ALBA_ASPBC
ID ALBA_ASPBC Reviewed; 2147 AA.
AC A0A1L9UCG2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 27.
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=ASPBRDRAFT_131114;
OS Aspergillus brasiliensis (strain CBS 101740 / IMI 381727 / IBT 21946).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=767769;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101740 / IMI 381727 / IBT 21946;
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
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 involved in the biosynthesis
CC of bifonsecin B, a dimeric gamma-naphthopyrone (PubMed:31067027). The
CC first step in the biosynthesis of bifonsecin B is the production of
CC gamma-naphthopyrone precursor YWA1 by the non-reducing polyketide
CC synthase albA, via condensation of one acetyl-CoA starter unit with 6
CC malonyl-CoA units (PubMed:31067027). YWA1 is then methylated by bfoE at
CC position C-6 to yield foncesin which is further methylated at position
CC C-8 by bfoD to produce fonsecin B (Probable). A key enzyme in the
CC biosynthetic pathway is the cytochrome P450 monooxygenase bfoB which
CC catalyzes the oxidative dimerization of fonsecin B to bifonsecin B
CC (PubMed:31067027). Bfob also catalyzes the oxidative dimerization of
CC rubrofusarin B into nigerone (PubMed:31067027). The stereoselectivity
CC of bfoB is influenced by the two natural monomeric substrates;
CC homodimerization of fonsecin B yields a stereochemically pure biaryl,
CC M-foncerine B, while rubrofusarin B yields a mixture of enantiomers
CC M- and P-nigerone (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; KV878688; OJJ69377.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9UCG2; -.
DR SMR; A0A1L9UCG2; -.
DR STRING; 767769.A0A1L9UCG2; -.
DR EnsemblFungi; OJJ69377; OJJ69377; ASPBRDRAFT_131114.
DR VEuPathDB; FungiDB:ASPBRDRAFT_131114; -.
DR OrthoDB; 68112at2759; -.
DR Proteomes; UP000184499; 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; -; 3.
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..2147
FT /note="Non-reducing polyketide synthase albA"
FT /id="PRO_0000448920"
FT DOMAIN 1642..1719
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1760..1837
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:0000250|UniProtKB:A0A142C799, ECO:0000255"
FT REGION 378..809
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000250|UniProtKB:A0A142C799, ECO:0000255"
FT REGION 912..1232
FT /note="Malonyl-CoA:ACP transacylase (MAT) domain"
FT /evidence="ECO:0000250|UniProtKB:A0A142C799, ECO:0000255"
FT REGION 1290..1603
FT /note="Product template (PT) domain"
FT /evidence="ECO:0000250|UniProtKB:A0A142C799, ECO:0000255"
FT REGION 1608..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1719..1759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..2145
