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Atrochrysone carboxylic acid synthase (ACAS) (EC 2.3.1.-) (Endocrocin synthesis protein A) (Non-reducing polyketide synthase encA)

 ENCA_ASPFU              Reviewed;        1775 AA.
Q4W944;
07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 1.
25-OCT-2017, entry version 86.
RecName: Full=Atrochrysone carboxylic acid synthase {ECO:0000305|PubMed:22492455};
Short=ACAS {ECO:0000305|PubMed:22492455};
EC=2.3.1.- {ECO:0000269|PubMed:22492455};
AltName: Full=Endocrocin synthesis protein A {ECO:0000303|PubMed:22492455};
AltName: Full=Non-reducing polyketide synthase encA {ECO:0000303|PubMed:22492455};
Name=encA {ECO:0000303|PubMed:22492455}; ORFNames=AFUA_4G00210;
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]
BIOTECHNOLOGY.
PubMed=20379952; DOI=10.1055/s-0030-1249779;
Gautam R., Karkhile K.V., Bhutani K.K., Jachak S.M.;
"Anti-inflammatory, cyclooxygenase (COX)-2, COX-1 inhibitory, and free
radical scavenging effects of Rumex nepalensis.";
Planta Med. 76:1564-1569(2010).
[3]
FUNCTION.
PubMed=22492455; DOI=10.1128/AEM.07710-11;
Lim F.Y., Hou Y., Chen Y., Oh J.H., Lee I., Bugni T.S., Keller N.P.;
"Genome-based cluster deletion reveals an endocrocin biosynthetic
pathway in Aspergillus fumigatus.";
Appl. Environ. Microbiol. 78:4117-4125(2012).
[4]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=23592999; DOI=10.1371/journal.ppat.1003289;
Berthier E., Lim F.Y., Deng Q., Guo C.J., Kontoyiannis D.P.,
Wang C.C., Rindy J., Beebe D.J., Huttenlocher A., Keller N.P.;
"Low-volume toolbox for the discovery of immunosuppressive fungal
secondary metabolites.";
PLoS Pathog. 9:E1003289-E1003289(2013).
[5]
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 endocrocin, a simple
anthraquinone interesting for many biotechnological applications
(PubMed:22492455, PubMed:23592999). The pathway begins with the
synthesis of atrochrysone thioester by the polyketide synthase
(PKS) encA (PubMed:22492455). The atrochrysone carboxyl ACP
thioesterase encB then breaks the thioester bond and releases the
atrochrysone carboxylic acid from encA (PubMed:22492455). The
atrochrysone carboxylic acid is then converted to endocrocin
anthrone which is further oxidized into endocrocin by the anthrone
oxygenase encC (PubMed:22492455). The exact function of encD has
not been identified yet, but it negatively regulates endocrocin
production, likely through the modification of endocrocin itself
(PubMed:22492455). {ECO:0000269|PubMed:22492455,
ECO:0000269|PubMed:23592999}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:22492455}.
-!- TISSUE SPECIFICITY: Endocrocin is specifically produced in
conidia. {ECO:0000305|PubMed:23592999}.
-!- 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: Abolishes the production of endocrocin
(PubMed:22492455, PubMed:23592999). Leads to attenuated virulence
in a toll-deficient Drosophila invasive aspergillosis model
(PubMed:23592999). {ECO:0000269|PubMed:22492455,
ECO:0000269|PubMed:23592999}.
-!- BIOTECHNOLOGY: Endocrocin and related anthraquinones compounds
have interesting activities for medicinal uses, including anti-
inflammatory activity (PubMed:20379952).
{ECO:0000269|PubMed:20379952}.
-----------------------------------------------------------------------
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EMBL; AAHF01000017; EAL84397.1; -; Genomic_DNA.
RefSeq; XP_746435.1; XM_741342.1.
ProteinModelPortal; Q4W944; -.
SMR; Q4W944; -.
STRING; 5085.CADAFUBP00009780; -.
EnsemblFungi; CADAFUAT00002448; CADAFUAP00002448; CADAFUAG00002448.
GeneID; 3503726; -.
KEGG; afm:AFUA_4G00210; -.
EuPathDB; FungiDB:Afu4g00210; -.
HOGENOM; HOG000168774; -.
InParanoid; Q4W944; -.
OMA; IALCRLW; -.
OrthoDB; EOG092C01G3; -.
Proteomes; UP000002530; Chromosome 4.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:1900602; P:endocrocin biosynthetic process; IMP:AspGD.
GO; GO:0009405; P:pathogenesis; IMP:AspGD.
GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
Gene3D; 1.10.1200.10; -; 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; 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; PF16073; SAT; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00825; PKS_KS; 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.
1: Evidence at protein level;
Complete proteome; Multifunctional enzyme; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1775 Atrochrysone carboxylic acid synthase.
