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
//