ID   MACB_PENTR              Reviewed;         338 AA.
AC   A0A2P1DP90;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Decarboxylase macB {ECO:0000303|PubMed:28926261};
DE            EC=4.1.1.52 {ECO:0000250|UniProtKB:G3Y417};
DE   AltName: Full=Macrophorins biosynthesis cluster protein B {ECO:0000303|PubMed:28926261};
GN   Name=macB {ECO:0000303|PubMed:28926261};
OS   Penicillium terrestre.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=374132;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC   STRAIN=LM2;
RX   PubMed=28926261; DOI=10.1021/acs.orglett.7b02653;
RA   Tang M.C., Cui X., He X., Ding Z., Zhu T., Tang Y., Li D.;
RT   "Late-stage terpene cyclization by an integral membrane cyclase in the
RT   biosynthesis of isoprenoid epoxycyclohexenone natural products.";
RL   Org. Lett. 19:5376-5379(2017).
CC   -!- FUNCTION: Decarboxylase; part of the gene cluster that mediates the
CC       biosynthesis of macrophorins, isoprenoid epoxycyclohexenones containing
CC       cyclized drimane moieties (PubMed:28926261). The first step of the
CC       pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the
CC       polyketide synthase macA (PubMed:28926261). 6-MSA is then converted to
CC       m-cresol by the decarboxylase macB (By similarity). The cytochrome P450
CC       monooxygenase macC then catalyzes the oxidation of m-cresol to
CC       toluquinol (By similarity). Epoxidation of toluquinol is then performed
CC       by the short chain dehydrogenase macD, with the help of macE, and a
CC       further prenylation by macG leads to 7-deacetoxyyanuthone A (By
CC       similarity). The next step is the hydroxylation of C-22 of 7-
CC       deacetoxyyanuthone A by the cytochrome P450 monooxygenase macH to yield
CC       22-deacetylyanuthone A (By similarity). O-Mevalon transferase macI then
CC       attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to
CC       produce yanuthone E (By similarity). The terpene cyclase macJ catalyzes
CC       the cyclization of 22-deacetylyanuthone A to macrophorin A
CC       (PubMed:28926261). MacJ is also able to catalyze cyclization of
CC       yanuthone E and 7-deacetoxyyanuthone A to their corresponding
CC       macrophorins (PubMed:28926261). The macJ products can be further
CC       modified by macH and macJ, as well as by the FAD-dependent
CC       monooxygenase macF, to produce additional macrophorins, including 4'-
CC       oxomacrophorin A, 4'-oxomacrophorin D and 4'-oxomacrophorin E
CC       (PubMed:28926261). {ECO:0000250|UniProtKB:G3Y417,
CC       ECO:0000269|PubMed:28926261}.
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:0000250|UniProtKB:G3Y417};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23113;
CC         Evidence={ECO:0000250|UniProtKB:G3Y417};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:28926261}.
CC   -!- MISCELLANEOUS: The macrophorins cluster contains a single gene
CC       insertion (encoding for the terpene cyclase macJ) compared with the
CC       yanuthone cluster that produces the linear compound yanuthone.
CC       {ECO:0000269|PubMed:28926261}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ACMSD family. {ECO:0000305}.
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DR   EMBL; MF989997; AVK70098.1; -; Genomic_DNA.
DR   EMBL; MH388470; QBC75450.1; -; Genomic_DNA.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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   Decarboxylase; Lyase; Metal-binding; Zinc.
FT   CHAIN           1..338
FT                   /note="Decarboxylase macB"
FT                   /id="PRO_0000454085"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TDX5"
FT   BINDING         283
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TDX5"
SQ   SEQUENCE   338 AA;  37146 MW;  B3E0ADF335104EA7 CRC64;
     MNRIDVHHHF IPPAYVKAFN STPGDPSGWH LPKWTPESTL SLMASHSTRT AILSLTAPGT
     SIMSNSPVES ANLARQINLY GFQLHQENPT RFGFFASLPH LTPETIPSAV EELAYALDTL
     QADGITLYTR YSGTGYLGHA AFAPLWEELN RRKAVVFIHP TNTASDAQNK PEMVNPKLPQ
     PIIDYPHETC RTAVDLITSG TISKNPDVKI ILSHGGGTLP ILATRAANLL YDAGLTEITP
     ETFLEQARSF YLDLALSGNV GNLELLVGKN GFAKPGHVLY GSDFPYAPVE TINKYVGMME
     EFFAQGGDKE EVARGAAAEL FPRFRIEDNK EMIPQNRL