CHEE_CHAGB
ID CHEE_CHAGB Reviewed; 512 AA.
AC P0CU31; Q2HEW2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Cytochrome P450 monooxygenase cheE {ECO:0000303|PubMed:33622536};
DE EC=1.-.-.- {ECO:0000305|PubMed:23611317};
DE AltName: Full=Chaetoglobosin A biosynthesis cluster protein E {ECO:0000303|PubMed:33622536};
GN Name=cheE {ECO:0000303|PubMed:33622536}; ORFNames=CHGG_01242-1;
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, DISRUPTION PHENOTYPE, AND PATHWAY.
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, AND INDUCTION.
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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of chaetoglobosin A which has a unique
CC inhibitory activity against actin polymerization in mammalian cells
CC (PubMed:23611317, PubMed:33622536). Chaetoglobosin A and its
CC intermediates are involved in the morphological differentiation of
CC C.globosum (PubMed:33622536). The first step of the pathway is the
CC synthesis of prochaetoglobosin I via condensation of one acetyl-CoA, 8
CC malonyl-CoA, and a L-tryptophan molecule by the PKS-NRPS hybrid
CC synthetase cheA, followed by reduction of backbone double bond to
CC install desired geometry by the enoyl reductase cheB (PubMed:23611317).
CC Further multiple oxidation steps performed by the cytochrome P450
CC monooxygenases cheE and cheG, as well as by the FAD-linked
CC oxidoreductase cheF, lead to the formation of chaetoglobosin A
CC (PubMed:23611317). Depending on the order of action of these
CC reductases, distinct intermediates can be identified (PubMed:23611317).
CC Within the pathway, the cytochrome P450 monooxygenase cheE catalyzes a
CC stereospecific epoxidation on prochaetoglobosin I, cytoglobosin D, and
CC chaetoglobosin J intermediates (PubMed:23611317). The FAD-linked
CC oxidoreductase cheF performs dehydrogenation of the C-20 hydroxyl
CC groups in the 20-dihyrochaetoglobosin A and cytoglobosin D
CC intermediates (PubMed:23611317). Finally, the cytochrome P450
CC monooxygenase cheG can catalyze the stereospecific dihydroxylation of
CC prochaetoglobosin I and prochaetoglobosin IV at C-19 and C-20,
CC respectively (PubMed:23611317). The Diels-Alderase cheD may play a role
CC in the post-PKS-NRPS biosynthetic steps catalyzing Diels-Alder
CC cyclization (Probable). {ECO:0000269|PubMed:23611317,
CC ECO:0000269|PubMed:33622536, ECO:0000305|PubMed:33622536}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:23611317}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
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: Impairs the production of chaetoglobosin A but
CC leads to the accumulation of cytoglobosin D and chaetoglobosin J
CC (PubMed:23611317). {ECO:0000269|PubMed:23611317}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ93007.1; Type=Erroneous gene model prediction; Note=The predicted gene CHGG_01242 has been split into 2 genes: CHGG_01242-1 and CHGG_01242-2.; Evidence={ECO:0000269|PubMed:23611317};
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DR EMBL; CH408029; EAQ93007.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0CU31; -.
DR SMR; P0CU31; -.
DR EnsemblFungi; EAQ93007; EAQ93007; CHGG_01242.
DR OrthoDB; 317492at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR019771; F-actin_capping_bsu_CS.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..512
FT /note="Cytochrome P450 monooxygenase cheE"
FT /evidence="ECO:0000255"
FT /id="PRO_0000438243"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 455
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 512 AA; 57842 MW; DE99E7E858527252 CRC64;
MTGFYFAAES SWSPYVILVL ALAAMVANRL VRPKRPNDGL NHIPMLEFED GDNSTERYIR
DTWALLHAGY LKYTKRGMPF QMRNPADPDH PQVVLPAKYL SELKSAPESR FSFRLYSEQA
FLLNYSHAPK QTDRTTHMVR TEMNKNMGAL LEATQEEIEV ALASKLPNST AWEPATPYMA
LAYTTSRAIA RVLGGRELSG SEEWIGMNVG VTGMTHQAAQ QIREQYPPHL RWMARWRHPG
ARAVIATRRR SAQIVDPIIQ KRLAGAQDTK PGEPDGIQWM LAAQGSRRPS AQEVADEQLF
VGIASVHTTS ATSLSILYDL LDRPNVAEEI IGEINAVAAR HRDVGGRWTK QALSELEKLD
SFMAESFRFN PVGLVTMQRS AVVDYVFQDG LRLPKHTQIL FPTCEFNRDG DVHPNPDVFD
PWRFLKMRKA GDPNKHHFAY VSDQMVGFGG GTHACPGRYF ASYEIKLILI HMLTRYDIKW
PDGLTRPPNM VHDFSNVPNF TATVLFRNKS KS
