ID B0JZH5_XENTR Unreviewed; 520 AA.
AC B0JZH5; F7DTY0;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=hmgcs1 {ECO:0000313|EMBL:AAI59180.1,
GN ECO:0000313|Ensembl:ENSXETP00000036168,
GN ECO:0000313|RefSeq:NP_001120172.1, ECO:0000313|RefSeq:XP_012811230.1,
GN ECO:0000313|Xenbase:XB-GENE-942074};
GN Synonyms=dhrs7b {ECO:0000313|Ensembl:ENSXETP00000013330};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI59180.1};
RN [1] {ECO:0000313|RefSeq:NP_001120172.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAI59180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testes {ECO:0000313|EMBL:AAI59180.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSXETP00000013330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000013330};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [4] {ECO:0000313|Ensembl:ENSXETP00000013330}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUN-2011) to UniProtKB.
RN [5] {ECO:0000313|RefSeq:NP_001120172.1, ECO:0000313|RefSeq:XP_012811230.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_012811230.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_012811230.1};
RG RefSeq;
RL Submitted (NOV-2023) 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|ARBA:ARBA00001222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10189;
CC Evidence={ECO:0000256|ARBA:ARBA00001222};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
CC {ECO:0000256|ARBA:ARBA00005218, ECO:0000256|RuleBase:RU364071}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; BC159179; AAI59180.1; -; mRNA.
DR RefSeq; NP_001120172.1; NM_001126700.1.
DR RefSeq; XP_012811230.1; XM_012955776.3.
DR Ensembl; ENSXETT00000013330; ENSXETP00000013330; ENSXETG00000006052.
DR Ensembl; ENSXETT00000036168; ENSXETP00000036168; ENSXETG00000016587.
DR GeneID; 100145212; -.
DR KEGG; xtr:100145212; -.
DR AGR; Xenbase:XB-GENE-942074; -.
DR AGR; Xenbase:XB-GENE-946473; -.
DR CTD; 3157; -.
DR Xenbase; XB-GENE-946473; dhrs7b.
DR Xenbase; XB-GENE-942074; hmgcs1.
DR eggNOG; KOG1393; Eukaryota.
DR HOGENOM; CLU_008065_0_1_1; -.
DR OMA; DDAYNWI; -.
DR OrthoDB; 1060at2759; -.
DR TreeFam; TF105361; -.
DR TreeFam; TF313474; -.
DR UniPathway; UPA00058; UER00102.
DR Proteomes; UP000008143; Chromosome 1.
DR Bgee; ENSXETG00000006052; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:InterPro.
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:SF4; HYDROXYMETHYLGLUTARYL-COA SYNTHASE, CYTOPLASMIC; 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 Cholesterol biosynthesis {ECO:0000256|ARBA:ARBA00022778};
KW Cholesterol metabolism {ECO:0000256|ARBA:ARBA00022548};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU364071};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW ECO:0000256|RuleBase:RU364071};
KW Reference proteome {ECO:0000313|Proteomes:UP000008143};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955,
KW ECO:0000256|RuleBase:RU364071};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW ECO:0000256|RuleBase:RU364071};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011,
KW ECO:0000256|RuleBase:RU364071};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166,
KW ECO:0000256|RuleBase:RU364071};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU364071}.
FT DOMAIN 13..185
FT /note="Hydroxymethylglutaryl-coenzyme A synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF01154"
FT DOMAIN 187..469
FT /note="Hydroxymethylglutaryl-coenzyme A synthase C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08540"
FT REGION 479..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 95
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT ACT_SITE 129
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-1"
FT BINDING 221
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT BINDING 269
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
FT BINDING 273
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR610122-2"
SQ SEQUENCE 520 AA; 57339 MW; F61F48A839265BFB CRC64;
MPGSLPPNGE SSWPKDVGIV ALEIYFPSQY VDQVELEKFD GVSAGKYTIG LGQCKMGFCS
DREDINSLCL TVVQRLMERN NLSYDCIGRL EVGTETIIDK SKSVKTVLMQ LFEDSGNTDV
EGIDTTNACY GGTAALFNAV NWVESSSWDG RYALVVAGDI AVYATGSARP TGGAGAVAML
VGPNATLVFE RGLRGTHMQH AYDFYKPDME SEYPVVDGKL SIQCYLSALD HCYTTYRKKI
HAQWQKEGTD KPFTLNDFGF MIFHSPYCKL VQKSLARLLV NDFISDSDPD MESGMYVGLD
SFRDLKLEET YFDRDVEKAF LKASTELFND KTKASLLVSR ENGNMYTPSV YGCLASVLAQ
YSPQQLAGQR IGVFSYGSGF AATMYSLRVS QDAMPGSSLD KLTSSLSDLK ARLDSRKNVS
PSNFADTMKL RQDTHHLANY IPQGSVDDLF PGTWYLVRVD EKHRRFYARS SLMNDGPLDA
APESVHASTA NEHFPSPAKK VPRIPPAAEA VPISVTNGEH
//
