CPAO_ASPFN
ID CPAO_ASPFN Reviewed; 455 AA.
AC B8NI10; C9K4U3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Beta-cyclopiazonate dehydrogenase {ECO:0000305};
DE EC=1.21.99.1 {ECO:0000269|PubMed:19410456, ECO:0000269|PubMed:19663400};
DE AltName: Full=Beta-Cyclopiazonate oxidocyclase {ECO:0000305};
DE AltName: Full=FAD-dependent oxidoreductase cpaO {ECO:0000305};
DE Flags: Precursor;
GN Name=cpaO {ECO:0000303|PubMed:19663400};
GN ORFNames=AFLA_139470 {ECO:0000312|EMBL:EED51181.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP COFACTOR.
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=19410456; DOI=10.1016/j.bmcl.2009.04.073;
RA Seshime Y., Juvvadi P.R., Tokuoka M., Koyama Y., Kitamoto K., Ebizuka Y.,
RA Fujii I.;
RT "Functional expression of the Aspergillus flavus PKS-NRPS hybrid CpaA
RT involved in the biosynthesis of cyclopiazonic acid.";
RL Bioorg. Med. Chem. Lett. 19:3288-3292(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19663400; DOI=10.1021/bi901123r;
RA Liu X., Walsh C.T.;
RT "Cyclopiazonic acid biosynthesis in Aspergillus sp.: characterization of a
RT reductase-like R* domain in cyclopiazonate synthetase that forms and
RT releases cyclo-acetoacetyl-L-tryptophan.";
RL Biochemistry 48:8746-8757(2009).
CC -!- FUNCTION: Beta-cyclopiazonate dehydrogenase involved in the synthesis
CC of the fungal neurotoxin alpha-cyclopiazonic acid (CPA). CpaO carries
CC out the dehydrogenation of beta-CPA to yield an unstable enimine
CC product, which is captured by intramolecular cyclization to create the
CC pentacyclic fused scaffold of alpha-cyclopiazonate.
CC {ECO:0000269|PubMed:19410456, ECO:0000269|PubMed:19663400}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + beta-cyclopiazonate = AH2 + alpha-cyclopiazonate;
CC Xref=Rhea:RHEA:14525, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58067, ChEBI:CHEBI:58256; EC=1.21.99.1;
CC Evidence={ECO:0000269|PubMed:19410456, ECO:0000269|PubMed:19663400};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:19410456};
CC -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; EQ963478; EED51181.1; -; Genomic_DNA.
DR EMBL; AB493825; BAI43679.1; -; Genomic_DNA.
DR RefSeq; XP_002379957.1; XM_002379916.1.
DR AlphaFoldDB; B8NI10; -.
DR SMR; B8NI10; -.
DR EnsemblFungi; EED51181; EED51181; AFLA_139470.
DR VEuPathDB; FungiDB:AFLA_139470; -.
DR eggNOG; ENOG502R1TU; Eukaryota.
DR HOGENOM; CLU_028280_0_0_1; -.
DR OMA; WASDYST; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0050448; F:beta-cyclopiazonate dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..455
FT /note="Beta-cyclopiazonate dehydrogenase"
FT /id="PRO_0000430693"
SQ SEQUENCE 455 AA; 50795 MW; 9FC62FDB330D38F0 CRC64;
MATRIASFIG ISTVASLALA NGINVPDTIS RDVIILGAGS SGTYAAIRLK DEGKTVAVVE
RNDYLGGHGE TYYTEDNTPL NFGVEGFFNT SVTRNYLERL QVPYGRRNPA PAHEDYVNLN
TGQRTEYPPG QLQDREAFAK WVDAISQFGF LDDGVYRITE PVPEDLIIPF ADFVKKYHLE
DAVYALFSHT SGDVLEMITL YVIQYIGIPH AAALNEGYVR PIEGIAALYK SAGKELGSDV
LLKTTPESVQ RSKDGVEVTV RSADGTKTLL KGKQLLVTIP PLLENLHGFP LSDQESRIFS
KWQYHQYWAA LVNDTGLPDD VNIVNVDTER LYGVPEEPFI WRLDNHWAPG YHNIKLVGGS
DFGEDEAKAY MYEKLDLLHE EGTYSTHKPE IVKFASHTPV TMFVSAEEIR GGFYRQLYEL
QGLNSTFWTG ATWASDYSTL LWGYTDEVLD QMASS