Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00312
Entry Name
UniProt Accession
Theoretical PI
8.71
Molecular Weight
44816.12
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Acetyl-CoA acetyltransferase, mitochondrial
Protein Synonyms/Alias
2.3.1.9; Acetoacetyl-CoA thiolase;
Gene Name
Acat1
Gene Synonyms/Alias
Created Date
13-SEP-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
25
Canonical
GLLQEVRCLERSYAS
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Plays a major role in ketone body metabolism.
Sequence Annotation
Region: 255 257 Coenzyme A binding.
Active site: 123 123 Acyl-thioester intermediate.
Active site: 382 382 Proton acceptor.
Active site: 410 410 Proton acceptor.
Metal binding site: 216 216 Potassium.
Metal binding site: 277 277 Potassium; via carbonyl oxygen.
Metal binding site: 278 278 Potassium; via carbonyl oxygen.
Metal binding site: 280 280 Potassium; via carbonyl oxygen.
Metal binding site: 378 378 Potassium; via carbonyl oxygen.
Binding site: 216 216 Coenzyme A.
Binding site: 260 260 Coenzyme A.
Binding site: 281 281 Coenzyme A.
Modified residue: 63 63 N6-acetyllysine; alternate.
Modified residue: 63 63 N6-succinyllysine; alternate.
Modified residue: 75 75 N6-succinyllysine.
Modified residue: 171 171 N6-acetyllysine; alternate.
Modified residue: 171 171 N6-succinyllysine; alternate.
Modified residue: 178 178 N6-acetyllysine; alternate.
Modified residue: 178 178 N6-succinyllysine; alternate.
Modified residue: 187 187 N6-acetyllysine; alternate.
Modified residue: 187 187 N6-succinyllysine; alternate.
Modified residue: 199 199 N6-acetyllysine; alternate.
Modified residue: 199 199 N6-succinyllysine; alternate.
Modified residue: 220 220 N6-acetyllysine; alternate.
Modified residue: 220 220 N6-succinyllysine; alternate.
Modified residue: 227 227 N6-acetyllysine; alternate.
Modified residue: 227 227 N6-succinyllysine; alternate.
Modified residue: 240 240 N6-succinyllysine.
Modified residue: 242 242 N6-acetyllysine; alternate.
Modified residue: 242 242 N6-succinyllysine; alternate.
Modified residue: 248 248 N6-acetyllysine.
Modified residue: 254 254 N6-acetyllysine.
Modified residue: 260 260 N6-acetyllysine; alternate.
Modified residue: 260 260 N6-succinyllysine; alternate.
Modified residue: 263 263 N6-succinyllysine.
Modified residue: 265 265 N6-succinyllysine.
Modified residue: 270 270 N6-acetyllysine.
Modified residue: 335 335 N6-acetyllysine.
Protein Length
424 AA.
Protein Sequence
(Canonical)
MAALVALHGV VRRPLLRGLL QEVRCLERSY ASKPTLNEVV IVSAIRTPIG SFLGSLASQP  60
ATKLGTAAIQ GAIEKAGIPK EEVKEVYMGN VIQGGEGQAP TRQATLGAGL PISTPCTTVN  120
KVCASGMKAI MMASQSLMCG HQDVMVAGGM ESMSNVPYVM SRGATPYGGV KLEDLIVKDG  180
LTDVYNKIHM GNCAENTAKK MNISRQEQDT YALSSYTRSK EAWDAGKFAS EITPITISVK  240
GKPDVVVKED EEYKRVDFSK VPKLKTVFQK ENGTITAANA STLNDGAAAL VLMTAEAAQR  300
LNVKPLARIA AFADAAVDPI DFPLAPAYAV PKVLKYAGLK KEDIAMWEVN EAFSVVVLAN  360
IKMLEIDPQK VNIHGGAVSL GHPIGMSGAR IVVHMAHALK PGEFGLASIC NGGGGASALL  420
IEKL                                                               424
FASTA
(Canonical)
>LipidDB-10090-00312|Q8QZT1
MAALVALHGVVRRPLLRGLLQEVRCLERSYASKPTLNEVVIVSAIRTPIGSFLGSLASQP
ATKLGTAAIQGAIEKAGIPKEEVKEVYMGNVIQGGEGQAPTRQATLGAGLPISTPCTTVN
KVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMSRGATPYGGVKLEDLIVKDG
LTDVYNKIHMGNCAENTAKKMNISRQEQDTYALSSYTRSKEAWDAGKFASEITPITISVK
GKPDVVVKEDEEYKRVDFSKVPKLKTVFQKENGTITAANASTLNDGAAALVLMTAEAAQR
LNVKPLARIAAFADAAVDPIDFPLAPAYAVPKVLKYAGLKKEDIAMWEVNEAFSVVVLAN
IKMLEIDPQKVNIHGGAVSLGHPIGMSGARIVVHMAHALKPGEFGLASICNGGGGASALL
IEKL
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005743; C:mitochondrial inner membrane; IDA:MGI
GO:0005759; C:mitochondrial matrix; IEA:Ensembl
GO:0005739; C:mitochondrion; IDA:MGI
GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:MGI
GO:0050662; F:coenzyme binding; IEA:Ensembl
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0060612; P:adipose tissue development; IEA:Ensembl
GO:0007420; P:brain development; IEA:Ensembl
GO:0001889; P:liver development; IEA:Ensembl
GO:0072229; P:metanephric proximal convoluted tubule development; IEA:Ensembl
GO:0051260; P:protein homooligomerization; IEA:Ensembl
GO:0009725; P:response to hormone; IEA:Ensembl
GO:0014070; P:response to organic cyclic compound; IEA:Ensembl
GO:0042594; P:response to starvation; IEA:Ensembl
Interpro
InterPro; IPR002155; Thiolase
InterPro; IPR016039; Thiolase-like
InterPro; IPR016038; Thiolase-like_subgr
InterPro; IPR020615; Thiolase_acyl_enz_int_AS
InterPro; IPR020610; Thiolase_AS
InterPro; IPR020617; Thiolase_C
InterPro; IPR020613; Thiolase_CS
InterPro; IPR020616; Thiolase_N
Pfam
Pfam; PF02803; Thiolase_C;
Pfam; PF00108; Thiolase_N;
SMART
PROSITE
PROSITE; PS00098; THIOLASE_1;
PROSITE; PS00737; THIOLASE_2;
PROSITE; PS00099; THIOLASE_3;
PRINTS