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Database: UniProt
Entry: A0A1J1HX27_9DIPT
LinkDB: A0A1J1HX27_9DIPT
Original site: A0A1J1HX27_9DIPT 
ID   A0A1J1HX27_9DIPT        Unreviewed;       458 AA.
AC   A0A1J1HX27;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Hydroxymethylglutaryl-CoA synthase {ECO:0000256|RuleBase:RU364071};
DE            Short=HMG-CoA synthase {ECO:0000256|RuleBase:RU364071};
DE            EC=2.3.3.10 {ECO:0000256|RuleBase:RU364071};
DE   AltName: Full=3-hydroxy-3-methylglutaryl coenzyme A synthase {ECO:0000256|RuleBase:RU364071};
GN   ORFNames=CLUMA_CG005528 {ECO:0000313|EMBL:CRK91908.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK91908.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRK91908.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA
CC       to form HMG-CoA. {ECO:0000256|RuleBase:RU364071}.
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:0000256|RuleBase:RU364071};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC       {ECO:0000256|RuleBase:RU364071}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. HMG-CoA synthase
CC       family. {ECO:0000256|ARBA:ARBA00007061, ECO:0000256|RuleBase:RU364071}.
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DR   EMBL; CVRI01000021; CRK91908.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1HX27; -.
DR   STRING; 568069.A0A1J1HX27; -.
DR   OrthoDB; 1060at2759; -.
DR   UniPathway; UPA00058; UER00102.
DR   Proteomes; UP000183832; Unassembled WGS sequence.
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; 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; 3-HYDROXY-3-METHYLGLUTARYL COENZYME A SYNTHASE; 1.
DR   Pfam; PF08540; HMG_CoA_synt_C; 1.
DR   Pfam; PF01154; HMG_CoA_synt_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW   Steroid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW   Steroid metabolism {ECO:0000256|RuleBase:RU364071};
KW   Sterol biosynthesis {ECO:0000256|RuleBase:RU364071};
KW   Sterol metabolism {ECO:0000256|RuleBase:RU364071};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364071}.
FT   DOMAIN          3..176
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          177..457
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   ACT_SITE        85
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        119
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        251
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   BINDING         211
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         256
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         260
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
SQ   SEQUENCE   458 AA;  51334 MW;  39FAB86CBAE308BA CRC64;
     MSWPSDVGIL GIELVFPSLF VDQTELEQFD GVSAGKYTVG LGQDRMGFCT DREDINSLCL
     TVVSNLMKRY DVKPKDIGRL EVGTETIIDK SKSVKSVLMQ LFEPHGVTDL EGIDTTNACY
     GGTAALFNAI NWVESSNYDG RLALVVCGDI AVYAKGSARP TGGAGAIAML VGPNAPLVFD
     RGVRSIYMKH AYDFYKPDLS SEYPTVDGKL SIQCYLSALD NCYRLYHQKY QRLHPNATVI
     GLNQFDALIF HTPYCKLVQK SLARISLNDF LLTSDSQKRK ELYPTFYEKY DSIKLEDTYF
     DRDVEKIFMD YSKGTFNEKT KPSLLLANQV GNMYTPSVYS GLVSLLISAD ADVSKLNGRH
     VGVFSYGSGL ASTMYSISIT SDSSKLQSLL DKLSYVKPLL EQRTKISPEQ FTSLMETRAH
     NSHRTNYEPS GDVSMLFPGT YYLKFVDDMH RRTYEKRE
//
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