WA_EMENI
ID WA_EMENI Reviewed; 2157 AA.
AC Q03149; C8V774; Q5AU21;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Conidial yellow pigment biosynthesis polyketide synthase {ECO:0000303|PubMed:11251292};
DE Short=PKS {ECO:0000303|PubMed:11251292};
DE EC=2.3.1.- {ECO:0000269|PubMed:11251292};
GN Name=wA {ECO:0000303|PubMed:11251292}; ORFNames=AN8209;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=1465094; DOI=10.1007/bf00279362;
RA Mayorga M.E., Timberlake W.E.;
RT "The developmentally regulated Aspergillus nidulans wA gene encodes a
RT polypeptide homologous to polyketide and fatty acid synthases.";
RL Mol. Gen. Genet. 235:205-212(1992).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS, AND FUNCTION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RA Watanabe A., Fujii I., Sankawa U., Mayorga M.E., Timberlake W.E.,
RA Ebizuka Y.;
RT "Re-identification of Aspergillus nidulans wA gene to code for a polyketide
RT synthase of naphthopyrone.";
RL Tetrahedron Lett. 40:91-94(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, ACTIVE SITE, AND MUTAGENESIS OF
RP SER-1682; SER-1804; SER-1967 AND HIS-2129.
RX PubMed=11251292; DOI=10.1016/s1074-5521(00)90068-1;
RA Fujii I., Watanabe A., Sankawa U., Ebizuka Y.;
RT "Identification of Claisen cyclase domain in fungal polyketide synthase WA,
RT a naphthopyrone synthase of Aspergillus nidulans.";
RL Chem. Biol. 8:189-197(2001).
CC -!- FUNCTION: Non-reducing polyketide synthase that condenses acetate units
CC to form a heptaketide naphthopyrene YWA1, a yellow pigment found in
CC mature asexual spores (conidia), via a polyketomethylene intermediate
CC step. {ECO:0000269|PubMed:11251292, ECO:0000269|PubMed:1465094,
CC ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 6 H(+) + 6 malonyl-CoA = 6 CO2 + 7 CoA + H2O +
CC YWA1; Xref=Rhea:RHEA:62652, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:133763;
CC Evidence={ECO:0000269|PubMed:11251292};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC Evidence={ECO:0000269|PubMed:11251292};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Note=Binds 2 phosphopantetheines covalently.
CC {ECO:0000269|PubMed:11251292};
CC -!- PATHWAY: Polyketide biosynthesis; heptaketide naphthopyrone YWA1
CC biosynthesis.
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 2 acyl-carrier protein (ACP) domains
CC that serve as the tethers of the growing and completed polyketide via
CC their phosphopantetheinyl arm. {ECO:0000250|UniProtKB:Q5B0D0}.
CC -!- DOMAIN: The C-terminal region is involved in Claisen-type cyclization
CC of the second ring of naphthopyrone. {ECO:0000269|PubMed:11251292}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA58778.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X65866; CAA46695.2; -; Genomic_DNA.
DR EMBL; AACD01000143; EAA58778.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001302; CBF74114.1; -; Genomic_DNA.
DR PIR; S28353; S28353.
DR RefSeq; XP_681478.1; XM_676386.1.
DR AlphaFoldDB; Q03149; -.
DR SMR; Q03149; -.
DR STRING; 162425.CADANIAP00004256; -.
DR EnsemblFungi; CBF74114; CBF74114; ANIA_08209.
DR EnsemblFungi; EAA58778; EAA58778; AN8209.2.
DR GeneID; 2868945; -.
DR KEGG; ani:AN8209.2; -.
DR VEuPathDB; FungiDB:AN8209; -.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_16_2_1; -.
DR InParanoid; Q03149; -.
DR OMA; VCVYGLN; -.
DR OrthoDB; 68112at2759; -.
DR BioCyc; MetaCyc:MON-19453; -.
DR UniPathway; UPA00167; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0052716; F:hydroquinone:oxygen oxidoreductase activity; IMP:AspGD.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0048315; P:conidium formation; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0046148; P:pigment biosynthetic process; IMP:AspGD.
