ACUF_ASPA1
ID ACUF_ASPA1 Reviewed; 433 AA.
AC P9WF00;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 1.
DT 25-MAY-2022, entry version 3.
DE RecName: Full=Oxidoreductase acuF {ECO:0000303|PubMed:26374386};
DE EC=1.-.-.- {ECO:0000305|PubMed:26374386};
DE AltName: Full=Aculin biosynthesis cluster protein F {ECO:0000303|PubMed:26374386};
GN Name=acuF {ECO:0000303|PubMed:26374386};
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: Oxidoreductase; part of the gene cluster that mediates the
CC biosynthesis of aculins (PubMed:26374386). The pathway begins with the
CC synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS)
CC acuA via condensation of acetate and malonate units (PubMed:26374386).
CC The 6-methylsalicylic acid decarboxylase acuB then catalyzes the
CC decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known
CC as 3-methylphenol) (Probable). These first reactions occur in the
CC cytosol (By similarity). The intermediate m-cresol is then transported
CC into the endoplasmic reticulum where the cytochrome P450 monooxygenase
CC acuC converts it to m-hydroxybenzyl alcohol, which is further converted
CC to gentisyl alcohol by the cytochrome P450 monooxygenase acuD
CC (Probable). Gentisyl alcohol is further oxidized by the oxidoreductase
CC acuE that probably catalyzes hydroxylation of the aromatic ring
CC (Probable). The aromatic system might then be opened by oxidation
CC through a Baeyer-Villiger type of oxidation, which could be catalyzed
CC by acuF, with the carboxylic acid at C-1 subsequently reduced to an
CC aldehyde by acuG (Probable). Subsequently, a hemiacetal is formed,
CC before the dehydrogenase acuH would reduce the double bond between C-4
CC and C-6 (Probable). Finally, keto-enol tautomerism results in formation
CC of aculinic acid, which exists as two diastereomers (both R/S
CC 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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26374386}.
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DR EMBL; KV878982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P9WF00; -.
DR Proteomes; UP000184546; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..433
FT /note="Oxidoreductase acuF"
FT /id="PRO_0000450421"
SQ SEQUENCE 433 AA; 49108 MW; 7EA548E084FCF20F CRC64;
MERAISTTPI LDQALTCVQS YKALAATVQE LASPELQRSI EEGLAQFLTH MPEFNILVNA
VEPPHTSWDY LLRNDASQRG EMTMLLMELQ CEIDQMAFAI RQAMQQQHPE AEPLSNNSRL
VDAWTENLRS VEDHTVWRLA FWRRDHAVHT TYPTTNPLVN QSFYFAIRNE LGLDVSTQFR
ECIRRAITQE CPTITARPAL HRRLVDLVVQ RRRFWNFQRR IRGLSKDAVL WGRDALAPPH
FAPGDERFTC PFCFFDLPVA AYRTPRAWTD HVMSDLEGYV CLYETCSSTR SWPETCPHAC
TSFGAWFTAM AGSFAEGVEW CSHAFACDGR RLEEVHRPRC AAPAVRLDSV CPLCGREPAV
EETELRMADA ADPLQDDDQN RAKARLLLSH IAGHLEVITP MAFTWNTDRN ALDPDRRLFW
GDIGSPGGAG GSA
