ALBA_ASPNA
ID ALBA_ASPNA Reviewed; 2128 AA.
AC G3XLL5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
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=ASPNIDRAFT_56896;
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL
RC 328 / USDA 3528.7;
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.I.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W.M., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N.M.E., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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; ACJE01000001; EHA28527.1; -; Genomic_DNA.
DR AlphaFoldDB; G3XLL5; -.
DR SMR; G3XLL5; -.
DR STRING; 380704.G3XLL5; -.
DR EnsemblFungi; EHA28527; EHA28527; ASPNIDRAFT_56896.
DR HOGENOM; CLU_000022_6_0_1; -.
DR Proteomes; UP000009038; Unassembled WGS sequence.
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 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..2128
FT /note="Non-reducing polyketide synthase albA"
FT /id="PRO_0000449883"
FT DOMAIN 1618..1695
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1739..1816
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 1695..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1854..2126
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT COMPBIAS 1696..1739
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 1944
FT /note="For Claisen cyclase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1655
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1776
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2128 AA; 231948 MW; D1422711D50010DE 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 TGGVNILTNP 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 IHHPFRVTAV 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 LPPSRASAPA PAKPAAKPSA
PSLVKRALTI LAEEVGLSES EITDDLVFAD YGVDSLLSLT VTGRYREELD IDLESSIFID
QPTVKDFKQF LAPMSQGEAS DGSTSDPESS SSFNGGSSTD ESSAGSPVSS PPNEKVTQVE
QHATIKEIRA ILADEIGVTE EELKDDENLG EMGMDSLLSL TVLGRIRETL DLDLPGEFFI
ENQTLNDVED ALGLKPKAAP APAPAPAPVP APVSAPILKE PVPNANSTIM ARASPHPRST
SILLQGNPKT ATKTLFLFPD GSGSATSYAT IPGVSPDVCV YGLNCPYMKT PEKLKYPLAE
MTFPYLAEIR RRQPKGPYNF GGWSAGGICA YDAARYLILE EGEQVDRLLL LDSPFPIGLE
KLPTRLYGFI NSMGLFGEGN KAPPAWLLPH FLAFIDSLDT YKAVPLPFDD PKWAKKMPKT
FMVWAKDGIC SKPDDPWPEP DPDGKPDTRE MVWLLKNRTD MGPNKWDTLV GPQNVGGITV
IEGANHFTMT LGPKAKELGS FIGNAMAN
