P13704 (HMCS1_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hydroxymethylglutaryl-CoA synthase, cytoplasmic
Short name=HMG-CoA synthase
EC=2.3.3.10

Alternative name(s):
3-hydroxy-3-methylglutaryl coenzyme A synthase

Gene names

Name:	HMGCS1
Synonyms:	HMGCS

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	520 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase.
Catalytic activity	Acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA.
Pathway	Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the HMG-CoA synthase family.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Cellular component	Cytoplasm
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW isoprenoid biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	hydroxymethylglutaryl-CoA synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 520	520	Hydroxymethylglutaryl-CoA synthase, cytoplasmic		PRO_0000213746
Sites
	Active site	129	1	Potential
Amino acid modifications
	Modified residue	4	1	Phosphoserine By similarity
	Modified residue	46	1	N6-acetyllysine By similarity
	Modified residue	246	1	N6-acetyllysine By similarity
	Modified residue	273	1	N6-acetyllysine By similarity
	Modified residue	321	1	N6-acetyllysine By similarity
	Modified residue	495	1	Phosphoserine By similarity
	Modified residue	516	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13704 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 2D4CAAE7DEE5D6BB	FASTA	520	57,318
	10 20 30 40 50 60 MPGSLPLNAE ACWPKDVGIV ALEIYFPSQY VDQAELEKYD GVDAGKYTIG LGQARMGFCT 70 80 90 100 110 120 DREDINSLCL TVVQNLMERN SLSYDCIGRL EVGTETIIDK SKSVKSNLMQ LFEESGNTDI 130 140 150 160 170 180 EGIDTTNACY GGTAAVFNAV NWIESSSWDG RYALVVAGDI AIYATGNARP TGGVGAVALL 190 200 210 220 230 240 IGPNAPLIFD RGLRGTHMQH AYDFYKPDML SEYPIVDGKL SIQCYLSALD RCYSVYRKKI 250 260 270 280 290 300 RAQWQKEGND NDFTLNDFGF MISHSPYCKL VQKSLARMFL NDFLNDQNRD KNSIYSGLEA 310 320 330 340 350 360 FGDVKLEDTY FDRDVEKAFM KASSELFNQK TKASLLVSNQ NGNMYTSSVY GSLASVLAQY 370 380 390 400 410 420 SPQQLAGKRI GVFSYGSGLA ATLYSLKVTQ DATPGSALDK VTASLCDLKS RLDSRTCVAP 430 440 450 460 470 480 DVFAENMKLR EDTHHLANYI PQCSIDSLFE GTWYLVRVDE KHRRTYARRP STNDHNLGDG 490 500 510 520 VGLVHSNTAT EHIPSPAKKV PRLPATAAES ESAVISNGEH

References

[1]

"Cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase from the hamster. I. Isolation and sequencing of a full-length cDNA." Gil G., Goldstein J.L., Slaughter C.A., Brown M.S. J. Biol. Chem. 261:3710-3716(1986) [PubMed: 2869035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Ovary.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L00334 , L00326, L00327, L00328, L00329, L00330, L00331, L00332, L00333 Genomic DNA. Translation: AAA37076.1.
PIR	A25332.
3D structure databases
ProteinModelPortal	P13704.
SMR	P13704. Positions 16-470.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG051912.
Enzyme and pathway databases
BRENDA	2.3.3.10. 1309.
Family and domain databases
InterPro	IPR000590. HMG_CoA_synt_AS. IPR013746. HMG_CoA_synt_C. IPR013528. HMG_CoA_synth_N. IPR010122. HMG_CoA_synthase_euk. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.
Pfam	PF08540. HMG_CoA_synt_C. 1 hit. PF01154. HMG_CoA_synt_N. 1 hit. [Graphical view]
SUPFAM	SSF53901. Thiolase-like. 2 hits.
TIGRFAMs	TIGR01833. HMG-CoA-S_euk. 1 hit.
PROSITE	PS01226. HMG_COA_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HMCS1_CRIGR

Accession

Primary (citable) accession number: P13704

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program