/FTId=PRO_0000437047.
DOMAIN 1698 1775 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 29 258 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255}.
REGION 394 824 Ketosynthase (KS) domain. {ECO:0000255}.
REGION 921 1241 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255}.
REGION 1305 1626 Product template (PT) domain.
{ECO:0000255}.
ACT_SITE 564 564 {ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 1735 1735 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 1775 AA; 194076 MW; 26F725DCAA4E1B11 CRC64;
MQGPSQLALF YFANGLPPDD IQDLFQRLRS QSKTESGWTL RAFVVQATNA LREEIRQLPH
HLRNPLTPLD NALDLAVVPD WRRGPLAGAL EGVLLCLIEI GSLIAYYERT PDPFKFSART
ACFTGIGTGL LAAAAAAASP TLADLPRLGA AAVRIALRMG VLVAETSQSV EAREPDAPAD
NWAAVVMDLD EDTVREELNL FNASTNNLGP SRLFISAGGT DNVTISGPPS KLRQVFRVSE
KLRSARYAQL PVYGGLCHAP HLYNCHHWTW IMEPINGAAF NQNMVDTAPL FSAGDDVPFE
ASTPRQLFES VVCDLLMGMI RWNRAVDGVV ELLGQTLPSE CQVYAFRPCA VVTGMVASGQ
VKLPHCQFQT HDLLGWTCHD DTDNGPTCRE DSSIAIVGMA CRFPGGANDL NQFWDLLEQG
ADVHRRVPAD RYDVESHTDT SGKSRNTSLT PFGCFIDQPG LFDAGFFDMS PREAMQTDPM
HRLALMTAYE ALEQAGFVPN RTESTHLKRI GTFYGQSCDD YREANAGQEV DTYYIPGGCR
AFAPGRINYF FKFSGPSFDC DTACSSSLAT IQMACTSLQH GDTNMAVAGG LNILTNSDGF
AGLSRGHFLS KTGGCKTFDC NADGYCRADG IGSIVLKRLD DAQRDNDHIF GIILAAATNH
SARAISITHP HAPSQAELYR DILTRAGVSP LDVDFIEMHG TGTQAGDSTE MESITSVFSP
GVPKRSRPLY IGSVKANVGH GEAAAGVMSL IKVLLVLQRQ AIPKHVGIKT ALNPRFPNLD
RLNVRIPHDQ VPWPRSPTRK RYALVNNFSA AGGNTSLLIE EPPVRPEPKA DPRAAFTVAV
SAKSKASLKN NLRSFLAYLE SQPSISLAHL SYTTTARRMH HNHRIAVHGS TLSSIMQELE
PYLPAVDTHR PVPNTPPSIA FVFSGQGSFY TGIARQLYEH HPGFRLQITR LHNICLSHGF
PSFRRAITGD LSNDGSEAEP IITHLTIVCV SIALCRLWET LGVKPCVVAG ASLGEFAALY
AAGVLSASDA IYLVGRRAQL LQELCTPNTH AMLAVRATVE QIRNVLAGQP YEVACINGSS
DITLSCSVAD IINLQLAIEQ HGYKCTRLDV PFAFHSAQMD PLLGPFEHIA RGVTFKAPNI
PVMSPSLGDC VFDGKTINAS YMCNVTRNPV KFVDALETAR GMDLVDAKTV WVEIGPHASY
SRFVGSAMPP GTATIASLNR NEDNWSTFAR SMAQLHNLGV DLNWHEWHAP FESELRLLTD
LPAYQWNMKN YWIQYNGDWM LRKDGKSSAA AASHPHQAIP PALRTSLVHR LVCESVQETR
VEVIVESDIL HPDFFEAMNG HRMNGCAVAT TAIHADIAFT LAKYLYSSIM PNSTDAPAIN
VKNMQVQHGL VARKDRSRPQ LIRIRGIADV TRGLVSLSWH LVDEQGRRVE ESFATAVAEF
GNHEAWLEEW SPMTHLVVSR IDVLQRLADD GTANRLSRDM VYMLFNNLVD YAEKYRGMQM
VVLHGLEAMA NVTLAAPEQS GGKWTVAPHY IDSVVHLAGF ILNGGNGLDP RRNFYVTPGW
KSMRFARPLV PGVRYQSYVK MMPIREQSGF YAGDVYILHE GQIVGLVGGI TFRTFPRSLI
NTFFSPPDTM THGGSQAGSV HQPACSERTL PVGPARQDSA ARETLCQGHG LSRTVMDSSD
SSPATTLTPP TLPSVAASTE SPIVHRAMAL IAAETAIELT ELSDETAFSS IGVDSLLSLV
LAEKFTAEFH LDFRSSLFLD CPTIGDLKAW LIDYC


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