ERG13_GIBZE
ID ERG13_GIBZE Reviewed; 456 AA.
AC I1RY35; A0A098DM80;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Hydroxymethylglutaryl-CoA synthase ERG13 {ECO:0000303|PubMed:30874562};
DE Short=HMG-CoA synthase {ECO:0000303|PubMed:30874562};
DE EC=2.3.3.10 {ECO:0000305|PubMed:30874562};
DE AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase ERG13 {ECO:0000305};
DE AltName: Full=Ergosterol biosynthesis protein 13 {ECO:0000303|PubMed:30874562};
GN Name=RGE13 {ECO:0000303|PubMed:30874562};
GN ORFNames=FG09266, FGRAMPH1_01T27519;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=30874562; DOI=10.1038/s41467-019-09145-6;
RA Liu Z., Jian Y., Chen Y., Kistler H.C., He P., Ma Z., Yin Y.;
RT "A phosphorylated transcription factor regulates sterol biosynthesis in
RT Fusarium graminearum.";
RL Nat. Commun. 10:1228-1228(2019).
CC -!- FUNCTION: Hydroxymethylglutaryl-CoA synthase; part of the first module
CC of ergosterol biosynthesis pathway that includes the early steps of the
CC pathway, conserved across all eukaryotes, and which results in the
CC formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By
CC similarity). ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form
CC hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module
CC starts with the action of the cytosolic acetyl-CoA acetyltransferase
CC ERG10B that catalyzes the formation of acetoacetyl-CoA. The
CC hydroxymethylglutaryl-CoA synthases ERG13 then condenses acetyl-CoA
CC with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the
CC early module is the reduction to mevalonate by the 3-hydroxy-3-
CC methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 (Probable).
CC {ECO:0000250|UniProtKB:P41338, ECO:0000305|PubMed:30874562}.
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:0000255|PROSITE-ProRule:PRU10116,
CC ECO:0000305|PubMed:30874562};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189;
CC Evidence={ECO:0000250|UniProtKB:P41338};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC {ECO:0000305|PubMed:30874562}.
CC -!- INDUCTION: Expression is regulated by the Zn(2)-C6 fungal-type
CC transcription factor FgSR which binds directly to the promoter.
CC {ECO:0000269|PubMed:30874562}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC family. {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; HG970335; CEF82946.1; -; Genomic_DNA.
DR RefSeq; XP_011328502.1; XM_011330200.1.
DR STRING; 5518.FGSG_09266P0; -.
DR GeneID; 23556228; -.
DR KEGG; fgr:FGSG_09266; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G27519; -.
DR eggNOG; KOG1393; Eukaryota.
DR HOGENOM; CLU_008065_0_1_1; -.
DR InParanoid; I1RY35; -.
DR UniPathway; UPA00058; UER00102.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Lipid biosynthesis; Lipid metabolism; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase.
FT CHAIN 1..456
FT /note="Hydroxymethylglutaryl-CoA synthase ERG13"
FT /id="PRO_0000454671"
FT ACT_SITE 86
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 118
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT ACT_SITE 259
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
SQ SEQUENCE 456 AA; 50352 MW; 70DF1FAEFC94DE27 CRC64;
MSSRPQNIGI KAIELYFPSQ YVDQVELEKF DGVSAGKYTI GLGQTKMSFC DDREDIYSFA
LTATSKLLKN YNIDPNSIGF LEVGTETLLD KSKSVKSVLM QLFGDNTNIE GVDTINACYG
GTNAVFNAIN WVESSAWDGR DAIVVAGDIA LYAKGNARPT GGAGAVALLI GPNAPIVAEP
GLRGTYMQHA YDFYKPDLTS EYPYVDGHYS VNCYSKALDA AYRAYCKREA KQANGTNGVT
NGDASTKTGL DRFDYMAFHS PTCKLVQKSY ARLLYHDYLA NADSPVFAEV APELRDMDYE
KSLTDKVVEK TFMTLTKKRF QERVNPAIQV ATNCGNMYCG SVWSGLASLI SVVDNKDLEG
KRIGLFSYGS GLAASFLSFR INGSVDKISD VLNIPSRLES RRAVPPETYD QMCDLRKQAH
LQKDYTPKGD PSTILPGTYY LTKVDDMFKR EYAIKE
