ACUB_ASPA1
ID ACUB_ASPA1 Reviewed; 330 AA.
AC A0A1L9WN60;
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=6-methylsalicylic acid decarboxylase acuB {ECO:0000303|PubMed:26374386};
DE EC=4.1.1.52 {ECO:0000305|PubMed:26374386};
DE AltName: Full=Aculin biosynthesis cluster protein B {ECO:0000303|PubMed:26374386};
GN Name=acuB {ECO:0000303|PubMed:26374386}; ORFNames=ASPACDRAFT_45672;
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: 6-methylsalicylic acid decarboxylase; part of the gene
CC cluster that mediates the biosynthesis of aculins (PubMed:26374386).
CC The pathway begins with the synthesis of 6-methylsalicylic acid by the
CC polyketide synthase (PKS) acuA via condensation of acetate and malonate
CC units (PubMed:26374386). The 6-methylsalicylic acid decarboxylase acuB
CC then catalyzes the decarboxylation of 6-methylsalicylic acid to yield
CC m-cresol (also known as 3-methylphenol) (Probable). These first
CC reactions occur in the cytosol (By similarity). The intermediate m-
CC cresol is then transported into the endoplasmic reticulum where the
CC cytochrome P450 monooxygenase acuC converts it to m-hydroxybenzyl
CC alcohol, which is further converted to gentisyl alcohol by the
CC cytochrome P450 monooxygenase acuD (Probable). Gentisyl alcohol is
CC further oxidized by the oxidoreductase acuE that probably catalyzes
CC hydroxylation of the aromatic ring (Probable). The aromatic system
CC might then be opened by oxidation through a Baeyer-Villiger type of
CC oxidation, which could be catalyzed by acuF, with the carboxylic acid
CC at C-1 subsequently reduced to an aldehyde by acuG (Probable).
CC Subsequently, a hemiacetal is formed, before the dehydrogenase acuH
CC would reduce the double bond between C-4 and C-6 (Probable). Finally,
CC keto-enol tautomerism results in formation of aculinic acid, which
CC exists as two diastereomers (both R/S configurations at C-1) by non-
CC enzymatic hemiacetal formation (Probable). The carboxypeptidase acuI
CC could be involved in the linking of aculinic acid to an aculene A
CC moiety produced by the aculene biosynthesis cluster and which leads to
CC the production of aculin A (Probable). AcuI may also be involved in the
CC attachment of proline to aculinic acid to form epi-aculins A and B
CC (Probable). {ECO:0000250|UniProtKB:A0A075TRC0,
CC ECO:0000269|PubMed:26374386, ECO:0000305|PubMed:26374386}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-methylsalicylate + H(+) = 3-methylphenol + CO2;
CC Xref=Rhea:RHEA:23112, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:17231, ChEBI:CHEBI:36658; EC=4.1.1.52;
CC Evidence={ECO:0000305|PubMed:26374386};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113;
CC Evidence={ECO:0000305|PubMed:26374386};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26374386}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8TDX5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:A0A075TXZ1}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ACMSD family. {ECO:0000305}.
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DR EMBL; KV878982; OJJ97581.1; -; Genomic_DNA.
DR RefSeq; XP_020053921.1; XM_020201649.1.
DR AlphaFoldDB; A0A1L9WN60; -.
DR SMR; A0A1L9WN60; -.
DR EnsemblFungi; OJJ97581; OJJ97581; ASPACDRAFT_45672.
DR GeneID; 30975463; -.
DR VEuPathDB; FungiDB:ASPACDRAFT_45672; -.
DR OrthoDB; 1119055at2759; -.
DR Proteomes; UP000184546; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0047596; F:6-methylsalicylate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR032465; ACMSD.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR21240; PTHR21240; 1.
DR Pfam; PF04909; Amidohydro_2; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Decarboxylase; Hydrolase; Lyase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..330
FT /note="6-methylsalicylic acid decarboxylase acuB"
FT /id="PRO_0000450414"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8TDX5"
SQ SEQUENCE 330 AA; 36231 MW; 11351FFF6C078398 CRC64;
MKIDVHHHFY PQAFREALEA AGGDPSGWYI PPWTLELDQE INATLNVTTT ILSVTAPGPV
IAKDPAAAAS LARECNRSAA AIRDAAPAQY GFFASVPSLF DTALALEEIR YALDELHADG
VTLFTRYGQG ANYLGHEAFA PIWAELSRRQ AVVFIHPTHP QDTALINRAL PQPMFDYPHE
TGRTAMDLLT SGRLRQHRGC RVILSHAGGT LPYLIHRAAT MLPCMPPDRN IGLSRDEILD
TAREVFYFDT AISANEVTLS ALARFAKPGH ILFGSDFPNA PRDAIVRFTR FVEEEAAALP
DGVTVEALKE NALQLFPRLK RAEANGVPKI
