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Non-reducing polyketide synthase ausA (EC 2.3.1.-) (Austinol synthesis protein A) (Methylorcinaldehyde synthase ausA)

 AUSA_EMENI              Reviewed;        2476 AA.
Q5ATJ7; C8VE81;
08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=Non-reducing polyketide synthase ausA {ECO:0000303|PubMed:21658102};
EC=2.3.1.- {ECO:0000305|PubMed:21658102, ECO:0000305|PubMed:22329759};
AltName: Full=Austinol synthesis protein A {ECO:0000303|PubMed:22329759};
AltName: Full=Methylorcinaldehyde synthase ausA {ECO:0000303|PubMed:22329759};
Name=ausA {ECO:0000303|PubMed:21658102}; ORFNames=AN8383;
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, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-1660.
PubMed=21658102; DOI=10.1111/j.1574-6968.2011.02327.x;
Nielsen M.L., Nielsen J.B., Rank C., Klejnstrup M.L., Holm D.K.,
Brogaard K.H., Hansen B.G., Frisvad J.C., Larsen T.O., Mortensen U.H.;
"A genome-wide polyketide synthase deletion library uncovers novel
genetic links to polyketides and meroterpenoids in Aspergillus
nidulans.";
FEMS Microbiol. Lett. 321:157-166(2011).
[4]
FUNCTION.
PubMed=22234162; DOI=10.1021/cb200455u;
Rodriguez-Urra A.B., Jimenez C., Nieto M.I., Rodriguez J., Hayashi H.,
Ugalde U.;
"Signaling the induction of sporulation involves the interaction of
two secondary metabolites in Aspergillus nidulans.";
ACS Chem. Biol. 7:599-606(2012).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22329759; DOI=10.1021/ja209809t;
Lo H.C., Entwistle R., Guo C.J., Ahuja M., Szewczyk E., Hung J.H.,
Chiang Y.M., Oakley B.R., Wang C.C.;
"Two separate gene clusters encode the biosynthetic pathway for the
meroterpenoids austinol and dehydroaustinol in Aspergillus nidulans.";
J. Am. Chem. Soc. 134:4709-4720(2012).
[6]
FUNCTION.
PubMed=23865690; DOI=10.1021/ja405518u;
Matsuda Y., Awakawa T., Wakimoto T., Abe I.;
"Spiro-ring formation is catalyzed by a multifunctional dioxygenase in
austinol biosynthesis.";
J. Am. Chem. Soc. 135:10962-10965(2013).
[7]
DOMAIN, AND MUTAGENESIS OF SER-2251; ASP-2413 AND HIS-2445.
PubMed=23368695; DOI=10.1021/ol303328t;
Yeh H.H., Chang S.L., Chiang Y.M., Bruno K.S., Oakley B.R., Wu T.K.,
Wang C.C.;
"Engineering fungal nonreducing polyketide synthase by heterologous
expression and domain swapping.";
Org. Lett. 15:756-759(2013).
-!- FUNCTION: Non-reducing polyketide synthase; part of the gene
cluster A that mediates the biosynthesis of austinol and
dehydroaustinol, two fungal meroterpenoids (PubMed:22329759). The
first step of the pathway is the synthesis of 3,5-
dimethylorsellinic acid by the polyketide synthase ausA
(PubMed:22329759). 3,5-dimethylorsellinic acid is then prenylated
by the polyprenyl transferase ausN (PubMed:22329759). Further
epoxidation by the FAD-dependent monooxygenase ausM and
cyclization by the probable terpene cyclase ausL lead to the
formation of protoaustinoid A (PubMed:22329759). Protoaustinoid A
is then oxidized to spiro-lactone preaustinoid A3 by the combined
action of the FAD-binding monooxygenases ausB and ausC, and the
dioxygenase ausE (PubMed:22329759, PubMed:23865690). Acid-
catalyzed keto-rearrangement and ring contraction of the
tetraketide portion of preaustinoid A3 by ausJ lead to the
formation of preaustinoid A4 (PubMed:22329759). The aldo-keto
reductase ausK, with the help of ausH, is involved in the next
step by transforming preaustinoid A4 into isoaustinone which is in
turn hydroxylated by the P450 monooxygenase ausI to form
austinolide (PubMed:22329759). Finally, the cytochrome P450
monooxygenase ausG modifies austinolide to austinol
(PubMed:22329759). Austinol can be further modified to
dehydroaustinol which forms a diffusible complex with diorcinol
that initiates conidiation (PubMed:22234162, PubMed:22329759).
{ECO:0000269|PubMed:22234162, ECO:0000269|PubMed:22329759,
ECO:0000269|PubMed:23865690}.
-!- PATHWAY: Secondary metabolite biosynthesis; terpenoid
biosynthesis. {ECO:0000269|PubMed:21658102,
ECO:0000269|PubMed:22329759}.
-!- 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
(PubMed:22329759). {ECO:0000250|UniProtKB:Q5B0D0,
ECO:0000305|PubMed:22329759}.
