| Tag |
Content |
LipidDB ID |
LipidDB-9606-00352 |
Entry Name |
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UniProt Accession |
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Theoretical PI |
6.12 |
Molecular Weight |
39514.32 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
3-hydroxymethyl-3-methylglutaryl-CoA lyase, cytoplasmic |
Protein Synonyms/Alias |
4.1.3.4; 3-hydroxymethyl-3-methylglutaryl-CoA lyase-like protein 1; Endoplasmic reticulum 3-hydroxymethyl-3-methylglutaryl-CoA lyase; er-cHL; |
Gene Name |
HMGCLL1 |
Gene Synonyms/Alias |
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Created Date |
20-MAY-2008 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGNVPSAVK | [1] | N-Myristoylation |
|
Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Montgomery C, Pei Z, Watkins PA, Miziorko HM. Identification andcharacterization of an extramitochondrial human 3-hydroxy-3-methylglutaryl-CoAlyase. J Biol Chem. 2012 Sep 28;287(40):33227-36. Epub 2012 Aug 3.[ PMID:22865860]
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Functional Description |
Non-mitochondrial 3-hydroxymethyl-3-methylglutaryl-CoA lyase that catalyzes a cation-dependent cleavage of (S)-3-hydroxy- 3-methylglutaryl-CoA into acetyl-CoA and acetoacetate, a key step in ketogenesis, the products of which support energy production in nonhepatic animal tissues. |
Sequence Annotation |
Active site: 311 311
Metal binding site: 87 87 Divalent metal cation.
Metal binding site: 278 278 Divalent metal cation.
Metal binding site: 280 280 Divalent metal cation.
Metal binding site: 320 320 Divalent metal cation.
Binding site: 86 86 Substrate.
|
Protein Length |
370 AA. |
Protein Sequence
(Canonical) |
MGNVPSAVKH CLSYQQLLRE HLWIGDSVAG ALDPAQTSLL TNLHCFQPDV SGFSVSLAGT 60
VACIHWETSQ LSGLPEFVKI VEVGPRDGLQ NEKVIVPTDI KIEFINRLSQ TGLSVIEVTS 120
FVSSRWVPQM ADHTEVMKGI HQYPGVRYPV LTPNLQGFHH AVAAGATEIS VFGAASESFS 180
KKNINCSIEE SMGKFEEVVK SARHMNIPAR GYVSCALGCP YEGSITPQKV TEVSKRLYGM 240
GCYEISLGDT IGVGTPGSMK RMLESVMKEI PPGALAVHCH DTYGQALANI LTALQMGINV 300
VDSAVSGLGG CPYAKGASGN VATEDLIYML NGLGLNTGVN LYKVMEAGDF ICKAVNKTTN 360
SKVAQASFNA 370
|
FASTA
(Canonical) |
>LipidDB-9606-00352|Q8TB92
MGNVPSAVKHCLSYQQLLREHLWIGDSVAGALDPAQTSLLTNLHCFQPDVSGFSVSLAGT
VACIHWETSQLSGLPEFVKIVEVGPRDGLQNEKVIVPTDIKIEFINRLSQTGLSVIEVTS
FVSSRWVPQMADHTEVMKGIHQYPGVRYPVLTPNLQGFHHAVAAGATEISVFGAASESFS
KKNINCSIEESMGKFEEVVKSARHMNIPARGYVSCALGCPYEGSITPQKVTEVSKRLYGM
GCYEISLGDTIGVGTPGSMKRMLESVMKEIPPGALAVHCHDTYGQALANILTALQMGINV
VDSAVSGLGGCPYAKGASGNVATEDLIYMLNGLGLNTGVNLYKVMEAGDFICKAVNKTTN
SKVAQASFNA
|
Gene Ontology |
GO:0005829; C:cytosol; IDA:UniProtKB GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB GO:0016020; C:membrane; IDA:UniProtKB GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB GO:0004419; F:hydroxymethylglutaryl-CoA lyase activity; IDA:UniProtKB GO:0046872; F:metal ion binding; ISS:UniProtKB GO:0046951; P:ketone body biosynthetic process; IDA:UniProtKB |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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