HYPC_ASPFN
ID HYPC_ASPFN Reviewed; 210 AA.
AC B8NI03;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Noranthrone monooxygenase;
DE EC=1.13.12.20;
GN Name=hypC; ORFNames=AFLA_139400;
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=20348292; DOI=10.1128/aem.02495-09;
RA Ehrlich K.C., Li P., Scharfenstein L., Chang P.K.;
RT "HypC, the anthrone oxidase involved in aflatoxin biosynthesis.";
RL Appl. Environ. Microbiol. 76:3374-3377(2010).
CC -!- FUNCTION: Monooxygenase that converts norsolorinic acid anthrone to
CC norsolorinic acid during aflatoxin biosynthesis.
CC {ECO:0000269|PubMed:20348292}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=noranthrone + O2 = H2O + norsolorinic acid;
CC Xref=Rhea:RHEA:35191, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:71533, ChEBI:CHEBI:77904; EC=1.13.12.20;
CC Evidence={ECO:0000269|PubMed:20348292};
CC -!- PATHWAY: Mycotoxin biosynthesis; aflatoxin biosynthesis.
CC {ECO:0000269|PubMed:20348292}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Cells accumulate excess amounts of norsolorinic
CC acid (NA) and a small amount of norsolorinic acid anthrone (NAA).
CC {ECO:0000269|PubMed:20348292}.
CC -!- SIMILARITY: Belongs to the anthrone oxygenase family. {ECO:0000305}.
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DR EMBL; EQ963478; EED51174.1; -; Genomic_DNA.
DR RefSeq; XP_002379950.1; XM_002379909.1.
DR AlphaFoldDB; B8NI03; -.
DR STRING; 5059.CADAFLAP00007815; -.
DR EnsemblFungi; EED51174; EED51174; AFLA_139400.
DR VEuPathDB; FungiDB:AFLA_139400; -.
DR eggNOG; ENOG502SBMN; Eukaryota.
DR HOGENOM; CLU_105974_0_0_1; -.
DR OMA; RMYHYGH; -.
DR UniPathway; UPA00287; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0045122; P:aflatoxin biosynthetic process; IEA:UniProtKB-UniPathway.
PE 1: Evidence at protein level;
KW Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..210
FT /note="Noranthrone monooxygenase"
FT /id="PRO_0000422196"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 210 AA; 23567 MW; 6C9F7AFBB767EEEA CRC64;
MEDLRDLSPR DLHKARGAKE EFKNVFLLAD GELTVHASFS RIFTRRTNKM GTEYVAVLTG
SFLTGAMMNL HLLTIPILIE TTRQPAQLVH QWSRIFYSGH RKGPGIALVT GALYGYAAWA
KYSVGEPWHH WMVAGVTTVS MVPYTWMFMN ATNTALFHAE DQFEKGGVEI SLQESVRLVG
KWDWLNTVRA LFPLAGSVMG MLGVCGVVRY
