ALBA_ASPNC
ID ALBA_ASPNC Reviewed; 2153 AA.
AC A2QUI2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Non-reducing polyketide synthase albA {ECO:0000303|PubMed:31067027};
DE Short=NR-PKS albA {ECO:0000303|PubMed:31067027};
DE EC=2.3.1.- {ECO:0000305|PubMed:31067027};
GN Name=albA {ECO:0000303|PubMed:31067027}; ORFNames=An09g05730;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=31067027; DOI=10.1021/acs.biochem.9b00291;
RA Obermaier S., Mueller M.;
RT "Biaryl-forming enzymes from Aspergilli exhibit substrate-dependent
RT stereoselectivity.";
RL Biochemistry 58:2589-2593(2019).
CC -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC that mediates the biosynthesis of aurasperone B, a dimeric gamma-
CC naphthopyrone (PubMed:31067027). The first step in the biosynthesis of
CC aurasperone B is the production of gamma-naphthopyrone precursor YWA1
CC by the non-reducing polyketide synthase albA, via condensation of one
CC acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:31067027).
CC YWA1 is then methylated by aunE at position C-6 to yield foncesin which
CC is further methylated at position C-8 by aunD to produce fonsecin B
CC (Probable). A key enzyme in the biosynthetic pathway is the cytochrome
CC P450 monooxygenase aunB which catalyzes the oxidative dimerization of
CC fonsecin B to aurasperone B (PubMed:31067027). AunB also catalyzes the
CC oxidative dimerization of rubrofusarin B into aurasperone A
CC (PubMed:31067027). {ECO:0000269|PubMed:31067027,
CC ECO:0000305|PubMed:31067027}.
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:0000305|PubMed:31067027};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62653;
CC Evidence={ECO:0000305|PubMed:31067027};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:31067027}.
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:0000250|UniProtKB:Q03149}.
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DR EMBL; AM270206; CAL00851.1; -; Genomic_DNA.
DR AlphaFoldDB; A2QUI2; -.
DR SMR; A2QUI2; -.
DR PaxDb; A2QUI2; -.
DR EnsemblFungi; CAL00851; CAL00851; An09g05730.
DR VEuPathDB; FungiDB:An09g05730; -.
DR HOGENOM; CLU_000022_6_0_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0042438; P:melanin biosynthetic process; IMP:AspGD.
DR GO; GO:1900787; P:naphtho-gamma-pyrone 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 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 3: Inferred from homology;
KW Multifunctional enzyme; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..2153
FT /note="Non-reducing polyketide synthase albA"
FT /id="PRO_0000449884"
FT DOMAIN 1643..1720
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1764..1841
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"
FT REGION 378..809
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000255"
FT REGION 912..1232
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000255"
FT REGION 1290..1603
