CHED_CHAGB
ID CHED_CHAGB Reviewed; 423 AA.
AC Q2HEW3;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Diels-Alderase cheD {ECO:0000303|PubMed:33622536};
DE EC=5.5.1.- {ECO:0000305|PubMed:33622536};
DE AltName: Full=Chaetoglobosin A biosynthesis cluster protein D {ECO:0000303|PubMed:33622536};
DE Flags: Precursor;
GN Name=cheD {ECO:0000303|PubMed:33622536}; ORFNames=CHGG_01241;
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.
RX PubMed=23611317; DOI=10.1021/ja402828w;
RA Ishiuchi K., Nakazawa T., Yagishita F., Mino T., Noguchi H., Hotta K.,
RA Watanabe K.;
RT "Combinatorial generation of complexity by redox enzymes in the
RT chaetoglobosin A biosynthesis.";
RL J. Am. Chem. Soc. 135:7371-7377(2013).
RN [3]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=33622536; DOI=10.1016/j.funbio.2020.10.010;
RA Cheng M., Zhao S., Liu H., Liu Y., Lin C., Song J., Thawai C.,
RA Charoensettasilp S., Yang Q.;
RT "Functional analysis of a chaetoglobosin A biosynthetic regulator in
RT Chaetomium globosum.";
RL Fungal Biol. 125:201-210(2021).
CC -!- FUNCTION: Diels-Alderase; part of the gene cluster that mediates the
CC biosynthesis of chaetoglobosin A which has a unique inhibitory activity
CC against actin polymerization in mammalian cells (PubMed:23611317,
CC PubMed:33622536). Chaetoglobosin A and its intermediates are involved
CC in the morphological differentiation of C.globosum (PubMed:33622536).
CC The first step of the pathway is the synthesis of prochaetoglobosin I
CC via condensation of one acetyl-CoA, 8 malonyl-CoA, and a L-tryptophan
CC molecule by the PKS-NRPS hybrid synthetase cheA, followed by reduction
CC of backbone double bond to install desired geometry by the enoyl
CC reductase cheB (PubMed:23611317). Further multiple oxidation steps
CC performed by the cytochrome P450 monooxygenases cheE and cheG, as well
CC as by the FAD-linked oxidoreductase cheF, lead to the formation of
CC chaetoglobosin A (PubMed:23611317). Depending on the order of action of
CC these reductases, distinct intermediates can be identified
CC (PubMed:23611317). Within the pathway, the cytochrome P450
CC monooxygenase cheE catalyzes a stereospecific epoxidation on
CC prochaetoglobosin I, cytoglobosin D, and chaetoglobosin J intermediates
CC (PubMed:23611317). The FAD-linked oxidoreductase cheF performs
CC dehydrogenation of the C-20 hydroxyl groups in the 20-
CC dihyrochaetoglobosin A and cytoglobosin D intermediates
CC (PubMed:23611317). Finally, the cytochrome P450 monooxygenase cheG can
CC catalyze the stereospecific dihydroxylation of prochaetoglobosin I and
CC prochaetoglobosin IV at C-19 and C-20, respectively (PubMed:23611317).
CC The Diels-Alderase cheD may play a role in the post-PKS-NRPS
CC biosynthetic steps catalyzing Diels-Alder cyclization (Probable).
CC {ECO:0000269|PubMed:23611317, ECO:0000269|PubMed:33622536,
CC ECO:0000305|PubMed:33622536}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:33622536}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor cheR that binds directly to an asymmetric direct
CC repeat present in the promoter. {ECO:0000269|PubMed:33622536}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of chaetoglobosin A.
CC {ECO:0000269|PubMed:33622536}.
CC -!- SIMILARITY: Belongs to the Diels-Alderase family. {ECO:0000305}.
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DR EMBL; CH408029; EAQ93006.1; -; Genomic_DNA.
DR RefSeq; XP_001220462.1; XM_001220461.1.
DR AlphaFoldDB; Q2HEW3; -.
DR SMR; Q2HEW3; -.
DR EnsemblFungi; EAQ93006; EAQ93006; CHGG_01241.
DR GeneID; 4387647; -.
DR eggNOG; ENOG502SK1F; Eukaryota.
DR HOGENOM; CLU_041924_1_0_1; -.
DR InParanoid; Q2HEW3; -.
DR OMA; GGHERFW; -.
DR OrthoDB; 1068172at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE 2: Evidence at transcript level;
KW Glycoprotein; Isomerase; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..423
FT /note="Diels-Alderase cheD"
FT /id="PRO_5004208867"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 423 AA; 46809 MW; BAEAC5F3AA5C7FA6 CRC64;
MKLCALFAGA VISTSAVAAS WEYAWPEEWH QEWPLDEQGP DAWSSSECTV SRLDAFEMEK
GRKPVFFSTD PLDDPEAPKM LPLNSTGGEQ WEFDGVSEDG QMAFCFGFYR DPNYAILGTG
NLRLSAEFSR PNKTRFVRVD YPSSSTVTSC PWGTRGVWKG ADYSYTFEVT RDIKVARIGV
DAPDLKGSVV MRSVMPPRYP DGSTYPNKEA STEVVPYFRW LEAIPAADVR VDVVMDGQPY
RWSGLGGHER LWTAFSWFTC LQAMTAVRVK AGPFAAVHGS FVSAIDKGLY RPSTVLAEND
EVIFSTTLHE PSDTEDYAVF TKTYGGRVSG NLKEKATGYE LVMVSPSAKK QWSFSITNEA
IGFEYMLGEG VGGTGFSGRA VGGSIGLKQY FGPSFAETLE FPKRSYLFKS NYVDAVPEEK
GEL
