CGHA_CHAGB
ID CGHA_CHAGB Reviewed; 503 AA.
AC Q2HBN6;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Diels-Alderase cghA {ECO:0000303|PubMed:26360642};
DE EC=5.5.1.- {ECO:0000269|PubMed:26360642};
DE AltName: Full=Sch210972 biosynthesis cluster protein A {ECO:0000303|PubMed:26360642};
GN Name=cghA {ECO:0000303|PubMed:26360642}; ORFNames=CHGG_02368;
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, CATALYTIC ACTIVITY, 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).
RN [3] {ECO:0007744|PDB:6KBC}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 109-503.
RA Hara K., Hashimoto H., Maeda N., Sato M., Watanabe K.;
RT "Crystal structure of CghA with Sch210972.";
RL Submitted (JUN-2019) to the PDB data bank.
RN [4] {ECO:0007744|PDB:6KAW}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 109-503.
RA Hara K., Hashimoto H., Yokoyama M., Sato M., Watanabe K.;
RT "Crystal structure of CghA.";
RL Submitted (JUN-2019) to the PDB data bank.
CC -!- FUNCTION: Diels-Alderase; part of the gene cluster that mediates the
CC biosynthesis of the tetramic acid Sch210972, a potential anti-HIV
CC fungal natural product that contains a decalin core (PubMed:26360642).
CC The PKS module of cghG together with the enoylreductase cghC catalyze
CC the formation of the polyketide unit which is then conjugated to 4-
CC hydroxyl-4-methyl glutamate (HMG) by the condensation domain of the
CC cghG NRPS module (PubMed:26360642). One unique structural feature of
CC Sch210972 is the tetramic acid motif proposed to be derived from the
CC non-proteinogenic amino acid HMG, by a Dieckmann-type condensation
CC catalyzed by the reductase domain of cghG (PubMed:26360642). The
CC aldolase cghB catalyzes the aldol condensation of 2 molecules of
CC pyruvic acid to yield the intermediate 4-hydroxyl-4-methyl-2-
CC oxoglutarate (HMOG), which can then be stereoselectively transaminated
CC by an unidentified enzyme to form HMG (PubMed:26360642). The Diels-
CC Alderase cghA then uses the Dieckmann product released by cghG as
CC substrate and catalyzes the Diels-Alder cycloaddition to form the
CC decalin ring of Sch210972 (PubMed:26360642). CghA also suppresses the
CC nonenzymatic formation of the alternative stereoisomer
CC (PubMed:26360642). {ECO:0000269|PubMed:26360642}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-3-[(2S)-3,5-dioxo-4-[(2E,4R,6R,8E,10E,12E)-4,6,12-
CC trimethyltetradeca-2,8,10,12-tetraenoyl]pyrrolidin-2-yl]-2-hydroxy-2-
CC methylpropanoate = sch 210972; Xref=Rhea:RHEA:67268,
CC ChEBI:CHEBI:167897, ChEBI:CHEBI:167907;
CC Evidence={ECO:0000269|PubMed:26360642};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67269;
CC Evidence={ECO:0000269|PubMed:26360642};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26360642}.
CC -!- SIMILARITY: Belongs to the Diels-Alderase family. {ECO:0000305}.
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DR EMBL; CH408030; EAQ90433.1; -; Genomic_DNA.
DR RefSeq; XP_001228884.1; XM_001228883.1.
DR PDB; 6KAW; X-ray; 2.01 A; A=109-503.
DR PDB; 6KBC; X-ray; 1.99 A; A=109-503.
DR PDBsum; 6KAW; -.
DR PDBsum; 6KBC; -.
DR SMR; Q2HBN6; -.
DR EnsemblFungi; EAQ90433; EAQ90433; CHGG_02368.
DR GeneID; 4388353; -.
DR eggNOG; ENOG502SISX; Eukaryota.
DR HOGENOM; CLU_041924_2_0_1; -.
DR InParanoid; Q2HBN6; -.
DR OMA; VGPYAMQ; -.
DR OrthoDB; 1068172at2759; -.
DR BioCyc; MetaCyc:MON-21736; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..503
FT /note="Diels-Alderase cghA"
FT /id="PRO_0000453339"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 166..177
FT /evidence="ECO:0007829|PDB:6KBC"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 198..204
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:6KBC"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 262..270
FT /evidence="ECO:0007829|PDB:6KBC"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 289..308
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 318..324
FT /evidence="ECO:0007829|PDB:6KBC"
FT TURN 326..329
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 331..341
FT /evidence="ECO:0007829|PDB:6KBC"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 347..357
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 360..369
FT /evidence="ECO:0007829|PDB:6KBC"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 446..463
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 471..483
FT /evidence="ECO:0007829|PDB:6KBC"
FT STRAND 490..500
FT /evidence="ECO:0007829|PDB:6KBC"
SQ SEQUENCE 503 AA; 54791 MW; EEB9F0DAC025802E CRC64;
MSGTPRTMPP LMMDWAEQPN GRAKPRGMVI SRVPYLPWYL LGAVRVGGVS NARPNSRPYS
AEQADFGRIS QTALCRYRSM PVRNPTPYGV GTQVWRAVVL HHLPLTAAMA AAPFISLLQG
DQFLADTPIP GSAVIPNSGN LFPKWADKLS PTAVETWLFD AMAEDGSAAF TVSFFRDGSQ
APASFRAAIN AAWSDGTVWS QHLVVPVSVV TSDGPDVGHG HVAGVWRTEE PQSNDTTRTT
ASFDVAADLS TTTVVFDAPG RITGSLTHRS LGYPTLPQSD REAEVAPGAY WFRPIAMANA
TVDLTFHIDD PTNPDKKTEK RMVLGPEQGA FGGMDRSWLP MVWGKEATDA LFVRAQAGPY
VMAVMRLVSK PHKYYQNTVN AALYRDGKIV SNALRSLPPD RRDTAATADA VRTEKLYDGD
GLVAKYRDKN VGYRLEFRSA GPEREKWSFD LRHHQAWWAK PTSRPGPDGT GNSGFVVEVT
GGLVGSEESV HGWGMTGEVE LSD
