ACUG_ASPA1
ID ACUG_ASPA1 Reviewed; 521 AA.
AC A0A1L9WN49;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=GMC-type oxidoreductase acuG {ECO:0000303|PubMed:26374386};
DE EC=1.1.-.- {ECO:0000305|PubMed:26374386};
DE AltName: Full=Aculin biosynthesis cluster protein G {ECO:0000303|PubMed:26374386};
GN Name=acuG {ECO:0000303|PubMed:26374386}; ORFNames=ASPACDRAFT_80410;
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, AND PATHWAY.
RX PubMed=26374386; DOI=10.1002/cbic.201500210;
RA Petersen L.M., Holm D.K., Gotfredsen C.H., Mortensen U.H., Larsen T.O.;
RT "Investigation of a 6-MSA Synthase Gene Cluster in Aspergillus aculeatus
RT Reveals 6-MSA-derived Aculinic Acid, Aculins A-B and Epi-Aculin A.";
RL ChemBioChem 16:2200-2204(2015).
CC -!- FUNCTION: GMC-type oxidoreductase; part of the gene cluster that
CC mediates the biosynthesis of aculins (PubMed:26374386). The pathway
CC begins with the synthesis of 6-methylsalicylic acid by the polyketide
CC synthase (PKS) acuA via condensation of acetate and malonate units
CC (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB then
CC catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-
CC cresol (also known as 3-methylphenol) (Probable). These first reactions
CC occur in the cytosol (By similarity). The intermediate m-cresol is then
CC transported into the endoplasmic reticulum where the cytochrome P450
CC monooxygenase acuC converts it to m-hydroxybenzyl alcohol, which is
CC further converted to gentisyl alcohol by the cytochrome P450
CC monooxygenase acuD (Probable). Gentisyl alcohol is further oxidized by
CC the oxidoreductase acuE that probably catalyzes hydroxylation of the
CC aromatic ring (Probable). The aromatic system might then be opened by
CC oxidation through a Baeyer-Villiger type of oxidation, which could be
CC catalyzed by acuF, with the carboxylic acid at C-1 subsequently reduced
CC to an aldehyde by acuG (Probable). Subsequently, a hemiacetal is
CC formed, before the dehydrogenase acuH would reduce the double bond
CC between C-4 and C-6 (Probable). Finally, keto-enol tautomerism results
CC in formation of aculinic acid, which exists as two diastereomers (both
CC R/S configurations at C-1) by non-enzymatic hemiacetal formation
CC (Probable). The carboxypeptidase acuI could be involved in the linking
CC of aculinic acid to an aculene A moiety produced by the aculene
CC biosynthesis cluster and which leads to the production of aculin A
CC (Probable). AcuI may also be involved in the attachment of proline to
CC aculinic acid to form epi-aculins A and B (Probable).
CC {ECO:0000250|UniProtKB:A0A075TRC0, ECO:0000269|PubMed:26374386,
CC ECO:0000305|PubMed:26374386}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:E4QP00};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26374386}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. {ECO:0000305}.
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DR EMBL; KV878982; OJJ97584.1; -; Genomic_DNA.
DR RefSeq; XP_020053924.1; XM_020205647.1.
DR AlphaFoldDB; A0A1L9WN49; -.
DR SMR; A0A1L9WN49; -.
DR STRING; 690307.A0A1L9WN49; -.
DR EnsemblFungi; OJJ97584; OJJ97584; ASPACDRAFT_80410.
DR GeneID; 30979461; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_80410; -.
DR OrthoDB; 798314at2759; -.
DR Proteomes; UP000184546; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..521
FT /note="GMC-type oxidoreductase acuG"
FT /id="PRO_0000450424"
FT BINDING 14..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 34..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 82
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 90..93
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 492
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
FT BINDING 503..504
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:E4QP00"
SQ SEQUENCE 521 AA; 56252 MW; 23EA6455ECC53A48 CRC64;
MSKTFEYVIC GGGTVGCVLA SRLSLAGHSV LLIEAGPEDY NDRIMSPVAA PHLHGTEWEH
NLMTTKQPGL GNRSVPNYAG KLLSGSSGIN YGLWTRGHSV DYDSWAKAVG DERWNYANML
KYFQKTETQI STTAAARIYP LREPIRNAMV AAGLDYNPDP NGGNPLGFGP FTENWKNALR
QPASKAYDLS KATVLTNSVI ARVDFDDPKT TATGVTLTDG TQYTATSEVL VTCGALKTPQ
LLMLSGIGPQ QHLAQHNIPI IADLPVGENY HDKISATFFW KLRHPEKGYA LGSPRFNKPE
FRHGNPIEWV ATVPTPHAEL IKATQQDQID SDDPYLQKPR GNVEVMVAYA PIAGGGSEFR
LPMDGTHISS PVVLLLPTSR GRITLASADP TADPVLDPGY LDTETDRAAI RAGMRVALRL
METESAKEVI DGETPPPGHE PLTSACSDAD LDRRVQIVGS SFFQNGGTAA MGTVVDTQCR
VKGVRNLRVC DASVLSVPLA GHYQAPMYAL GEAVADMLLA Q