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000255"
FT REGION 1608..1643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1879..2151
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT COMPBIAS 1721..1764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 547
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 1969
FT /note="For Claisen cyclase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1680
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1801
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2153 AA; 234150 MW; A7D7A84883039168 CRC64;
MEGPSRVYLF GDQTSDIEAG LRRLLQAKNS TIVQSFFQQC FHAIRQEIAK LPPSHRKLFP
RFTSIVDLLS RSRESGPSPV LESALTCIYQ LGCFIHFYGD LGHDYPTPSN SHLVGLCTGV
LSCTAVSCAR NVGELIPAAV ESVVIALRLG ICVFRVRELV DSADSESTCW SALVSGISEA
EASHLIDEYS SKKATPPSSK PYISAVSSNG VTVSAPPTVL DEFVETCISK NYKPVKAPIH
GPYHAPHLYD DKDIDRILQQ SSALEGLTGC SPVIPIISSN TGKPIKAKSI KDLFKVALEE
ILLRRLCWDK VTESCTSVCK TGTNHSCKLF PISSSATQSL FTVLKKAGVS ISLETGVGEI
ATNPEMRNLT GKAENSKIAI IGMSGRFPDS DGTESFWNLL YKGLDVHRKV PADRWDVDAH
VDMTGSKRNT SKVAYGCWIN EPGLFDPRFF NMSPREALQA DPAQRLALLT AYEALEMAGF
IPDSSPSTQR DRVGIFYGMT SDDYREINSG QDIDTYFIPG GNRAFTPGRI NYYFKFSGPS
VSVDTACSSS LAAIHMACNS IWRNDCDAAI TGGVNILTSP DNHAGLDRGH FLSTTGNCNT
FDDGADGYCR ADGVGSIVLK RLEDAEADND PILAVINGAY TNHSAEAVSI TRPHVGAQAF
IFNKLLNDAN IDPKDVSYVE MHGTGTQAGD AVEMQSVLDV FAPDYRRGPG QSLHIGSAKA
NIGHGESASG VTALVKVLLM MRENMIPPHC GIKTKINSNF PTDLAKRNVH IAFQPTPWNR
PASGKRRTFV NNFSAAGGNT ALLLEDAPIP ERQGQDPRSF HLVSVSARSQ SALKNNVEAL
VKYIDSQGKS FGVKETEFLP NLAYTTTARR IHHPFRVIAV GANLQSLRDS LHGALHRETY
TPVPSTAPGI GFVFTGQGAQ YSGMGKELYR SCFQFRTTIE HFDCIARSQG LPSILPLVDG
SVAVEELSPV VVQVGTTCVQ MALVNYWTAL GVKPAFIIGH SLGDYAALNT AGVLSTSDTI
YLCGRRAQLL TKECKIGTHS MLAIKASLAE VKHFLRDELH EVSCVNAPAE TVVSGLVADI
DELAQKCSTE GLKSTKLKVP YAFHSSQVDP ILEAFEDIAQ GVTFHKPTTP FVSALFGEVI
TDANWECLGP KYLRDHCRKT VNFLGGVEAT RHAKLTNDKT LWVEIGSHTI CSGMIKATLG
PQVTTVASLR REEDTWKVLS NSLASLHLAG IDINWKQYHQ DFSSSLQVLR LPAYKWDLKN
YWIPYTNNFC LSKGAPVATV AAGPQHEYLT TAAQKVIETR SDGATATVVI ENDIADPELN
RVIQGHKVNG TALCPSSLYA DISQTLAEYL IKKYKPEYDG LGLDVCEVTV PRPLIAKGGQ
QLFRVSATAD WAEKKTTLQI YSVTAEGKKT ADHATCTVRF FDCAAAEAEW KRVSYLVKRS
IDRLHDIAEN GDAHRLGRGM VYKLFAALVD YDDNFKSIRE VILDSEQHEA TARVKFQAPQ
GNFHRNPFWI DSFGHLSGFI MNASDATDSK NQVFVNHGWD SMRCLKKFSP DVTYRTYVRM
QPWKDSIWAG DVYVFDGDDI VAVYGAVKFQ ALSRKILDTV LPPVGASKGP ARPAASAQKA
APAAAASKSR ASAPAPAKPA AKPSAPSLVK RALTILAEEV GLSESEITDD LVFADYGVDS
LLSLTVTGRY REELDIDLES SIFIDQPTVK DFKQFLAPMS QGEASDGSTS DPESSSSFNG
GSSTDESSAG SPVSSPPNEK VTQVEQHATI KEIRAILADE IGVTEEELKD DENLGEMGMD
SLLSLTVLGR IRETLDLDLP GEFFIENQTL NDVEDALGLK PKAAPAPAPA PAPVPAPVSA
PILKEPVPNA NSTIMARASP HPRSTSILLQ GNPKTATKTL FLFPDGSGSA TSYATIPGVS
PDVCVYGLNC PYMKTPEKLK YPLAEMTFPY LAEIRRRQPK GPYNFGGWSA GGICAYDAAR
YLILEEGEQV DRLLLLDSPF PIGLEKLPTR LYGFINSMGL FGEGNKAPPA WLLPHFLAFI
DSLDTYKAVP LPFDDPKWAK KMPKTFMVWA KDGICSKPDD PWPEPDPDGK PDTREMVWLL
KNRTDMGPNK WDTLVGPQNV GGITVIEGAN HFTMTLGPKA KELGSFIGNA MAN