-!- DOMAIN: The release of the polyketide chain from the non-reducing
polyketide synthase is mediated by the thioesterase (TE) domain
localized at the C-terminus of the protein (PubMed:23368695).
{ECO:0000269|PubMed:23368695}.
-!- DISRUPTION PHENOTYPE: Impairs the synthesis of austinol and
dehydroaustinol (PubMed:21658102, PubMed:22329759).
{ECO:0000269|PubMed:21658102, ECO:0000269|PubMed:22329759}.
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EMBL; BN001305; CBF80428.1; -; Genomic_DNA.
EMBL; AACD01000153; EAA67005.1; -; Genomic_DNA.
RefSeq; XP_681652.1; XM_676560.1.
ProteinModelPortal; Q5ATJ7; -.
SMR; Q5ATJ7; -.
ESTHER; emeni-q5atj7; Hormone-sensitive_lipase_like.
EnsemblFungi; CADANIAT00002854; CADANIAP00002854; CADANIAG00002854.
EnsemblFungi; EAA67005; EAA67005; AN8383.2.
GeneID; 2868762; -.
KEGG; ani:AN8383.2; -.
HOGENOM; HOG000137555; -.
OMA; INLPPYQ; -.
OrthoDB; EOG092C00JV; -.
UniPathway; UPA00213; -.
Proteomes; UP000000560; Chromosome V.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.30.70.250; -; 1.
Gene3D; 3.40.47.10; -; 2.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR013094; AB_hydrolase_3.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR013217; Methyltransf_12.
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; IPR006162; Ppantetheine_attach_site.
InterPro; IPR029063; SAM-dependent_MTases.
InterPro; IPR016039; Thiolase-like.
Pfam; PF07859; Abhydrolase_3; 1.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF08242; Methyltransf_12; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00826; PKS_DH; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53335; SSF53335; 1.
SUPFAM; SSF53474; SSF53474; 3.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
Complete proteome; Methyltransferase; Multifunctional enzyme;
Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 2476 Non-reducing polyketide synthase ausA.
/FTId=PRO_0000436482.
DOMAIN 1626 1700 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 14 253 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255}.
REGION 379 742 Ketosynthase (KS) domain. {ECO:0000255}.
REGION 906 1210 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255}.
REGION 1280 1583 Product template (PT) domain.
{ECO:0000255}.
REGION 1862 2095 Methyltransferase (CMeT) domain.
{ECO:0000255}.
REGION 2128 2476 Thioesterase (TE) domain.
{ECO:0000269|PubMed:23368695}.
ACT_SITE 544 544 For beta-ketoacyl synthase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 993 993 For acyl/malonyl transferase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 2251 2251 For thioesterase activity.
{ECO:0000269|PubMed:23368695}.
ACT_SITE 2413 2413 For thioesterase activity.
{ECO:0000269|PubMed:23368695}.
ACT_SITE 2445 2445 For thioesterase activity.
{ECO:0000269|PubMed:23368695}.
MOD_RES 1660 1660 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
MUTAGEN 1660 1660 S->A: Impairs the production of austinol
and dehydroaustinol.
{ECO:0000269|PubMed:21658102}.
MUTAGEN 2251 2251 S->A: Abolishes the function of the TE
domain. {ECO:0000269|PubMed:23368695}.
MUTAGEN 2413 2413 D->N: Abolishes the function of the TE
domain. {ECO:0000269|PubMed:23368695}.
MUTAGEN 2445 2445 H->F: Abolishes the function of the TE
domain. {ECO:0000269|PubMed:23368695}.
