ID   ATO1_OMPOL              Reviewed;         393 AA.
AC   Q52UT1;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Acyltransferase ato1 {ECO:0000303|PubMed:16019163};
DE            EC=2.3.1.- {ECO:0000305|PubMed:16019163};
DE   AltName: Full=Ferrichrome A biosynthesis cluster protein ato1 {ECO:0000303|PubMed:16019163};
GN   Name=ato1 {ECO:0000303|PubMed:16019163};
OS   Omphalotus olearius (Jack o'lantern).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Omphalotaceae; Omphalotus.
OX   NCBI_TaxID=72120;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=TA90170;
RX   PubMed=16019163; DOI=10.1016/j.femsle.2005.06.013;
RA   Welzel K., Eisfeld K., Antelo L., Anke T., Anke H.;
RT   "Characterization of the ferrichrome A biosynthetic gene cluster in the
RT   homobasidiomycete Omphalotus olearius.";
RL   FEMS Microbiol. Lett. 249:157-163(2005).
CC   -!- FUNCTION: L-ornithine N(5)-monooxygenase; part of the siderophore
CC       biosynthetic pathway (PubMed:16019163). Omphalotus olearius produces
CC       ferrichrome A, but no other siderophore has been detected
CC       (PubMed:16019163). Ferrichrome A consists of a hexapeptide ring made up
CC       of one glycine, two serine, and three N(5)-hydroxyornithine amino acid
CC       residues, the latter acylated by trans-(alpha-methyl)-glutaconic acid
CC       residues (PubMed:16019163). The biosynthesis of ferrichrome A depends
CC       on the hydroxylation of ornithine to N(5)-hydroxyornithine, catalyzed
CC       by the monooxygenase omo1 (PubMed:16019163). The second step, the
CC       acylation of N(5)-hydroxy-L-ornithine is probably catalyzed by the N-
CC       acyltransferase ato1 (PubMed:16019163). Finally, assembly of
CC       ferrichrome A is catalyzed by the nonribosomal peptide synthase (NRPS)
CC       fso1 (PubMed:16019163). {ECO:0000269|PubMed:16019163}.
CC   -!- PATHWAY: Siderophore biosynthesis; ferrichrome biosynthesis.
CC       {ECO:0000305|PubMed:16019163}.
CC   -!- SIMILARITY: Belongs to the lysine N-acyltransferase mbtK family.
CC       {ECO:0000305}.
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DR   EMBL; AY929616; AAX49354.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q52UT1; -.
DR   SMR; Q52UT1; -.
DR   UniPathway; UPA00783; -.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031169; P:ferrichrome biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR019432; Acyltransferase_MbtK/IucB-like.
DR   SMART; SM01006; AlcB; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Transferase.
FT   CHAIN           1..393
FT                   /note="Acyltransferase ato1"
FT                   /id="PRO_0000444317"
SQ   SEQUENCE   393 AA;  44426 MW;  773CC8E2DE46F25F CRC64;
     MTTRTSGYVR EEFVAPPEHT FTLPDSTIVR SIEQDGTVEV FLAQSSAPIA IFSPHARTLR
     VSPHGIVNDD RAVSSPAPCF TTAEPALSTE DAWAALYALW MRRTEKDVLP LVLDSRTESL
     KPYLVQTGLA FSPPDAQSEF ELLVVRAAFW QGAGAPVNRH WLQNMVPDPS TSIAPFPAIT
     SFTRTEHVLT THPLRPPKPA PGAVIYSRYI HTVNQQLTLT HIDANNLEHF AAYSRWQNSE
     RVNIGWRERG PDEKHRKYLA DRLADLHSMG VIIAWDGQLA GYGEVCWVKE DPMGTYVGGL
     GDYDQGIHIL IGEEKFRGRH RFTAVMTSLY HACFLREPRT EVVVSEPRAD LPIVPRLIAY
     LPQELNREFE LPHKRAVYTV VRRERFFQAA MLY