ID   HMCS1_BLAGE             Reviewed;         453 AA.
AC   P54961;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Hydroxymethylglutaryl-CoA synthase 1;
DE            Short=HMG-CoA synthase 1;
DE            EC=2.3.3.10;
DE   AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase 1;
GN   Name=HMGCS-1;
OS   Blattella germanica (German cockroach) (Blatta germanica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Blattellidae;
OC   Blattella.
OX   NCBI_TaxID=6973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7901012; DOI=10.1111/j.1432-1033.1993.tb18295.x;
RA   Martinez-Gonzalez J., Buesa C., Piulachs M.D., Belles X., Hegardt F.G.;
RT   "3-hydroxy-3-methylglutaryl-coenzyme-A synthase from Blattella germanica.
RT   Cloning, expression, developmental pattern and tissue expression.";
RL   Eur. J. Biochem. 217:691-699(1993).
CC   -!- FUNCTION: This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form
CC       HMG-CoA, which is the substrate for HMG-CoA reductase. {ECO:0000250}.
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   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC       family. {ECO:0000305}.
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DR   EMBL; X73679; CAA52032.1; -; mRNA.
DR   PIR; S38986; S38986.
DR   AlphaFoldDB; P54961; -.
DR   SMR; P54961; -.
DR   BRENDA; 2.3.3.10; 875.
DR   UniPathway; UPA00058; UER00102.
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   CDD; cd00827; init_cond_enzymes; 1.
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   NCBIfam; TIGR01833; HMG-CoA-S_euk; 1.
DR   PANTHER; PTHR43323; 3-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASE; 1.
DR   PANTHER; PTHR43323:SF2; HYDROXYMETHYLGLUTARYL-COA SYNTHASE; 1.
DR   Pfam; PF08540; HMG_CoA_synt_C; 1.
DR   Pfam; PF01154; HMG_CoA_synt_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS01226; HMG_COA_SYNTHASE; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis; Lipid metabolism; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..453
FT                   /note="Hydroxymethylglutaryl-CoA synthase 1"
FT                   /id="PRO_0000213752"
FT   ACT_SITE        84
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT   ACT_SITE        116
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
FT   ACT_SITE        246
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10116"
SQ   SEQUENCE   453 AA;  50332 MW;  C79EB2376270F348 CRC64;
     MWPSDVGIVA LELIFPSQYV DQVDLEVYDN VSAGKYTVGL GQARMGFCTD REDINSLCLT
     VVSRLMERWS IPYSQIGRLE VGTETLLDKS KSVKTVLMQL FKDNTDIEGV DTVNACYGGT
     SALFNAISWV ESSSWDGRYA LVVAGDIAVY AKGSARPTGG AGAVAMLVGA NAPLVFDRGV
     RSSHMQHAYD FYKPDLSSLY PTVDGKLSIQ CYLSALDHCY QLYCSKIQKQ LGEKFDIERL
     DAVLFHAPYC KLVQKSLARL VLNDFVRASE EERTTKYSSL EALKGVKLED TYFDREVEKA
     VMTYSKNMFE EKTKPSLLLA NQVGNMYTPS LYGGLVSLLV SKSAQELAGK RVALFSYGSG
     LASSMFSLRI SSDASAKSSL QRLVSNLSHI KPQLDLRHKV SPEEFAQTME TREHNHHKAP
     YTPEGSIDVL FPGTWYLESV DSLYRRSYKQ VPG
//