ID   ASAB_ASPFN              Reviewed;         227 AA.
AC   B8N0E7;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Hydroxylase/desaturase asaB {ECO:0000303|PubMed:29674152};
DE            EC=1.-.-.- {ECO:0000269|PubMed:29674152};
DE   AltName: Full=Aspergillic acid biosynthesis cluster protein B {ECO:0000303|PubMed:29674152};
GN   Name=asaB {ECO:0000303|PubMed:29674152}; ORFNames=AFLA_023010;
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   IDENTIFICATION WITHIN THE CLUSTER, AND INDUCTION.
RX   PubMed=23834374; DOI=10.1111/mpp.12056;
RA   Dolezal A.L., Obrian G.R., Nielsen D.M., Woloshuk C.P., Boston R.S.,
RA   Payne G.A.;
RT   "Localization, morphology and transcriptional profile of Aspergillus flavus
RT   during seed colonization.";
RL   Mol. Plant Pathol. 14:898-909(2013).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=29674152; DOI=10.1016/j.fgb.2018.04.009;
RA   Lebar M.D., Cary J.W., Majumdar R., Carter-Wientjes C.H., Mack B.M.,
RA   Wei Q., Uka V., De Saeger S., Diana Di Mavungu J.;
RT   "Identification and functional analysis of the aspergillic acid gene
RT   cluster in Aspergillus flavus.";
RL   Fungal Genet. Biol. 116:14-23(2018).
CC   -!- FUNCTION: Hydroxylase/desaturase; part of the gene cluster that
CC       mediates the biosynthesis of aspergillic acid, a hydroxamic acid-
CC       containing pyrazinone with aliphatic side chains that originates from
CC       leucine (Leu) and isoleucine (Ile) (PubMed:29674152). Aspergillic acid
CC       has antibiotic properties and was shown to be lethal to mice
CC       (PubMed:29674152). The first step in the pathway is the production of
CC       deoxyaspergillic acid via a condensation between the Ile amine and the
CC       Leu carboxylic acid, followed by a reductive release from the protein
CC       forming the dipeptide aldehyde NH(2)-Leu-Ile-CHO, which could undergo
CC       an intermolecular cyclization resulting in a dihydropyrazinone
CC       (PubMed:29674152). As the NRPS asaC lacks a condensation domain, it is
CC       improbable that it is responsible for condensation of Leu and Ile
CC       (PubMed:29674152). One possibility is that asaC acts on a previously
CC       condensed dipeptide and functions as a Leu-Ile reductase to yield
CC       deoxyaspergillic acid (PubMed:29674152). After asaC forms
CC       deoxyaspergillic acid, the cytochrome P450 asaD oxidizes the pyrazinone
CC       to the hydroxamic acid-containing bioactive metabolite aspergillic acid
CC       (PubMed:29674152). The hydroxylase/desaturase asaB can then convert
CC       aspergillic acid to hydroxyaspergillic acid (PubMed:29674152). Both
CC       aspergillic acid and hydroxyaspergillic acid can form complexes with
CC       iron producing ferriaspergillin analogs (PubMed:29674152).
CC       {ECO:0000269|PubMed:29674152}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:29674152}.
CC   -!- INDUCTION: Expressed during the earliest stages of maize kernel
CC       infection (PubMed:23834374). {ECO:0000269|PubMed:23834374}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of hydroxyaspergillic
CC       acid and leads to a reduction of ferriaspergillin analog containing
CC       hydroxyaspergillic acid (PubMed:29674152).
CC       {ECO:0000269|PubMed:29674152}.
CC   -!- SIMILARITY: Belongs to the asaB hydroxylase/desaturase family.
CC       {ECO:0000305}.
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DR   EMBL; EQ963473; EED55030.1; -; Genomic_DNA.
DR   RefSeq; XP_002373812.1; XM_002373771.1.
DR   AlphaFoldDB; B8N0E7; -.
DR   SMR; B8N0E7; -.
DR   EnsemblFungi; EED55030; EED55030; AFLA_023010.
DR   VEuPathDB; FungiDB:AFLA_023010; -.
DR   eggNOG; ENOG502RZAA; Eukaryota.
DR   HOGENOM; CLU_042688_2_0_1; -.
DR   OMA; AVCDWSS; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR044053; AsaB-like.
DR   PANTHER; PTHR34598; PTHR34598; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase.
FT   CHAIN           1..227
FT                   /note="Hydroxylase/desaturase asaB"
FT                   /id="PRO_0000444457"
SQ   SEQUENCE   227 AA;  26072 MW;  70C2263D1FDF9626 CRC64;
     MRFRQQVETC LNYWPAEGPV QRELILGTVG AYRRPIDSRP VLIQDVRGQE GTFTLDIHGF
     QFIKHISQHV ASFDEASVLK DNMTALEAEH LLKTRWAIVN IWRPLKPVPR DPLAVSDARS
     FHDKDLLEIY GRVPGRQAKK DYDAATKGSG FGMLYGKYSP GQQWFYMSDM KPDEALLIKC
     YDSKDDGRTA RRTPHTAFVD PRTRDVKVAR ESLELRCLVF FEDQPLA