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Orsellinic acid synthase (OAS) (EC 2.3.1.-) (Non-reducing polyketide synthase orsA) (Orsellinic acid/F9775 biosynthesis cluster protein A)

 ORSA_EMENI              Reviewed;        2103 AA.
Q5AUX1; C8V4V0;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=Orsellinic acid synthase {ECO:0000303|PubMed:19666480};
Short=OAS {ECO:0000303|PubMed:19666480};
EC=2.3.1.- {ECO:0000269|PubMed:19666480, ECO:0000269|PubMed:20174687};
AltName: Full=Non-reducing polyketide synthase orsA {ECO:0000303|PubMed:20174687};
AltName: Full=Orsellinic acid/F9775 biosynthesis cluster protein A {ECO:0000303|PubMed:19666480};
Name=orsA {ECO:0000303|PubMed:19666480}; ORFNames=AN7909;
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]
INDUCTION.
PubMed=19448638; DOI=10.1038/nchembio.177;
Bok J.W., Chiang Y.M., Szewczyk E., Reyes-Dominguez Y., Davidson A.D.,
Sanchez J.F., Lo H.C., Watanabe K., Strauss J., Oakley B.R.,
Wang C.C., Keller N.P.;
"Chromatin-level regulation of biosynthetic gene clusters.";
Nat. Chem. Biol. 5:462-464(2009).
[4]
IDENTIFICATION OF THE ORS CLUSTER, INDUCTION, FUNCTION, DISRUPTION
PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
PubMed=19666480; DOI=10.1073/pnas.0901870106;
Schroeckh V., Scherlach K., Nuetzmann H.W., Shelest E.,
Schmidt-Heck W., Schuemann J., Martin K., Hertweck C., Brakhage A.A.;
"Intimate bacterial-fungal interaction triggers biosynthesis of
archetypal polyketides in Aspergillus nidulans.";
Proc. Natl. Acad. Sci. U.S.A. 106:14558-14563(2009).
[5]
FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, CATALYTIC ACTIVITY, AND
PATHWAY.
PubMed=20174687; DOI=10.1039/b904541d;
Sanchez J.F., Chiang Y.M., Szewczyk E., Davidson A.D., Ahuja M.,
Elizabeth Oakley C., Woo Bok J., Keller N., Oakley B.R., Wang C.C.;
"Molecular genetic analysis of the orsellinic acid/F9775 gene cluster
of Aspergillus nidulans.";
Mol. Biosyst. 6:587-593(2010).
[6]
INDUCTION.
PubMed=23892751; DOI=10.1128/AEM.01578-13;
Nuetzmann H.W., Fischer J., Scherlach K., Hertweck C., Brakhage A.A.;
"Distinct amino acids of histone H3 control secondary metabolism in
Aspergillus nidulans.";
Appl. Environ. Microbiol. 79:6102-6109(2013).
[7]
INDUCTION.
PubMed=23841751; DOI=10.1111/mmi.12326;
Bok J.W., Soukup A.A., Chadwick E., Chiang Y.M., Wang C.C.,
Keller N.P.;
"VeA and MvlA repression of the cryptic orsellinic acid gene cluster
in Aspergillus nidulans involves histone 3 acetylation.";
Mol. Microbiol. 89:963-974(2013).
-!- FUNCTION: Non-reducing polyketide synthase; part of the gene
cluster that mediates the biosynthesis of orsellinic acid, as well
as of the cathepsin K inhibitors F9775 A and F9775 B
(PubMed:19666480, PubMed:20174687). The non-reducing polyketide
synthase orsA produces orsellinic acid by condensing acetyl-CoA
with 3 malonyl-CoA units (PubMed:19666480, PubMed:20174687).
Further modifications by the decarboxylase orsB and the
tyrosinase-like protein orsC lead to the production of F9775 A and
F9775 B (PubMed:20174687). The functions of orsD and orsE remain
unclear since only orsB and orsC are required to convert
orsellinic acid into F9775 A and F9775 B (PubMed:20174687).
{ECO:0000269|PubMed:19666480, ECO:0000269|PubMed:20174687}.
-!- PATHWAY: Secondary metabolite biosynthesis.
{ECO:0000269|PubMed:19666480, ECO:0000269|PubMed:20174687}.
-!- INDUCTION: Expression is induced by an intimate physical
interaction of the fungal mycelia with the bacterium Streptomyces
hygroscopicus (PubMed:19666480). Expression is repressed by VeA
and MvlA via histone 3 acetylation by the SAGA/ADA complex
(PubMed:23892751, PubMed:23841751). {ECO:0000269|PubMed:19666480,
ECO:0000269|PubMed:23841751, ECO:0000269|PubMed:23892751}.
