ER10B_GIBZE
ID ER10B_GIBZE Reviewed; 396 AA.
AC I1RY81;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Acetyl-CoA acetyltransferase ERG10, cytosolic {ECO:0000303|PubMed:30874562};
DE EC=2.3.1.9 {ECO:0000305|PubMed:30874562};
DE AltName: Full=Acetoacetyl-CoA thiolase ERG10 {ECO:0000305};
DE Short=ACAT {ECO:0000305};
DE AltName: Full=Cytosolic thiolase ERG10 {ECO:0000305};
DE Short=CT {ECO:0000305};
DE AltName: Full=Ergosterol biosynthesis protein 10 {ECO:0000303|PubMed:30874562};
GN Name=ERG10 {ECO:0000303|PubMed:30874562};
GN ORFNames=FG09321, FGRAMPH1_01T27377;
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: Acetyl-CoA acetyltransferase; part of the first module of
CC 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). ERG10B catalyzes the formation of acetoacetyl-CoA from
CC acetyl-CoA (By similarity). The first module starts with the action of
CC the cytosolic acetyl-CoA acetyltransferase ERG10B that catalyzes the
CC formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases
CC ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA.
CC The rate-limiting step of the early module is the reduction to
CC mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA)
CC reductases HMG1 (Probable). {ECO:0000250|UniProtKB:Q4WCL5,
CC ECO:0000305|PubMed:30874562}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020,
CC ECO:0000305|PubMed:30874562};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:Q4WCL5};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC {ECO:0000305|PubMed:30874562}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P41338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
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. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; HG970335; CEF84991.1; -; Genomic_DNA.
DR RefSeq; XP_011328435.1; XM_011330133.1.
DR STRING; 5518.FGSG_09321P0; -.
DR GeneID; 23556278; -.
DR KEGG; fgr:FGSG_09321; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G27377; -.
DR eggNOG; KOG1390; Eukaryota.
DR HOGENOM; CLU_031026_0_1_1; -.
DR InParanoid; I1RY81; -.
DR UniPathway; UPA00058; UER00101.
DR Proteomes; UP000070720; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Potassium; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT CHAIN 1..396
FT /note="Acetyl-CoA acetyltransferase ERG10, cytosolic"
FT /id="PRO_0000454670"
FT ACT_SITE 91
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT ACT_SITE 351
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 381
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q4WCL5"
FT BINDING 227
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q4WCL5"
FT BINDING 230
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:Q4WCL5"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q4WCL5"
FT BINDING 247
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q4WCL5"
FT BINDING 347
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:Q4WCL5"
FT BINDING 382
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:Q4WCL5"
SQ SEQUENCE 396 AA; 41189 MW; D0FB61FCD13CF7C7 CRC64;
MANLPPVYIV STARTPIGSF LGSLSSQTAV QLGSVAIKGA VERAGIKPED VDEVFFGNVL
SAGVGQGPAR QCALGAGLPQ TVIATTVNKV CASSLKAIIL GAQNIMLGTS DIVVAGGTES
MSNTPHYLPN LRNGAKYGDQ TLVDGVLKDG LTDSFKKDHM GISAELCVDD HDLTREAQDE
YAINSYKKAQ AATEAGLFTE IVPVEIPGGR GKPAIKVERD DEVKNLNVDK LKAMRPAFKP
DGTVTAPNAA PINDGAAAVV LVSEAKLKEL NLKPVAKILG WGDAEREPER FTIAPALAIP
KAIKHAGLTA EQVEYYEINE AFSAVALANM KILGLNPDQV NVYGGSVAIG HPLGCSGARI
VTTLTSVLKE RKAKIGAVGI CNGGGGASAM VIENLQ
