HCS1_ZYMTI
ID HCS1_ZYMTI Reviewed; 460 AA.
AC F9X3D9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 25-MAY-2022, entry version 50.
DE RecName: Full=Hydroxymethylglutaryl-CoA synthase MYCGRDRAFT_54740 {ECO:0000303|PubMed:28818040};
DE Short=HMG-CoA synthase MYCGRDRAFT_54740 {ECO:0000303|PubMed:28818040};
DE EC=2.3.3.10 {ECO:0000305|PubMed:28818040};
DE AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase MYCGRDRAFT_54740 {ECO:0000255|RuleBase:RU364071};
DE AltName: Full=Ferrichrome A-like siderophore biosynthesis protein MYCGRDRAFT_54740 {ECO:0000303|PubMed:28818040};
GN Name=ERG13; ORFNames=MYCGRDRAFT_54740;
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: Hydroxymethylglutaryl-CoA synthase involved in the
CC biosynthesis of a ferrichrome A-like siderophors which may contribute
CC to organismal virulence (Probable). The first step of siderophore
CC 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 -!- CATALYTIC ACTIVITY:
CC Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-
CC methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10;
CC Evidence={ECO:0000250|UniProtKB:Q4P3F1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189;
CC Evidence={ECO:0000250|UniProtKB:Q4P3F1};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:28818040}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {ECO:0000305}.
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DR EMBL; CM001197; EGP90734.1; -; Genomic_DNA.
DR RefSeq; XP_003855758.1; XM_003855710.1.
DR AlphaFoldDB; F9X3D9; -.
DR SMR; F9X3D9; -.
DR STRING; 1047171.Mycgr3P54740; -.
DR EnsemblFungi; Mycgr3T54740; Mycgr3P54740; Mycgr3G54740.
DR GeneID; 13403698; -.
DR KEGG; ztr:MYCGRDRAFT_54740; -.
DR VEuPathDB; FungiDB:ZTRI_2.154; -.
DR eggNOG; KOG1393; Eukaryota.
DR HOGENOM; CLU_008065_0_1_1; -.
DR InParanoid; F9X3D9; -.
DR Proteomes; UP000008062; Chromosome 2.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:EnsemblFungi.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:EnsemblFungi.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR000590; HMG_CoA_synt_AS.
DR InterPro; IPR013746; HMG_CoA_synt_C_dom.
DR InterPro; IPR013528; HMG_CoA_synth_N.
DR InterPro; IPR010122; HMG_CoA_synthase_euk.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF08540; HMG_CoA_synt_C; 1.
DR Pfam; PF01154; HMG_CoA_synt_N; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01833; HMG-CoA-S_euk; 1.
DR PROSITE; PS01226; HMG_COA_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Reference proteome; Transferase; Virulence.
FT CHAIN 1..460
FT /note="Hydroxymethylglutaryl-CoA synthase MYCGRDRAFT_54740"
FT /id="PRO_0000451097"
FT ACT_SITE 86
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 120
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 262
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
SQ SEQUENCE 460 AA; 51028 MW; 1FF81541C1785C5E CRC64;
MAARPNNIGI KAIELYFPSQ CVDQAELEKF DGVSAGKYTI GLGQTRMSFC DDREDIYSLT
LTTVSSLLRK YNIDPKSIGR LEVGTETLLD KSKSCKTVLM QLFEPCGNTN IEGVDTVNAC
YGGTNALFNT LNWMESSAWD GRNAIVVAGD IALYKKGNAR PTGGAGCVAM LIGPDAPLVI
EPGLRGSFVK HAYDFYKADL TSEYPLVDGQ YSIKCYTEAV DKCYEAYNGR EKTLKSQANG
HSNGVDAAQE APLDRFDYMC FHAPTCKLVS KSYARLLYND YLADPTNELF KEVPAELKDL
SYEASITDKT VEKTFMGLAK KRFAQRVQPS IQVPTMCGNM YCASVYASLV SLISNVSSAD
FQGKRVGIFS YGSGLASSLF SLKVKGSTEE ITKNLNLQER LDARRVVAPE VYDEMCNLRE
KAHLQKDFKP KGSVDTILPN TYYLTNVDDM FRREYEVKKE
