ID   FER5_ZYMTI              Reviewed;         414 AA.
AC   F9X9V2;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Acyltransferase MYCGRDRAFT_85486 {ECO:0000303|PubMed:28818040};
DE            EC=2.3.-.- {ECO:0000250|UniProtKB:Q4PEN1};
DE   AltName: Full=Ferrichrome A-like siderophore biosynthesis protein MYCGRDRAFT_85486 {ECO:0000303|PubMed:28818040};
GN   ORFNames=MYCGRDRAFT_85486;
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323;
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RX   PubMed=28818040; DOI=10.1186/s12864-017-3969-y;
RA   Cairns T., Meyer V.;
RT   "In silico prediction and characterization of secondary metabolite
RT   biosynthetic gene clusters in the wheat pathogen Zymoseptoria tritici.";
RL   BMC Genomics 18:631-631(2017).
CC   -!- FUNCTION: Acyltransferase; part of the gene cluster 14 that mediates
CC       the biosynthesis of a ferrichrome A-like siderophore which may
CC       contribute to organismal virulence (Probable). The first step of
CC       siderophore biosynthesis is performed by the HMG-CoA synthase (HMGS)
CC       MYCGRDRAFT_54740 which catalyzes the generation of HMG-CoA and CoA
CC       using acetoacetyl-CoA and acetyl-CoA as substrates (By similarity). The
CC       enoyl-CoA isomerase/hydratase MYCGRDRAFT_76805 then catalyzes the
CC       conversion of HMG-CoA to methylglutaconyl-CoA (By similarity). The
CC       acyltransferase MYCGRDRAFT_85486 then fuses methylglutaconyl-CoA with
CC       hydroxyornithine to yield methylglutaconyl hydroxyornithine (By
CC       similarity). Methylglutaconyl hydroxyornithine is then available for
CC       use by the nonribosomal peptide synthetase NRPS2 to generate the
CC       ferrichrome A-like siderophore (By similarity).
CC       {ECO:0000250|UniProtKB:Q4P3F1, ECO:0000250|UniProtKB:Q4PEM9,
CC       ECO:0000250|UniProtKB:Q4PEN0, ECO:0000250|UniProtKB:Q4PEN1,
CC       ECO:0000305|PubMed:28818040}.
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:28818040}.
CC   -!- SIMILARITY: Belongs to the lysine N-acyltransferase mbtK family.
CC       {ECO:0000305}.
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DR   EMBL; CM001199; EGP87766.1; -; Genomic_DNA.
DR   RefSeq; XP_003852790.1; XM_003852742.1.
DR   AlphaFoldDB; F9X9V2; -.
DR   SMR; F9X9V2; -.
DR   STRING; 1047171.Mycgr3P85486; -.
DR   EnsemblFungi; Mycgr3T85486; Mycgr3P85486; Mycgr3G85486.
DR   GeneID; 13400881; -.
DR   KEGG; ztr:MYCGRDRAFT_85486; -.
DR   eggNOG; ENOG502RZMI; Eukaryota.
DR   HOGENOM; CLU_039848_7_0_1; -.
DR   InParanoid; F9X9V2; -.
DR   Proteomes; UP000008062; Chromosome 4.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
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; Reference proteome; Transferase; Virulence.
FT   CHAIN           1..414
FT                   /note="Acyltransferase MYCGRDRAFT_85486"
FT                   /id="PRO_0000451094"
FT   REGION          16..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        367
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   414 AA;  46480 MW;  0656548406837C0D CRC64;
     MTTTTTTTAL TFTLPDGTST VTIRPTQKAA PSEEPSQDTA PSKKDSNHEV YLNDHLIATW
     VIDPSVKTRV SPAQVLDERA EFDSVRHLVL SSRRSNDNGH TWISIYALWL LHHDLDVIPI
     SSPSNSAVTT YLINTGLAAP SPFEPADTDA GRTLLLAREA FWQGAGTPDN LSWLRSRPEA
     SIPGFNSHLG AFASQMSFTR RGNVCTTHPL RPQKPAPGTV VYSRYIVEVG QHLQLVHIDA
     SNPVHFSAYA RWQNSDRVNH GWRERGPDEK HAAYLESQRI DPHTMSLIFL WDGEPAGYSE
     VGWAKEDNTA CFVSSNCGIH IGEFDQLSHI LVGEEKFRGG KRYQAVATSI KHLCFLRDPR
     TTQVIAEPRF DLPSVPIQAR FLPQERKKRV QLPHKQAVLF ALQRERFFQE GHFY