-!- 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}.
-!- DOMAIN: The release of the polyketide chain from the non-reducing
polyketide synthase is mediated by the thioesterase (TE) domain
localized at the C-ter of the protein (By similarity).
{ECO:0000250|UniProtKB:Q5ATJ7}.
-!- DISRUPTION PHENOTYPE: Abolishes the production of orsellinic acid,
lecanoric acid and F-9775A/B (PubMed:19666480, PubMed:20174687).
{ECO:0000269|PubMed:19666480, ECO:0000269|PubMed:20174687}.
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EMBL; BN001302; CBF73505.1; -; Genomic_DNA.
EMBL; AACD01000135; EAA59563.1; -; Genomic_DNA.
RefSeq; XP_681178.1; XM_676086.1.
ProteinModelPortal; Q5AUX1; -.
SMR; Q5AUX1; -.
STRING; 162425.CADANIAP00003928; -.
ESTHER; emeni-q5aux1; Thioesterase.
EnsemblFungi; CADANIAT00003928; CADANIAP00003928; CADANIAG00003928.
EnsemblFungi; EAA59563; EAA59563; AN7909.2.
GeneID; 2868938; -.
KEGG; ani:AN7909.2; -.
KO; K15416; -.
OMA; DDWREYN; -.
OrthoDB; EOG092C0150; -.
Proteomes; UP000000560; Chromosome II.
Proteomes; UP000005890; Unassembled WGS sequence.
GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
GO; GO:1900557; P:emericellamide biosynthetic process; IMP:AspGD.
GO; GO:1900611; P:F-9775A biosynthetic process; IMP:AspGD.
GO; GO:1900614; P:F-9775B biosynthetic process; IMP:AspGD.
GO; GO:1900815; P:monodictyphenone biosynthetic 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:0045461; P:sterigmatocystin biosynthetic process; IMP:AspGD.
GO; GO:1900590; P:violaceol I biosynthetic process; IMP:AspGD.
GO; GO:1900593; P:violaceol II biosynthetic process; IMP:AspGD.
Gene3D; 1.10.1200.10; -; 2.
Gene3D; 3.30.70.250; -; 1.
Gene3D; 3.40.47.10; -; 2.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
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; IPR006162; Ppantetheine_attach_site.
InterPro; IPR030918; PT_fungal_PKS.
InterPro; IPR032088; SAT.
InterPro; IPR001031; Thioesterase.
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; 2.
Pfam; PF14765; PS-DH; 1.
Pfam; PF16073; SAT; 1.
Pfam; PF00975; Thioesterase; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 2.
SUPFAM; SSF47336; SSF47336; 2.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53474; SSF53474; 2.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 2.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
Complete proteome; Multifunctional enzyme; Phosphopantetheine;
Phosphoprotein; Reference proteome; Repeat; Transferase.
CHAIN 1 2103 Orsellinic acid synthase.
/FTId=PRO_0000438572.
DOMAIN 1640 1716 Carrier 1. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
DOMAIN 1741 1815 Carrier 2. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
REGION 17 232 N-terminal acylcarrier protein
transacylase domain (SAT). {ECO:0000255,
ECO:0000305|PubMed:20174687}.
REGION 351 785 Ketosynthase (KS) domain. {ECO:0000255,
ECO:0000305|PubMed:20174687}.
REGION 881 1197 Malonyl-CoA:ACP transacylase (MAT)
domain. {ECO:0000255,
ECO:0000305|PubMed:20174687}.
REGION 1303 1579 Product template (PT) domain.
{ECO:0000255,
ECO:0000305|PubMed:20174687}.
REGION 1849 2082 Thioesterase (TE) domain. {ECO:0000255,
ECO:0000305|PubMed:20174687}.
COMPBIAS 1614 1623 Poly-Ser. {ECO:0000255}.
