HMGC2_DANRE
ID HMGC2_DANRE Reviewed; 335 AA.
AC A8WG57;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic;
DE EC=4.1.3.4;
DE AltName: Full=3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1;
GN Name=hmgcll1; ORFNames=zgc:172206;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase
CC that catalyzes a cation-dependent cleavage of (S)-3-hydroxy-3-
CC methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in
CC ketogenesis, the products of which support energy production in
CC nonhepatic animal tissues. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA;
CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57288; EC=4.1.3.4;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Metabolic intermediate metabolism; (S)-3-hydroxy-3-
CC methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-
CC methylglutaryl-CoA: step 1/1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HMG-CoA lyase family. {ECO:0000305}.
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DR EMBL; BC154587; AAI54588.1; -; mRNA.
DR RefSeq; NP_001103870.1; NM_001110400.1.
DR AlphaFoldDB; A8WG57; -.
DR SMR; A8WG57; -.
DR STRING; 7955.ENSDARP00000105104; -.
DR PaxDb; A8WG57; -.
DR Ensembl; ENSDART00000164764; ENSDARP00000133158; ENSDARG00000088740.
DR GeneID; 571388; -.
DR KEGG; dre:571388; -.
DR CTD; 54511; -.
DR ZFIN; ZDB-GENE-080220-15; hmgcll1.
DR eggNOG; KOG2368; Eukaryota.
DR GeneTree; ENSGT00940000159467; -.
DR InParanoid; A8WG57; -.
DR OrthoDB; 1029775at2759; -.
DR PhylomeDB; A8WG57; -.
DR Reactome; R-DRE-77111; Synthesis of Ketone Bodies.
DR UniPathway; UPA00896; UER00863.
DR PRO; PR:A8WG57; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 13.
DR Bgee; ENSDARG00000088740; Expressed in mature ovarian follicle and 8 other tissues.
DR ExpressionAtlas; A8WG57; baseline.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0046951; P:ketone body biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR030021; ER-cHL.
DR InterPro; IPR043594; HMGL.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR42738; PTHR42738; 1.
DR PANTHER; PTHR42738:SF5; PTHR42738:SF5; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Lipid metabolism;
KW Lipoprotein; Lyase; Membrane; Metal-binding; Myristate; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..335
FT /note="3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic"
FT /id="PRO_0000334671"
FT DOMAIN 43..310
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT ACT_SITE 276
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 335 AA; 35891 MW; 2BBAFD527B08EE2C CRC64;
MGNVSSAVKH CLSYETFLRD YPWLPRLLWE EKCSELPKLP VYVKIVEVGP RDGLQNEKEI
VPTEVKIQLI DLLSQTGLPV IEATSFVSSK WVAQMADHTA VLKGIKRSPD VRYPVLTPNI
QGFQAAVAAG ANEVAVFGSA SETFSRKNIN CSIEESLQRF EQVVSAAKQE GIPVRGYVSC
ALGCPYEGQV KPSQVTKVAK RLFELGCYEV SLGDTIGVGT AGSMAEMLSD VLTEVPAGAL
AVHCHDTYGQ ALPNILIALQ MGVSVVDASV AGLGGCPFAK GASGNVSTED LLYMLHGLGI
ETGVDLLKVM EAGDFICKAL NRKTNSKVSQ ATRNN
