYGHKMN GRGVVTSSIH
ADIAFTLGEY LYKKLNPNQE PHMNIANLEV VKALVAQENT KSPQLIQVSA STDNIRSRQA
HLKWHNVING SIEEPFASAT VYYEEASDWL ASWRPATHLV QGRIHALEQL AEDGVANRFT
RRMAYGLFAS SLVDYADKYR GMQSVVLHEL EAFADVVLTT EKGGTWTVPP YFIDSVAHLA
GFIMNVSDAN DTNANFCVTP GWSSMRFAAP LLPGSKYRSY VKMIPTVEDN NIYLGDVYIL
QDETIVGMVG GIKFRRYPRI LLNRFFSAPD ADARKSTPAT SAPAPAPPAG SEALQPKAAP
ASTPAAPASA DAPTTNGVKA AAEPDANSTA AKAIALVATE AGLGLSDLKD SASFSSLGID
SLMSLVISEK FRETLGVTVT GSLFLEYPTV GDLKSWLLEY YS


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