DR GO; GO:0043324; P:pigment metabolic process involved in developmental pigmentation; IMP:AspGD.
DR GO; GO:0019748; P:secondary metabolic process; NAS:AspGD.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 2.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR030918; PT_fungal_PKS.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF16073; SAT; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR TIGRFAMs; TIGR04532; PT_fungal_PKS; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Conidiation; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Sporulation; Transferase.
FT CHAIN 1..2157
FT /note="Conidial yellow pigment biosynthesis polyketide
FT synthase"
FT /id="PRO_0000180305"
FT DOMAIN 1645..1722
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1767..1844
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 8..244
FT /note="N-terminal acylcarrier protein transacylase domain
FT (SAT)"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11251292"
FT REGION 379..810
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11251292"
FT REGION 912..1232
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11251292"
FT REGION 1290..1603
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1607..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1725..1760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..2149
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000269|PubMed:11251292"
FT COMPBIAS 1608..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1851..1888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 548
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1001
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1967
FT /note="For thioesterase activity"
FT /evidence="ECO:0000269|PubMed:11251292"
FT MOD_RES 1682
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1804
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MUTAGEN 1682
FT /note="S->A: Fails to form the naphthopyrene YWA1; when
FT associated with A-1804."
FT /evidence="ECO:0000269|PubMed:11251292"
FT MUTAGEN 1682
FT /note="S->C,A: Forms the naphthopyrene YWA1."
FT /evidence="ECO:0000269|PubMed:11251292"
FT MUTAGEN 1682
FT /note="S->C: Fails to form the naphthopyrene YWA1; when
FT associated with C-1804."
FT /evidence="ECO:0000269|PubMed:11251292"
FT MUTAGEN 1804
FT /note="S->A: Fails to form the naphthopyrene YWA1; when
FT associated with A-1682."
FT /evidence="ECO:0000269|PubMed:11251292"
FT MUTAGEN 1804
FT /note="S->C,A: Forms the naphthopyrene YWA1."
FT /evidence="ECO:0000269|PubMed:11251292"
FT MUTAGEN 1804
FT /note="S->C: Fails to form the naphthopyrene YWA1; when
FT associated with C-1682."
FT /evidence="ECO:0000269|PubMed:11251292"
FT MUTAGEN 1967