ACT_SITE 525 525 For beta-ketoacyl synthase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
ACT_SITE 973 973 For acyl/malonyl transferase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 1676 1676 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
MOD_RES 1775 1775 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
SEQUENCE 2103 AA; 225849 MW; 24941E20ABF74DB1 CRC64;
MAPNHVLFFP QERVTFDAVH DLNVRSKSRR RLQSLLAAAS NVVQHWTASL DGLERADIGS
FEDLVELAER QTTQTRGSIV ADLVLLTTVQ IGQLLVLAED DPAILSGHAG ARAIPMGFGA
GLVAAGVAAA ATSADGIVNL GLEAVSVAFR LGVELQRRGK DIEDSNGPWA QVISSATTIA
DLEQALDRIN ASLRPINQAY IGEVMTESTV VFGPPSTLDA LAKRPELAHA TITSPASALA
QVPLHGAHLP PISATMIAAS SSQQATELWK LAVEEVANKP IDVHQAVTAL IHDLHRANIT
DIVLTAIGAS TETSGIQSLL EKNGLAVELG QLSPTPRPYG NDLDSIPADA IAVVGMSGRF
PNSDTLDEFW RLLETATTTH QVIPESRFNV DDFYDPTRAK HNALLARYGC FLKNPGDFDH
RLFNISPREA MQMDPVQRML LMTTYEALEM AGYSPPTPAA PGDSEQAPPR IATYFGQTID
DWKSINDQQG IDTHYLPGVN RGFAPGRLSH FFQWAGGFYS IDTGCSSSAT ALCLARDALT
AGKYDAAVVG GGTLLTAPEW FAGLSQGGFL SPTGACKTYS DSADGYCRGE GVGVVILKRL
ADAVRSKDNV IAVIAGASRN CNAGAGSITY PGEKAQGALY RRVMRQAAVR PEQVDVVEMH
GTGTQAGDRV ETHAVQSVFA PSNGNQREKP LIVGALKANI GHSEAAAGII SLMKAILILQ
HDKIPAQPNQ PIKMNPYLEP LIGKQIQLAN GQSWTRNGAE PRYIFVNNFD AAGGNVSMLL
QDPPAFALPA PASGPGLRTH HVVVTSGRTA TAHEANRKRL HAYLSAHPDT NLADLAYTTT
ARRIHNVHRE AYVASSTSDL VRQLEKPLAD KVESAPPPAV VFTFTGQGAQ SLGMGGALYS
TSPTFRRLLD SLQSICEVQG LPTKFLNAIR GSGAEGATVT EVDMQVATVA LEIALARYWR
SLGIRPTVLI GHSLGEYAAL CVAGVLSASD ALALAFRRAT LIFTRCPPSE AAMLAVGLPM
RTVQYRIRDS AATTGCEVCC VNGPSSTVVG GPVAAIQALD EYLKSDGKVS TTRLRVQHAF
HTRQMDVLLD ELEASAAQVP FHAPTLPVAS TVLGRIVRPG EQGVFDANYL RRHTREPVAF
LDAVRACETE GLIPDRSFAV EIGPHPICIS LMATCLQSAK INAWPSLRRG GDDWQSVSST
LAAAHSAQLP VAWSEFHKDH LDTVRLISDL PTYAFDLKTF WHSYKTPAAA VSAASATPST
TGLSRLASTT LHAVEKLQRE EGKILGTFTV DLSDPKLAKA ICGHVVDESA ICPASIFIDM
AYTAAVFLEQ ENGAGAALNT YELSSLEMHS PLVLREDIEV LPQVWVEAVL DIKSNAVSVH
FKGQTSKGAV GYGSATMRLG QPDSAVRRDW SRIQSLVRAR VQTLNRSVRP REVHAMDTAL
FYKVFSEIVD YSAPYHAVQE AVIAADFHDA AVTLQLTPTA DLGTFTSSPF AVDALVHVAG
FLLNADVRRP KNEVHIANHI GSLRIVGDLS SPGPYHVYAT IREQDQKAGT SLCDVYTTDS
QDRLVAVCSD ICFKKLERDF FALLTGATRG RSTKPVAAAP AKSMAKRARQ LAPSPSPSSS
SGSNTPMSRS PTPSSVSDMV DLGTELLQAV AEQTGVSVAE MKSSPGTTFT EFGVDSQMAI
SILANFQRTT AVELPAAFFT NFPTPADAEA ELGGSALDDL EEDITKPTPS PEQTQARKQG
PAPSQHLLSL VAQALGLEAS DLTPSTTFDS VGMDSMLSIK ITAAFHAKTG IELPAAFFSA
NPTVGAAQEA LDDDAEEESA PAQTSTNPAK ETTIDSSRQH KLDAAVSRAS YIHLKALPKG
RRIYALESPF LEQPELFDLS IEEMATIFLR TIRRIQPHGP YLIGGWSAGS MYAYEVAHRL
TREGETIQAL IILDMRAPSL IPTSIVTTDF VDKLGTFEGI NRARDLPEDL SVKERAHLMA
TCRALSRYDA PAFPSDRQPK QVAVVWALLG LDNRPDAPIA SMGRPGLDIG KSMYEMNLDE
FERYFNSWFY GRRQQFGTNG WEDLLGDHIA VYTVNGDHFS MMCPPYASEV GDIVIETVTR
AVE


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