CPAO_ASPOR
ID CPAO_ASPOR Reviewed; 455 AA.
AC Q2UG11;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Beta-cyclopiazonate dehydrogenase {ECO:0000303|PubMed:21608094};
DE EC=1.21.99.1 {ECO:0000303|PubMed:21608094};
DE AltName: Full=Beta-Cyclopiazonate oxidocyclase {ECO:0000303|PubMed:21608094};
DE AltName: Full=FAD-dependent oxidoreductase cpaO {ECO:0000305};
DE Flags: Precursor;
GN Name=cpaO {ECO:0000250|UniProtKB:F5HN72};
GN ORFNames=AO090026000003 {ECO:0000312|EMBL:BAE59504.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000312|EMBL:BAE59504.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=NBRC 4177;
RX PubMed=21608094; DOI=10.1002/cbic.201000672;
RA Kato N., Tokuoka M., Shinohara Y., Kawatani M., Uramoto M., Seshime Y.,
RA Fujii I., Kitamoto K., Takahashi T., Takahashi S., Koyama Y., Osada H.;
RT "Genetic safeguard against mycotoxin cyclopiazonic acid production in
RT Aspergillus oryzae.";
RL ChemBioChem 12:1376-1382(2011).
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:0000303|PubMed:21608094}.
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:0000303|PubMed:21608094};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:B8NI10};
CC -!- SIMILARITY: Belongs to the beta-cyclopiazonate dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AP007159; BAE59504.1; -; Genomic_DNA.
DR RefSeq; XP_001821506.1; XM_001821454.2.
DR AlphaFoldDB; Q2UG11; -.
DR SMR; Q2UG11; -.
DR EnsemblFungi; BAE59504; BAE59504; AO090026000003.
DR GeneID; 5993534; -.
DR KEGG; aor:AO090026000003; -.
DR VEuPathDB; FungiDB:AO090026000003; -.
DR HOGENOM; CLU_028280_0_0_1; -.
DR OMA; WASDYST; -.
DR Proteomes; UP000006564; Chromosome 3.
DR GO; GO:0050448; F:beta-cyclopiazonate dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome; Signal; Virulence.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..455
FT /note="Beta-cyclopiazonate dehydrogenase"
FT /id="PRO_0000430692"
SQ SEQUENCE 455 AA; 50983 MW; 387A45ECE71D7A72 CRC64;
MAVRIARFLG LSTVAYLALA NGIDARDTIS RDVIILGGGS SGTYAAIRLR DQGKTVAVVE
RNNYLGGHGE TYYTEDNTPL NFGVEGFFNT TVTRNYLERL QVPYGRRDPA PAHEDYVNLN
TGQRTEYTPG QLQDREAFAK WVDAISQFGF LDDGVYRIPE PVPEDLISPF ADFVKKYHLE
DAVYALFSHT SGDVLEMITL YVIQYIGVPH AAALNEGYVR PIEGIAALYK SAGKELGSDV
LLETTPEAVQ RFEDGVEVIV RSADGTKTLL KGKQLLVTIP PLLENLHGFP LSDQESRLFS
KWQYHQYWAA LVNDTGLPDD VNIVNVDTER LYGVPEEPFI WRLDNHWAPG YHNIKLVGGS
EFGEDEAKAY MYERLDLLHA EGTYATHKPE IVKFASHTPV TMFVSAEEIR GGFYRQLYEL
QGLNSTFWTG ATWASDYSTL LWGYTDEVLD QMASS