ID   ANAAT_NEOFI             Reviewed;         509 AA.
AC   A1DN11;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=O-acetyltransferase ANAat {ECO:0000303|PubMed:19001367};
DE            EC=2.3.1.- {ECO:0000269|PubMed:19001367, ECO:0000269|PubMed:20165805};
DE   AltName: Full=Acetylaszonalenin synthesis protein anaAT {ECO:0000303|PubMed:19001367};
GN   Name=anaAT {ECO:0000303|PubMed:19001367}; ORFNames=NFIA_055310;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX   PubMed=19001367; DOI=10.1074/jbc.m807606200;
RA   Yin W.B., Grundmann A., Cheng J., Li S.M.;
RT   "Acetylaszonalenin biosynthesis in Neosartorya fischeri. Identification of
RT   the biosynthetic gene cluster by genomic mining and functional proof of the
RT   genes by biochemical investigation.";
RL   J. Biol. Chem. 284:100-109(2009).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=20165805; DOI=10.1039/b922440h;
RA   Yin W.B., Xie X.L., Matuschek M., Li S.M.;
RT   "Reconstruction of pyrrolo[2,3-b]indoles carrying an alpha-configured
RT   reverse C3-dimethylallyl moiety by using recombinant enzymes.";
RL   Org. Biomol. Chem. 8:1133-1141(2010).
CC   -!- FUNCTION: O-acetyltransferase; part of the gene cluster that mediates
CC       the biosynthesis of the prenylated pyrroloindoline diketopiperazine
CC       acetylaszonalenin (PubMed:19001367). The first step in the pathway is
CC       the formation of (R)-benzodiazepinedione by condensation of tryptophan
CC       and anthranilic acid catalyzed by the non-ribosomal peptide synthetase
CC       anaPS (PubMed:19001367). The prenyltransferase anaPT then converts (R)-
CC       benzodiazepinedione to aszonalenin in the presence of dimethylallyl
CC       diphosphate (DMAPP) via C3-prenylation (PubMed:19001367,
CC       PubMed:20165805). The last step in the biosynthesis of
CC       acetylaszonalenin via acetylation of aszonalenin at position N1
CC       catalyzed by anaAT (PubMed:19001367, PubMed:20165805).
CC       {ECO:0000269|PubMed:19001367, ECO:0000269|PubMed:20165805}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=61 uM for aszonalenin {ECO:0000269|PubMed:19001367};
CC         KM=96 uM for acetyl coenzyme A {ECO:0000269|PubMed:19001367};
CC   -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:19001367}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4WZ64}.
CC   -!- SIMILARITY: Belongs to the fumigaclavine B O-acetyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; DS027698; EAW16182.1; -; Genomic_DNA.
DR   RefSeq; XP_001258079.1; XM_001258078.1.
DR   AlphaFoldDB; A1DN11; -.
DR   SMR; A1DN11; -.
DR   EnsemblFungi; EAW16182; EAW16182; NFIA_055310.
DR   GeneID; 4584594; -.
DR   KEGG; nfi:NFIA_055310; -.
DR   VEuPathDB; FungiDB:NFIA_055310; -.
DR   eggNOG; ENOG502RPW3; Eukaryota.
DR   HOGENOM; CLU_026450_1_1_1; -.
DR   OMA; ILPRMYF; -.
DR   OrthoDB; 1130893at2759; -.
DR   BioCyc; MetaCyc:MON-18808; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alkaloid metabolism; Reference proteome; Transferase.
FT   CHAIN           1..509
FT                   /note="O-acetyltransferase ANAat"
FT                   /id="PRO_0000438418"
SQ   SEQUENCE   509 AA;  56729 MW;  A192287632C23267 CRC64;
     MTVTISFEPY VGSSVDALSI PLYLRCQLVF KLSKPLAAVP LLESGVNRLV QALPFLSGEF
     TAVPASDGGK EILLVRPVLN FELSRILKIK YHETSLRHVC KQMNRPSSQG GDLPHEPYMP
     YPRLPDPSRP QPIVGFQVNV HTDGIILSVA THHCSFDATG MGSIVQNLAA CCRSPPSDEP
     DLTTSPAQEA EARKVLSQVR ETPFDPKMFP EYRPLDSMLS YYKGVQSALQ GRQTTIVNRC
     FTIAADKINA LKRRCNQLIP EMVKKYGLST EDAIGSAWVS SNDVVAALLW TCINRARYPE
     IRERSVHQLP PDLLHATSSL GVPVNVRSRL SPPLPKSTLG NAVCLLREKV PLQFFALPSH
     ANMEATSSVC ADHSGDDEWA LSFCRVAYGL RAKLNAIDDD YIRDYISYVQ KSPCHLSVTL
     DTENLYLSNW REIGVYDADF GGMLGKPLRM RAPDGYTDGL IFVMAQRSED KSAPWEFNIS
     LEASTMKRIV HDPLWCKYVE LDAFWHGEE