FER4_ZYMTI
ID FER4_ZYMTI Reviewed; 306 AA.
AC F9XMX6;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Enoyl-CoA isomerase/hydratase MYCGRDRAFT_76805 {ECO:0000303|PubMed:28818040};
DE EC=4.2.1.17 {ECO:0000250|UniProtKB:Q4PEN0};
DE AltName: Full=Ferrichrome A-like siderophore biosynthesis protein MYCGRDRAFT_76805 {ECO:0000303|PubMed:28818040};
GN ORFNames=MYCGRDRAFT_76805;
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: Enoyl-CoA isomerase/hydratase involved in the biosynthesis of
CC a ferrichrome A-like siderophore which may contribute to organismal
CC virulence (Probable). The first step of siderophore biosynthesis is
CC performed by the HMG-CoA synthase (HMGS) MYCGRDRAFT_54740 which
CC catalyzes the generation of HMG-CoA and CoA using acetoacetyl-CoA and
CC acetyl-CoA as substrates (By similarity). The enoyl-CoA
CC isomerase/hydratase MYCGRDRAFT_76805 then catalyzes the conversion of
CC HMG-CoA to methylglutaconyl-CoA (By similarity). The acyltransferase
CC MYCGRDRAFT_85486 then fuses methylglutaconyl-CoA with hydroxyornithine
CC to yield methylglutaconyl hydroxyornithine (By similarity).
CC Methylglutaconyl hydroxyornithine is then available for use by the
CC nonribosomal peptide synthetase NRPS2 to generate the ferrichrome A-
CC like siderophore (By similarity). {ECO:0000250|UniProtKB:Q4P3F1,
CC ECO:0000250|UniProtKB:Q4PEM9, ECO:0000250|UniProtKB:Q4PEN0,
CC ECO:0000250|UniProtKB:Q4PEN1, ECO:0000305|PubMed:28818040}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:58856; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q4PEN0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16106;
CC Evidence={ECO:0000250|UniProtKB:Q4PEN0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC ChEBI:CHEBI:137480; EC=4.2.1.17;
CC Evidence={ECO:0000250|UniProtKB:Q4PEN0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20725;
CC Evidence={ECO:0000250|UniProtKB:Q4PEN0};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:28818040}.
CC -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001206; EGP83314.1; -; Genomic_DNA.
DR RefSeq; XP_003848338.1; XM_003848290.1.
DR AlphaFoldDB; F9XMX6; -.
DR SMR; F9XMX6; -.
DR STRING; 1047171.Mycgr3P76805; -.
DR EnsemblFungi; Mycgr3T76805; Mycgr3P76805; Mycgr3G76805.
DR GeneID; 13396294; -.
DR KEGG; ztr:MYCGRDRAFT_76805; -.
DR VEuPathDB; FungiDB:ZTRI_11.199; -.
DR eggNOG; KOG1679; Eukaryota.
DR HOGENOM; CLU_009834_7_6_1; -.
DR InParanoid; F9XMX6; -.
DR Proteomes; UP000008062; Chromosome 11.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
PE 3: Inferred from homology;
KW Isomerase; Lyase; Reference proteome; Virulence.
FT CHAIN 1..306
FT /note="Enoyl-CoA isomerase/hydratase MYCGRDRAFT_76805"
FT /evidence="ECO:0000255"
FT /id="PRO_0000451098"
FT BINDING 103..107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P42126"
FT SITE 173
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P42126"
SQ SEQUENCE 306 AA; 32851 MW; 972F5D258BC8997C CRC64;
MFALAQHTAR RTLSRQQWTK VVVSAANYSS GSLSSTIRIS SIPAPHTGEI TVLSLNRPRA
RNAISTALLG ELNTVVEQLH AQGDKSSTRA LILTSESDDA FCAGADLKER LTFTEEDTRN
FLKTLRHTFT RLSTLPIPTI SAISSIAFGG GLELALCTNF RVLASTASIG LPETRLAIIP
GGGGTYRLPA LIGETRARDL ILTGRRVSGE EAYFIGLADR LVQISEQELG EKGVARGRVL
EEATAMAKGI CEGGPVAIRA AQAAVSGWRD GEGSENKAYE RVIPTKDRLE ALTAFGEKRK
PSFQGR