FT /note="S->A: Required for Claisen-type cyclization of the
FT final product."
FT /evidence="ECO:0000269|PubMed:11251292"
FT MUTAGEN 2129
FT /note="H->Q: Required for Claisen-type cyclization of the
FT final product."
FT /evidence="ECO:0000269|PubMed:11251292"
SQ SEQUENCE 2157 AA; 235604 MW; BD35334B4FD7530A CRC64;
MEDPYRVYLF GDQTGDFEVG LRRLLQAKNH SLLSSFLQRS YHAVRQEISH LPPSERSTFP
RFTSIGDLLA RHCESPGNPA IESVLTCIYQ LGCFINYYGD LGHTFPSHSQ SQLVGLCTGL
LSCAAVSCAS NIGELLKPAV EVVVVALRLG LCVYRVRKLF GQDQAAPLSW SALVSGLSES
EGTSLIDKFT RRNVIPPSSR PYISAVCANT LTISGPPVVL NQFLDTFISG KNKAVMVPIH
GPFHASHLYE KRDVEWILKS CNVETIRNHK PRIPVLSSNT GELIVVENME GFLKIALEEI
LLRQMSWDKV TDSCISILKS VGDNKPKKLL PISSTATQSL FNSLKKSNLV NIEVDGGISD
FAAETQLVNQ TGRAELSKIA IIGMSGRFPE ADSPQDFWNL LYKGLDVHRK VPEDRWDADA
HVDLTGTATN TSKVPYGCWI REPGLFDPRF FNMSPREALQ ADPAQRLALL TAYEALEGAG
FVPDSTPSTQ RDRVGIFYGM TSDDYREVNS GQDIDTYFIP GGNRAFTPGR INYYFKFSGP
SVSVDTACSS SLAAIHLACN SIWRNDCDTA ITGGVNILTN PDNHAGLDRG HFLSRTGNCN
TFDDGADGYC RADGVGTVVL KRLEDALADN DPILGVINGA YTNHSAEAVS ITRPHVGAQA
FIFKKLLNEA NVDPKNISYI EMHGTGTQAG DAVEMQSVLD VFAPDHRRGP GQSLHLGSAK
SNIGHGESAS GVTSLVKVLL MMKENMIPPH CGIKTKINHN FPTDLAQRNV HIALQPTAWN
RPSFGKRQIF LNNFSAAGGN TALLLEDGPV SDPEGEDKRR THVITLSARS QTALQNNIDA
LCQYISEQEK TFGVKDSNAL PSLAYTTTAR RIHHPFRVTA IGSSFQEMRD SLIASSRKEF
VAVPAKTPGI GFLFTGQGAQ YAAMGKQLYE DCSHFRSAIE HLDCISQGQD LPSILPLVDG
SLPLSELSPV VVQLGTTCVQ MALSSFWASL GITPSFVLGH SLGDFAAMNA AGVLSTSDTI
YACGRRAQLL TERCQPGTHA MLAIKAPLVE VKQLLNEKVH DMACINSPSE TVISGPKSSI
DELSRACSEK GLKSTILTVP YAFHSAQVEP ILEDLEKALQ GITFNKPSVP FVSALLGEVI
TEAGSNILNA EYLVRHCRET VNFLSAFEAV RNAKLGGDQT LWLEVGPHTV CSGMVKATLG
PQTTTMASLR RDEDTWKVLS NSLSSLYLAG VDINWKQYHQ DFSSSHRVLP LPTYKWDLKN
YWIPYRNNFC LTKGSSMSAA SASLQPTFLT TSAQRVVESR DDGLTATVVV HNDIADPDLN
RVIQGHKVNG AALCPSSLYA DSAQTLAEYL IEKYKPELKG SGLDVCNVTV PKPLIAKTGK
EQFRISATAN WVDKHVSVQV FSVTAEGKKL IDHAHCEVKL FDCMAADLEW KRGSYLVKRS
IELLENSAVK GDAHRLRRGM VYKLFSALVD YDENYQSIRE VILDSEHHEA TALVKFQAPQ
ANFHRNPYWI DSFGHLSGFI MNASDGTDSK SQVFVNHGWD SMRCLKKFSA DVTYRTYVRM
QPWRDSIWAG NVYIFEGDDI IAVFGGVKFQ ALSRKILDIA LPPAGLSKAQ TSPIQSSAPQ
KPIETAKPTS RPAPPVTMKS FVKKSAGPSV VVRALNILAS EVGLSESDMS DDLVFADYGV
DSLLSLTVTG KYREELNLDM DSSVFIEHPT VGDFKRFVTQ LSPSVASDSS STDRESEYSF
NGDSCSGLSS PASPGTVSPP NEKVIQIHEN GTMKEIRAII ADEIGVSADE IKSDENLNEL
GMDSLLSLTV LGKIRESLDM DLPGEFFIEN QTLDQIETAL DLKPKAVPTA VPQSQPITLP
QSQSTKQLST RPTSSSDNHP PATSILLQGN PRTASKTLFL FPDGSGSATS YATIPGVSPN
VAVYGLNCPY MKAPEKLTCS LDSLTTPYLA EIRRRQPTGP YNLGGWSAGG ICAYDAARKL
VLQQGEIVET LLLLDTPFPI GLEKLPPRLY SFFNSIGLFG EGKAAPPAWL LPHFLAFIDS
LDAYKAVPLP FNEQEWKGKL PKTYLVWAKD GVCPKPGDPW PEPAEDGSKD PREMVWLLSN
RTDLGPNGWD TLVGKENIGG ITVIHDANHF TMTKGEKAKE LATFMKNALG VCERRLV
