ID   CGHE_CHAGB              Reviewed;         137 AA.
AC   Q2HBN2;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   29-SEP-2021, entry version 29.
DE   RecName: Full=Sch210972 biosynthesis cluster protein E {ECO:0000303|PubMed:26360642};
GN   Name=cghE {ECO:0000303|PubMed:26360642}; ORFNames=CHGG_02372;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=26360642; DOI=10.1002/cbic.201500386;
RA   Sato M., Yagishita F., Mino T., Uchiyama N., Patel A., Chooi Y.H., Goda Y.,
RA   Xu W., Noguchi H., Yamamoto T., Hotta K., Houk K.N., Tang Y., Watanabe K.;
RT   "Involvement of lipocalin-like CghA in decalin-forming stereoselective
RT   intramolecular [4+2] cycloaddition.";
RL   ChemBioChem 16:2294-2298(2015).
CC   -!- FUNCTION: Part of the gene cluster that mediates the biosynthesis of
CC       the tetramic acid Sch210972, a potential anti-HIV fungal natural
CC       product that contains a decalin core (PubMed:26360642). The PKS module
CC       of cghG together with the enoylreductase cghC catalyze the formation of
CC       the polyketide unit which is then conjugated to 4-hydroxyl-4-methyl
CC       glutamate (HMG) by the condensation domain of the cghG NRPS module
CC       (PubMed:26360642). One unique structural feature of Sch210972 is the
CC       tetramic acid motif proposed to be derived from the non-proteinogenic
CC       amino acid HMG, by a Dieckmann-type condensation catalyzed by the
CC       reductase domain of cghG (PubMed:26360642). The aldolase cghB catalyzes
CC       the aldol condensation of 2 molecules of pyruvic acid to yield the
CC       intermediate 4-hydroxyl-4-methyl-2-oxoglutarate (HMOG), which can then
CC       be stereoselectively transaminated by an unidentified enzyme to form
CC       HMG (PubMed:26360642). The Diels-Alderase cghA then uses the Dieckmann
CC       product released by cghG as substrate and catalyzes the Diels-Alder
CC       cycloaddition to form the decalin ring of Sch210972 (PubMed:26360642).
CC       CghA also suppresses the nonenzymatic formation of the alternative
CC       stereoisomer (PubMed:26360642). {ECO:0000269|PubMed:26360642}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:26360642}.
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DR   EMBL; CH408030; EAQ90437.1; -; Genomic_DNA.
DR   RefSeq; XP_001228888.1; XM_001228887.1.
DR   EnsemblFungi; EAQ90437; EAQ90437; CHGG_02372.
DR   GeneID; 4388357; -.
DR   HOGENOM; CLU_1864896_0_0_1; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
PE   4: Predicted;
KW   Reference proteome.
FT   CHAIN           1..137
FT                   /note="Sch210972 biosynthesis cluster protein E"
FT                   /id="PRO_0000453357"
FT   REGION          1..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   137 AA;  14594 MW;  FDD7F58D1E832635 CRC64;
     MTKYTSVNSS LPSLPRQTTP TRPATQTGRW DRMGMQTGNT PSSPLGFETK GSLNGSPTLR
     TTLDTSLSGT RSHPALRATR WMMGVNDIDS IQGDEDHPHD PGPDSDAKKR CASGKAPKDR
     PTSSVAVAST IRPPCCG