ID   ASCM_PETAA              Reviewed;         459 AA.
AC   P0DOW1;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Asperlicin C monooxygenase {ECO:0000305};
DE            EC=1.14.13.216 {ECO:0000269|PubMed:23030663};
GN   Name=aspB {ECO:0000303|PubMed:23030663};
OS   Petromyces alliaceus (Aspergillus alliaceus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=209559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   COFACTOR.
RC   STRAIN=ATCC 20656 / MF4925;
RX   PubMed=23030663; DOI=10.1021/ja308371z;
RA   Haynes S.W., Gao X., Tang Y., Walsh C.T.;
RT   "Assembly of asperlicin peptidyl alkaloids from anthranilate and
RT   tryptophan: a two-enzyme pathway generates heptacyclic scaffold complexity
RT   in asperlicin E.";
RL   J. Am. Chem. Soc. 134:17444-17447(2012).
CC   -!- FUNCTION: Catalyzes the conversion of asperlicin A to form asperlicin
CC       E, a potent cholecystokinin receptor CCK(A) antagonist.
CC       {ECO:0000269|PubMed:23030663}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=asperlicin C + H(+) + NADPH + O2 = asperlicin E + H2O +
CC         NADP(+); Xref=Rhea:RHEA:49056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:90903, ChEBI:CHEBI:90904; EC=1.14.13.216;
CC         Evidence={ECO:0000269|PubMed:23030663};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=asperlicin C + H(+) + NADH + O2 = asperlicin E + H2O + NAD(+);
CC         Xref=Rhea:RHEA:49052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:90903, ChEBI:CHEBI:90904; EC=1.14.13.216;
CC         Evidence={ECO:0000269|PubMed:23030663};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000303|PubMed:23030663};
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P0DOW1; -.
DR   SMR; P0DOW1; -.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..459
FT                   /note="Asperlicin C monooxygenase"
FT                   /id="PRO_0000438497"
FT   BINDING         30
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         323
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         333..337
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
SQ   SEQUENCE   459 AA;  50701 MW;  83C2E4FCC75E8062 CRC64;
     MTMHVEVGPD STAPPHSSGI KVIIIGLGIG GLAAAIECHR KGHSVIAFDK AQELKPVGDG
     IALAHNAVRV IEKWGKGTVG QELGRLSSRL NTTVIYDQTG RFIAEDKLDG FKAGEGHLLP
     RGELSQVMYK HAKSLGIDMR LASEVDEYWE DENSAGVIVD GEKITADCVV ACDGVNSKAR
     RHIIGYEPEL RSSGSCVFRG WMTTEEPLVG SHWLLSHTDQ ADQVKVFAGD GVHVLLSTIQ
     HGKMVFWLCT HKDNDCYDRK KEAPPTPEVD GMIHLIRDWP MRGQIESTIR KTLAKNVMHY
     PLLIREALSN WRSKGGRMVI IGDAAHPFLP VSGQGAAQAI EDAAVLAITL HLAGKEEVPL
     ALHALEKIRL PRTALLQRSS LELERFWLNI DWPEVEKCPE LLTIPRPKWI HGHDCQTHAY
     TEFAKVVSAI QMREEYHPLG GPRDSTNGES LLALLRQDT