ERG10_SCHPO
ID ERG10_SCHPO Reviewed; 395 AA.
AC Q9UQW6; P78835; Q1L848;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Acetyl-CoA acetyltransferase {ECO:0000250|UniProtKB:P41338};
DE EC=2.3.1.9 {ECO:0000250|UniProtKB:P41338};
DE AltName: Full=Acetoacetyl-CoA thiolase {ECO:0000250|UniProtKB:P41338};
DE AltName: Full=Ergosterol biosynthesis protein 10 {ECO:0000250|UniProtKB:P41338};
GN Name=erg10; ORFNames=SPBC215.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=8750242; DOI=10.1002/yea.320111509;
RA Katayama S., Adachi N., Takao K., Nakagawa T., Matsuda H., Kawamukai M.;
RT "Molecular cloning and sequencing of the hcs gene, which encodes 3-hydroxy-
RT 3-methylglutaryl coenzyme A synthase of Schizosaccharomyces pombe.";
RL Yeast 11:1533-1537(1995).
RN [4]
RP FUNCTION.
RX PubMed=8896278;
RX DOI=10.1002/(sici)1097-0061(19960915)12:11<1107::aid-yea992>3.0.co;2-e;
RA Lum P.Y., Edwards S., Wright R.;
RT "Molecular, functional and evolutionary characterization of the gene
RT encoding HMG-CoA reductase in the fission yeast, Schizosaccharomyces
RT pombe.";
RL Yeast 12:1107-1124(1996).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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). Erg10 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 eg10 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 hcs1 (Probable). {ECO:0000250|UniProtKB:P41338,
CC ECO:0000305}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21037;
CC Evidence={ECO:0000250|UniProtKB:P41338};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC {ECO:0000250|UniProtKB:P41338}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P41338}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; D89184; BAA13846.1; -; mRNA.
DR EMBL; CU329671; CAA22123.1; -; Genomic_DNA.
DR PIR; T39899; T39899.
DR PIR; T42741; T42741.
DR RefSeq; NP_596686.1; NM_001022609.2.
DR AlphaFoldDB; Q9UQW6; -.
DR SMR; Q9UQW6; -.
DR BioGRID; 277142; 5.
DR STRING; 4896.SPBC215.09c.1; -.
DR iPTMnet; Q9UQW6; -.
DR MaxQB; Q9UQW6; -.
DR PaxDb; Q9UQW6; -.
DR PRIDE; Q9UQW6; -.
DR EnsemblFungi; SPBC215.09c.1; SPBC215.09c.1:pep; SPBC215.09c.
DR GeneID; 2540616; -.
DR KEGG; spo:SPBC215.09c; -.
DR PomBase; SPBC215.09c; erg10.
DR VEuPathDB; FungiDB:SPBC215.09c; -.
DR eggNOG; KOG1390; Eukaryota.
DR HOGENOM; CLU_031026_0_1_1; -.
DR InParanoid; Q9UQW6; -.
DR OMA; ICPSIAI; -.
DR PhylomeDB; Q9UQW6; -.
DR UniPathway; UPA00058; UER00101.
DR PRO; PR:Q9UQW6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; ISS:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006696; P:ergosterol biosynthetic process; ISS:PomBase.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Metal-binding; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..395
FT /note="Acetyl-CoA acetyltransferase"
FT /id="PRO_0000310395"
FT ACT_SITE 90
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 185
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 230
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 246
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 247
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 249
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 250
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT BINDING 347
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P24752"
FT CONFLICT 387
FT /note="A -> P (in Ref. 1; BAA13846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 40998 MW; 382822A9EF686544 CRC64;
MVNTEVYIVS AVRTPMGSFG GSFASLPATK LGSIAIKGAL ERVNIKPSDV DEVFMGNVVS
ANLGQNPARQ CALGAGLPRS IVCTTVNKVC ASGMKATILG AQTIMTGNAE IVVAGGTESM
SNAPYYAPKN RFGAKYGNVE LVDGLLRDGL SDAYDGLPMG NAAELCAEEH SIDRASQDAF
AISSYKRAQN AQATKAFEQE IVPVEVPVGR GKPNKLVTED EEPKNLNEDK LKSVRAVFKS
NGTVTAANAS TLNDGASALV LMSAAKVKEL GLKPLAKIIG WGEAAQDPER FTTSPSLAIP
KALKHAGIEA SQVDYYEINE AFSVVAVANT KILGLDPERV NINGGGVAMG HPLGSSGSRI
ICTLAYILAQ KDAKIGVAAV CNGGGGASSI VIERV
