(data stored in SCRATCH zone)

SWISSPROT: ENCA_ASPFU

ID   ENCA_ASPFU              Reviewed;        1775 AA.
AC   Q4W944;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 95.
DE   RecName: Full=Atrochrysone carboxylic acid synthase {ECO:0000305|PubMed:22492455};
DE            Short=ACAS {ECO:0000305|PubMed:22492455};
DE            EC=2.3.1.- {ECO:0000269|PubMed:22492455};
DE   AltName: Full=Endocrocin synthesis protein A {ECO:0000303|PubMed:22492455};
DE   AltName: Full=Non-reducing polyketide synthase encA {ECO:0000303|PubMed:22492455};
GN   Name=encA {ECO:0000303|PubMed:22492455}; ORFNames=AFUA_4G00210;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   BIOTECHNOLOGY.
RX   PubMed=20379952; DOI=10.1055/s-0030-1249779;
RA   Gautam R., Karkhile K.V., Bhutani K.K., Jachak S.M.;
RT   "Anti-inflammatory, cyclooxygenase (COX)-2, COX-1 inhibitory, and free
RT   radical scavenging effects of Rumex nepalensis.";
RL   Planta Med. 76:1564-1569(2010).
RN   [3]
RP   FUNCTION.
RX   PubMed=22492455; DOI=10.1128/aem.07710-11;
RA   Lim F.Y., Hou Y., Chen Y., Oh J.H., Lee I., Bugni T.S., Keller N.P.;
RT   "Genome-based cluster deletion reveals an endocrocin biosynthetic pathway
RT   in Aspergillus fumigatus.";
RL   Appl. Environ. Microbiol. 78:4117-4125(2012).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=23592999; DOI=10.1371/journal.ppat.1003289;
RA   Berthier E., Lim F.Y., Deng Q., Guo C.J., Kontoyiannis D.P., Wang C.C.,
RA   Rindy J., Beebe D.J., Huttenlocher A., Keller N.P.;
RT   "Low-volume toolbox for the discovery of immunosuppressive fungal secondary
RT   metabolites.";
RL   PLoS Pathog. 9:E1003289-E1003289(2013).
RN   [5]
RP   INDUCTION.
RX   PubMed=26242966; DOI=10.1111/1462-2920.13007;
RA   Throckmorton K., Lim F.Y., Kontoyiannis D.P., Zheng W., Keller N.P.;
RT   "Redundant synthesis of a conidial polyketide by two distinct secondary
RT   metabolite clusters in Aspergillus fumigatus.";
RL   Environ. Microbiol. 18:246-259(2016).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of endocrocin, a simple anthraquinone
CC       interesting for many biotechnological applications (PubMed:22492455,
CC       PubMed:23592999). The pathway begins with the synthesis of atrochrysone
CC       thioester by the polyketide synthase (PKS) encA (PubMed:22492455). The
CC       atrochrysone carboxyl ACP thioesterase encB then breaks the thioester
CC       bond and releases the atrochrysone carboxylic acid from encA
CC       (PubMed:22492455). The atrochrysone carboxylic acid is then converted
CC       to endocrocin anthrone which is further oxidized into endocrocin by the
CC       anthrone oxygenase encC (PubMed:22492455). The exact function of encD
CC       has not been identified yet, but it negatively regulates endocrocin
CC       production, likely through the modification of endocrocin itself
CC       (PubMed:22492455). {ECO:0000269|PubMed:22492455,
CC       ECO:0000269|PubMed:23592999}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:22492455}.
CC   -!- TISSUE SPECIFICITY: Endocrocin is specifically produced in conidia.
CC       {ECO:0000305|PubMed:23592999}.
CC   -!- INDUCTION: Expression is positively regulated by the transcription
CC       factors brlA and laeA (PubMed:26242966). {ECO:0000269|PubMed:26242966}.
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: Abolishes the production of endocrocin
CC       (PubMed:22492455, PubMed:23592999). Leads to attenuated virulence in a
CC       toll-deficient Drosophila invasive aspergillosis model
CC       (PubMed:23592999). {ECO:0000269|PubMed:22492455,
CC       ECO:0000269|PubMed:23592999}.
CC   -!- BIOTECHNOLOGY: Endocrocin and related anthraquinones compounds have
CC       interesting activities for medicinal uses, including anti-inflammatory
CC       activity (PubMed:20379952). {ECO:0000269|PubMed:20379952}.
DR   EMBL; AAHF01000017; EAL84397.1; -; Genomic_DNA.
DR   RefSeq; XP_746435.1; XM_741342.1.
DR   SMR; Q4W944; -.
DR   STRING; 746128.CADAFUBP00009780; -.
DR   EnsemblFungi; EAL84397; EAL84397; AFUA_4G00210.
DR   GeneID; 3503726; -.
DR   KEGG; afm:AFUA_4G00210; -.
DR   EuPathDB; FungiDB:Afu4g00210; -.
DR   HOGENOM; HOG000168774; -.
DR   InParanoid; Q4W944; -.
DR   OMA; IALCRLW; -.
DR   OrthoDB; 68112at2759; -.
DR   Proteomes; UP000002530; Chromosome 4.
DR   Proteomes; UP000002530; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:1900602; P:endocrocin biosynthetic process; IMP:AspGD.
DR   GO; GO:0009405; P:pathogenesis; IMP:AspGD.
DR   GO; GO:0019748; P:secondary metabolic process; NAS: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; IPR032821; KAsynt_C_assoc.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR020801; PKS_acyl_transferase.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
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; PF16073; SAT; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00825; PKS_KS; 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   1: Evidence at protein level;
DR   PRODOM; Q4W944.
DR   SWISS-2DPAGE; Q4W944.
KW   Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   CHAIN           1..1775
FT                   /note="Atrochrysone carboxylic acid synthase"
FT                   /id="PRO_0000437047"
FT   DOMAIN          1698..1775
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          29..258
FT                   /note="N-terminal acylcarrier protein transacylase domain
FT                   (SAT)"
FT                   /evidence="ECO:0000255"
FT   REGION          394..824
FT                   /note="Ketosynthase (KS) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          921..1241
FT                   /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT                   /evidence="ECO:0000255"
FT   REGION          1305..1626
FT                   /note="Product template (PT) domain"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        564
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         1735
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   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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