SEQUENCE 2476 AA; 271827 MW; 1CFA270B5B7E319E CRC64;
MGSLDDNTLQ QVSVLFGPKY PEVELPAGHI RRYLSNQRNA NWLHDAIRDL PSVWHDILRL
WPAAEKLHGD ARLRQLSAFL GGGTLRPDMA EPMNFLLVPA TVLRHLVDFL ELKEDKNYDV
CDIQGFCVGF LAAIAAACWS DNEDEFGKVV STVLRLAVYI GAAVDLDELC EQPARSIAVR
WRTAQEHKLL TEVLTRYQGA YISCVTDENA VTVTVWDSQS VSFAKELEKH GLSVKTTTLR
GRFHHSNHTQ AVEDILQSCE RNSRLCLPSK CHKRSLPRSN INGRVCEADS LFTVAVESIL
TTQANWKITV TATLDNMGQS DARSIIPIGA GQFVPRHARC RMLNIVEFNK GEHINGRRKM
QSATALDVGV NVTAPETTAV PIAVTGMACR YPQADSVEEL WRILDLGQCT VSPMPNSRLK
SGSLQREPKG PFFGNYLARP DAFDHRFFGI SAREAESMDP QQRVLLQVAY EAMESAGYCG
LRRSKLPDDI GCYVGVGCDD YSENVGSRNA TAFSATGTLQ AFNSGRISHY FGWSGPSVTV
DTACSSAAVA IHLACQAIRT NDCAIAVAGG VNIMTDPRWS QNLAGASFLS PTGASKAFDA
DANGYCRGEG AGLLVLRPLE AALRDGDPIH AVITGTSVNQ GANCSPITVP DSNSQRSLYL
KALSLSGLTP DVVGYVEAHG TGTQVGDPIE FESIRKTFSG PNRATKLYVG SIKDNIGHTE
TSSGVAGMLK TILMIQKRRI PKQANFRRLN PRITLNERNH IEIPTQSIDW EAEKRVAMVT
NYGAAGSNAA IVLREPASTP ATSNSAHRET LPSHVPFYVS ARTEESLRSY CEALQSTIRE
VAQSGTNTVQ HIAYNLARKQ NRDMEHFVTF PAAAGEPSEL MTRLGSIASA HTQVERRSQS
FHPVIICFGG QTGDTASISR NLFESCELLR FHVDECENAC NALDLPSLFP AIVSPFPNKD
IVNLHCVLFS IQYATAKAWL DSGLQVTRMI GHSFGQLTAL CVAGGLSLID GMRLVATRAQ
LIQKHWGPHT GVMLSLRASK EKVQALLDAA SGHADLACLN GPDNFVVAGD EESIRRIEII
ATEKGMHVEL KRLKNTHAFH SRLVDAILPG LSEVANTLTF RQLDIPVEAC AEQEDDWLWV
TGDKIVQHSR KPVFFHDAVE RTLSRVDGPC VWLEAGTASP VINMVRRVVE ASRPLKSHVY
LPTDLSGAQA QANLAKVTCT LWSKAVPVQF WPFHPSETGY RWINLPPYQF AKTSHWIEYN
PDAFRSPPQV PDQENVQEAS LVRLLRQDGK EALFTINNKD NVFRMCTAGH AVANQNLCPA
SLYFELVVQA ALLVSSTATK PTMYHIESLN ICSPLVLGMP GAVLLQLTQQ DESHGQWSFV
LSTRDGLQDA VTHATGRVSL QAAGSNTGIC ARLSSLQRLL NLASWNSIAT SPSSSGLKRS
TVYQAFARAV NYADYYRGVE EVYAVGHEAT GRVILPSSPT KCNPCDPILI DNFIQVAGIH
VNCLSETHDD EVFVCSSVGD VLIGESFVRR DTAATVPWAV YSNYEPESKK KIVCDVFVLD
HTTGALAVCM LSATFTGVSI QSLKRTLNRL SNHTARPTEA EQVSINVAAE ATALSSTPVA
HVSSSDGDLL AVQTMLGELL GISADELSAA AALGDIGVDS LMSTEVLTEI NKRFGVAISN
AELTQIPDVG GLVQRIFPGH SVVRIKTHSQ GAVETEITIT DREPKSISVD LAPVCDTSPT
AFVDKASKLF ATTRTSAEFS RKTRFAGFCD TVFPQQMELV TSYVVEAFHA LGADLASLTP
GQVVPPVKIL PQHGKVMNQL VAVLEYSDLI ERRESEIIRS QQPVGTVPSL ILYKKILNKH
AQHASEHKLL HTTGSRLAEC LSGKADPLSL LFQNAEARAL MTDVYSNAPM FKSATIQLAQ
YLKDLLFNLG TQREIKVLEI GAGTGGTTNY LVQELAAVPG LRFQYTFTDI SSSLVTLARK
RFKAYDFMRY TTLDIENDPS PELQGQYDII ISTNCIHATR NLITSCTNIR RLLRPEGILC
LIELTRNLFW FDLVFGLLEG WWLFNDGRSH ALAHERLWDH NLRQAGFNWV DWTDNDSAES
DILRLIVASS TQPFYALEGD DECEADCNTV QEQTVLYNTR DGLELFADIY YPEKTDRSGA
KRPIALLIHG GGHIMLSRKE IHHEQVRMLF DMGFLPVSID YRLCPEVSLL DGPMQDACDA
LAWARNKLPQ LQLQRRDILP DGNNVVAVGW STGGHLAMTL AWTAPARGVS APEAILSFYS
PTDYTDPFWS KPNFPYRVDV STSDIQTGNP LDALQDAPIS GYNPPPSKRA LGGWMAPSDP
RSRIALYMNW TGQTLPVLFY GCNYRARAAE SGQDYEVVLP EPILSEVQKV CPFSQISAGS
YRAPTFLIHG TLDDLIPVQQ AQRTHDKMQA CGVDSDLRIV RDGLHLFDLE ANFAGNQHAF
QAVVDGYEFL RRHVGL


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U0167p CLIA Glutathione-independent PGD synthase,Lipocalin-type prostaglandin-D synthase,PGD2 synthase,PGDS,PGDS2,Pig,Prostaglandin-D2 synthase,Prostaglandin-H2 D-isomerase,PTGDS,Sus scrofa 96T


 

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