FT /note="Claisen cyclase domain"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT COMPBIAS 1720..1759
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 1963
FT /note="For Claisen cyclase activity"
FT /evidence="ECO:0000250|UniProtKB:Q03149"
FT MOD_RES 1679
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1797
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2147 AA; 233620 MW; F8205FC31A1F8B3E CRC64;
MEGPSRVYLF GDQTSDIEAG LRRLLQAKNS TIVQSFFQQC FHAIRQEIAK LPPSQRKLFP
RFTSIVDLLS KSRESGPSPV LESALTCIYQ LGCFIHYYGD LGHGYPTPSN SHLVGLCLGV
LSCTAVSCAK NVGELIPAAV EAVVVALRLG ICVFRVRELV DSGDSESTCW SALISGISET
EASRLIDEYS NKKATPPSSK PYISAVSSNG VTVSAPPTVL DEFIGTCISK NYKPVKAPIH
GPYHAPHLYD NKDIERILQQ SSALESLTAS SPTVPVISSN TGKPINAKST RDLFKVALEE
ILLRRLCWDK VTESCTSVCK TGTNHSCKLF PISSSATQSL FTALKKAGVN ISLETGVGEI
ATNPDMRNLT GKAECSKIAI IGMSGRFPDA DGTESFWDLL YKGLDVHRKV PADRWDVDAH
VDLTGSKRNT SKVPYGCWIN EPGLFDPRFF NMSPREALQA DPAQRLALLT AYEALEMAGF
IPDSSPSTQR DRVGIFYGMT SDDYREINSG QDIDTYFIPG GNRAFTPGRI NYYFKFSGPS
VSVDTACSSS LAAIHMACNS IWRNDCDAAI TGGVNILTNP DNHAGLDRGH FLSTTGNCNT
FDDGADGYCR ADGVGSIVLK RLEDAEADND PILAVINGAY TNHSAEAVSI TRPHVGAQAF
IFNKLLNDAN IDPKEVSYVE MHGTGTQAGD AVEMQSVLDV FAPDYRRGPG QSLHIGSAKA
NIGHGESASG VTALVKVLLM MRENMIPPHC GIKTKINHNF PTDLAKRNVH IAFQPTPWNR
PASGKRRSFV NNFSAAGGNT AILLEDAPIP ERQGQDPRAF HLVSVSARSQ SALKNNIESL
VKYIDSQGKS FGVKETEFLP NLAYTTTARR IHHPFRVTAV GANLQSLRDS LHGALHRETY
TPVPSTAPGI GFVFTGQGAQ YTGMGKELYS TCFQFRTTIE HFDCIARSQG LPSILPLVDG
SVPVEDLSPV VVQVGTTCVQ MALVNYWTAL GVKPAFIIGH SLGDYAALNT AGVLSTSDTI
YLCGRRAQLL TKECKIGTHS MLAIKASLAE VKQFLKDELH EVSCVNAPAE TVVSGLVADI
DDLAQKCSTE GLKSTKLRVP YAFHSSQVDP ILDTFEEIAQ GVTFHKPTTP FVSALFGEVI
TDANWECLGP KYLRDHCRKT VNFLGGVEAT RHAKLTNDKT LWVEIGSHTI CSGMIKATLG
PQVTTVASLR REEDTWKVLS NSLSSLHLAG IDINWKQYHQ DFSSSHQVLR LPSYKWDLKN
YWIPYTNNFC LHKGAPVAAV AAGPQHEFLT TAAQKVIETR SDGATATVVV ENDIADPDLN
RVIQGHKVNG AALCPSSLYA DISQTLAEYL IKKYKPEYDG LGLDVCEVTV PRPLIAKSGQ
QLFRVSATAD WAEKKVTLQV YSVTAEGKKT ADHATCTVRF FDCAAAEAEW KRVSYLVKRS
IDRLHDIAEN GDAHRLGRGM VYKLFAALVD YDDNFKSIRE VILDSEQHEA TARVKFQAPQ
GNFHRNPFWI DSFGHLSGFI MNASDATDSK NQVFVNHGWD SMRCLKKFSP DVTYRTYVRM
QPWKDSIWAG DVYVFDGDDI VAVYGAVKFQ GLSRKILDTV LPPVGASKGP ARPAASAQKA
APAATSKSRA SAPAPAKAVA KPSAPSLVKR ALTILAEEVG LSESELTDEL VFADYGVDSL
LSLTVTGRYR EELDIDLESS VFIDQPTVKD FKQFLAPMSQ GEASDGSTSD PESSSSFNGG
SSTDESSAGS PVSSPPNEKI EQHATMKEIR AILADEIGVS EEELKDDENL GEMGMDSLLS
LTVLGRIRET LDLDLPGEFF IENQTLNDVE DALGLKPKVA PAPAPTPAPA PVSAPILSEP
VPNPKSTIMT RASPHPRSTS ILLQGNPKTA TKTLFLFPDG SGSATSYATI PGVSPDVCVY
GLNCPYMKTP EKLKYPLAEM TFPYLAEIRR RQPKGPYNFG GWSAGGICAY DAARYLILEE
GERVDRLLLL DSPFPIGLEK LPTRLYGFIN SKGLFGEGNK APPSWLLPHF LAFIDSLDTY
RAVPLPFDDP KWANKMPKTF LVWAKDGICN KPDDPWPEPD PDGKPDTREM VWLLKNRTDM
GPNKWDTLVG PANVGGISVI EGANHFTMTL GPKAKELGSF IGNAMAN
