EPAB_ASPNC
ID EPAB_ASPNC Reviewed; 539 AA.
AC A2QTE5;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Phenylacetyl-CoA ligase epaB {ECO:0000303|PubMed:30384904};
DE EC=6.2.1.- {ECO:0000305|PubMed:30384904};
DE AltName: Full=Pestalamide A biosynthesis cluster protein B {ECO:0000303|PubMed:30384904};
GN Name=epaB {ECO:0000303|PubMed:30384904}; ORFNames=An09g01820;
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 IDENTIFICATION, FUNCTION, AND PATHWAY.
RX PubMed=30384904; DOI=10.1016/j.micres.2018.10.004;
RA Wang B., Li X., Yu D., Chen X., Tabudravu J., Deng H., Pan L.;
RT "Deletion of the epigenetic regulator GcnE in Aspergillus niger FGSC A1279
RT activates the production of multiple polyketide metabolites.";
RL Microbiol. Res. 217:101-107(2018).
CC -!- FUNCTION: Phenylacetyl-CoA ligase; part of the gene cluster that
CC mediates the biosynthesis of nigerpyrone and its derivatives
CC carbonarone A and pestalamide A (PubMed:30384904). The biosynthesis
CC pathway begins with the polyketide assembly by epaA to form
CC phenylacetyl triketide precursor from successive condensation of two
CC malonyl-CoA, presumably with one phenylacetyl-CoA starter unit produced
CC by the phenylacetyl-CoA ligase epaB (PubMed:30384904). For the
CC nigerpyrone biosynthesis, the reactive polyketide chain is released as
CC an aldehyde through the R-domain. A nonenzymatic cyclization and
CC dehydration may create nigerpyrone (PubMed:30384904). For the
CC biosynthesis of carbonarone A and pestalamide A, an extra methyl group
CC is added through the C-methyltransferase domain. Several further steps
CC involving the dehydrogenase orf1, the cytochrome P450 monooxygenase
CC orf2 and the FAD-dependent monooxygenase orf3 are required to form a
CC carbonarone A precursor which is converted to carbonarone A via
CC cyclization (PubMed:30384904). The O-acetyltransferase epaC could
CC catalyze the transfer of 2-methylsuccinyl-CoA, a common intermediate in
CC the ethylmalonyl-CoA pathway, to generate the final product pestalamide
CC A (Probable). {ECO:0000269|PubMed:30384904,
CC ECO:0000305|PubMed:30384904}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30384904}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AM270194; CAK40120.1; -; Genomic_DNA.
DR RefSeq; XP_001393497.1; XM_001393460.1.
DR AlphaFoldDB; A2QTE5; -.
DR SMR; A2QTE5; -.
DR PaxDb; A2QTE5; -.
DR EnsemblFungi; CAK40120; CAK40120; An09g01820.
DR GeneID; 4983713; -.
DR KEGG; ang:ANI_1_1124084; -.
DR VEuPathDB; FungiDB:An09g01820; -.
DR HOGENOM; CLU_000022_59_2_1; -.
DR Proteomes; UP000006706; Chromosome 1L.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..539
FT /note="Phenylacetyl-CoA ligase epaB"
FT /id="PRO_0000446155"
FT REGION 449..525
FT /note="AMP-binding"
FT /evidence="ECO:0000255"
FT BINDING 188..199
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
SQ SEQUENCE 539 AA; 59956 MW; 8A5DEED9E2CF590D CRC64;
MFFQGEGSID IPVQDIISWI FDQARYEIEK PVYIDASNTS RSISWRQART LVRQLAAGLR
AAGLKDGDCV CLHSFNDIYY SILVLGIIAA GGIYMGTNPG YTSHELDYHL RVAQAKFVIS
DPEMLDRMIP AAEGNGIPKD RIWAFTTRES QVIATTGLAH WTALLNHGEA DWRRLDDPNH
AKTTVVARLF SSGTTGLPKP VDFTHYNIIA QHTLVYDAHP VPFETSRILS LPFFHAAAAP
SAHFSALRLG DPSYVLRRFE PDLFLTTVAK HNITECTAVP PIILAILSHC TTPKYSNSLQ
SLKIVRCGAA PLDKTTQARF QSLLAPDATF TQVWGMTESS CIATMIPYPE SDDTGSVGRL
LPGMEAKIIN TDGDDITAPD TTGEVCLRGP TVVRGYFNLP SANESAFDKD GFYRTGDLGY
CDGKTRKWYL LDRKKDIIKV RGFQVAPAEV EGVLRNHPRI RDVAVVGVYD AEAKTEYPRA
YVVRQDQSLQ EEEVKEFVAL RLAKYKRLDG GVRFVDAIPR NASGKILKRL LEDKRDEKL
