ACRG_ASPA1
ID ACRG_ASPA1 Reviewed; 374 AA.
AC A0A1L9WQN9;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=O-methyltransferase acrG {ECO:0000303|PubMed:32234543};
DE EC=2.1.1.- {ECO:0000269|PubMed:32234543};
DE AltName: Full=Acurin A biosynthesis cluster protein G {ECO:0000303|PubMed:32234543};
GN Name=acrG {ECO:0000303|PubMed:32234543}; ORFNames=ASPACDRAFT_122283;
OS Aspergillus aculeatus (strain ATCC 16872 / CBS 172.66 / WB 5094).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=690307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 16872 / CBS 172.66 / WB 5094;
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, DISRUPTION PHENOTYPE, PATHWAY, AND INDUCTION.
RX PubMed=32234543; DOI=10.1016/j.fgb.2020.103378;
RA Wolff P.B., Nielsen M.L., Slot J.C., Andersen L.N., Petersen L.M.,
RA Isbrandt T., Holm D.K., Mortensen U.H., Noedvig C.S., Larsen T.O.,
RA Hoof J.B.;
RT "Acurin A, a novel hybrid compound, biosynthesized by individually
RT translated PKS- and NRPS-encoding genes in Aspergillus aculeatus.";
RL Fungal Genet. Biol. 139:103378-103378(2020).
CC -!- FUNCTION: O-methyltransferase; part of the cluster that mediates the
CC biosynthesis of acurin A, a highly reduced polyketide coupled to a
CC serine via a peptide bond (PubMed:32234543). The activities of the
CC highly reducing polyketide synthase acrA and the nonribosomal peptide
CC synthetase acrB are collectively responsible for the synthesis of the
CC acurin A core structure with a heptaketide backbone produced by acrA
CC covalently fused to a L-serine by acrB (PubMed:32234543). After the
CC formation of the PK-NRP hybrid product, it is detached from acrB by
CC reductive release to set up the formation of the lactam ring by aldol
CC condensation (Probable). The hydrolyase acrC then catalyzes water loss
CC to generate a double bond in the ring (Probable). This double bond is
CC probably reduced, which is followed by three oxidations at C-22 to
CC generate the carboxylic acid moiety, involving probably the FAD-binding
CC monooxygenase acrE and the cytochrome P450 monooxygenases acrD and acrF
CC (Probable). Finally, a last methylation step performed by the O-
CC methyltransferase acrG leads to the production of acurin A (Probable).
CC {ECO:0000269|PubMed:32234543, ECO:0000305|PubMed:32234543}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:32234543}.
CC -!- INDUCTION: Expression is positively regulated by the acurin A cluster-
CC specific transcription regulator acrR. {ECO:0000269|PubMed:32234543}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of acurin A.
CC {ECO:0000269|PubMed:32234543}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; KV878980; OJJ98491.1; -; Genomic_DNA.
DR RefSeq; XP_020054831.1; XM_020196520.1.
DR AlphaFoldDB; A0A1L9WQN9; -.
DR SMR; A0A1L9WQN9; -.
DR EnsemblFungi; OJJ98491; OJJ98491; ASPACDRAFT_122283.
DR GeneID; 30970334; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_122283; -.
DR OrthoDB; 689338at2759; -.
DR Proteomes; UP000184546; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 2: Evidence at transcript level;
KW Magnesium; Metal-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..374
FT /note="O-methyltransferase acrG"
FT /id="PRO_0000450426"
FT BINDING 19
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 22..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 64..65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 70
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 94..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 128..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 145..147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 146..150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 216..221
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2KPR3"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
SQ SEQUENCE 374 AA; 40910 MW; 6F05719ADE084B68 CRC64;
MSPAKVSAND VPMHGNGFYS SNSALQHSAM LNALPLLAAA AAASKAKQQE EQENSRPFAI
LEFGSAHGNN SHTPITTVLK SRAPAPSREI HLQFNDRPTN DFSTLATNLT TMTWPVSNAI
FTSLLPASFY SRVSPKGSVD VAFSLAALHH LDRVTPVPPE GPIPTHEVRQ AEFRAQAHAD
LLSFLSHRAE EIVPGGGLVL SFVGQELGPN GEEITNYAGP VDACRSAMID MLQAGVLSPA
VANVFEVPAY NRTIADVRRT LAEGEVVAAW EVEEVFERKV VHPALQELEA RREAAPGKEE
EHAEWYARTV VDWLMAVVAG YFVKAVREGM GVTDQTVLDG LLAEWVERTR GRFLEGHRNE
PVECWFVYVR LGRK
