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Database: UniProt
Entry: A5A798_BOMMO
LinkDB: A5A798_BOMMO
Original site: A5A798_BOMMO 
ID   A5A798_BOMMO            Unreviewed;       456 AA.
AC   A5A798;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 96.
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   Name=HMG-S_Bm {ECO:0000313|EMBL:BAF62107.1};
GN   Synonyms=100101203 {ECO:0000313|EnsemblMetazoa:NP_001093297.1};
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091 {ECO:0000313|EMBL:BAF62107.1};
RN   [1] {ECO:0000313|EMBL:BAF62107.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P50T {ECO:0000313|EMBL:BAF62107.1};
RC   TISSUE=Pheromone gland {ECO:0000313|EMBL:BAF62107.1};
RX   PubMed=17628279; DOI=10.1016/j.ibmb.2007.03.008;
RA   Kinjoh T., Kaneko Y., Itoyama K., Mita K., Hiruma K., Shinoda T.;
RT   "Control of juvenile hormone biosynthesis in Bombyx mori: cloning of the
RT   enzymes in the mevalonate pathway and assessment of their developmental
RT   expression in the corpora allata.";
RL   Insect Biochem. Mol. Biol. 37:808-818(2007).
RN   [2] {ECO:0000313|Proteomes:UP000005204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p50T {ECO:0000313|Proteomes:UP000005204};
RX   PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG   International Silkworm Genome Consortium;
RT   "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL   Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN   [3] {ECO:0000313|EnsemblMetazoa:NP_001093297.1}
RP   IDENTIFICATION.
RC   STRAIN=p50T (Dazao) {ECO:0000313|EnsemblMetazoa:NP_001093297.1};
RG   EnsemblMetazoa;
RL   Submitted (JUN-2022) to UniProtKB.
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; AB274989; BAF62107.1; -; mRNA.
DR   RefSeq; NP_001093297.1; NM_001099827.1.
DR   AlphaFoldDB; A5A798; -.
DR   SMR; A5A798; -.
DR   STRING; 7091.A5A798; -.
DR   PaxDb; 7091-BGIBMGA004001-TA; -.
DR   EnsemblMetazoa; NM_001099827.1; NP_001093297.1; GeneID_100101203.
DR   GeneID; 100101203; -.
DR   KEGG; bmor:100101203; -.
DR   CTD; 100101203; -.
DR   eggNOG; KOG1393; Eukaryota.
DR   HOGENOM; CLU_008065_0_1_1; -.
DR   InParanoid; A5A798; -.
DR   OMA; DDAYNWI; -.
DR   OrthoDB; 1060at2759; -.
DR   UniPathway; UPA00058; UER00102.
DR   Proteomes; UP000005204; 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   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000313|EMBL:BAF62107.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU364071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005204};
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          6..177
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01154"
FT   DOMAIN          178..455
FT                   /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08540"
FT   ACT_SITE        86
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        120
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   ACT_SITE        250
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT   BINDING         212
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         255
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT   BINDING         259
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
SQ   SEQUENCE   456 AA;  50917 MW;  C8061C417C06038D CRC64;
     MGGKVENVGI LAMELYFPSQ YVDQTELEKF DEVSTGKYTI GLGQSKMGFC SDREDINSIC
     LTALHRLIDK QKINLHDIGR LEVGTETIID KSKSVKTFLM TLFAKEGATD IEGIDTTNAC
     YGGTAALFNA INWVESSSWD GRKAIVVAGD IAVYGKGPAR PTGGAGAVAM LIGPDAPLVF
     DCGVRASYMT HAYDFYKPDL SSEFPYVDGK LSIQCYLNAL DNCYNLFSKK MRKTDPNFKG
     LLSLDGMLFH SPYCKLVQKS LARVCFNDFL NIPAEEREKQ FPGLSEFSNH KLEDTYFDRE
     VEKAFMTYSL SLFEEKTKPS LHIARNVGNM YTPSLYGGLV SYLISKSPDQ LIGKKFALFS
     YGSGLASTMY SINVCHDMST GSKLEKLISS LHETVALLDK RQSVEPSKFS DIMDVRTKNY
     HSAPYEPTGS LDVLFPGTYY LVKIDDQRRR TYDRKH
//
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