1NDI

Carnitine Acetyltransferase in complex with CoA

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ndia2	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	Choline/Carnitine O-acyltransferase	Carnitine acetyltransferase, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d1ndia1	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	Choline/Carnitine O-acyltransferase	Carnitine acetyltransferase, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1ndib2	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	Choline/Carnitine O-acyltransferase	Carnitine acetyltransferase, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1ndib1	Alpha and beta proteins (a/b)	CoA-dependent acyltransferases	CoA-dependent acyltransferases	Choline/Carnitine O-acyltransferase	Carnitine acetyltransferase, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	CoA-dependent acyltransferases	8043752	3000272	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	CoA-dependent acyltransferases	8043754	3000272	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	CoA-dependent acyltransferases	8043752	3000272	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	CoA-dependent acyltransferases	8043754	3000272	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Carn_acyltransf_2nd	e1ndiA2	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Carn_acyltransf_2nd	ECOD (1.6)
A	Carn_acyltransf_1st	e1ndiA1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Carn_acyltransf_1st	ECOD (1.6)
B	Carn_acyltransf_2nd	e1ndiB2	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Carn_acyltransf_2nd	ECOD (1.6)
B	Carn_acyltransf_1st	e1ndiB1	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Carn_acyltransf_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
A	3.30.559.70	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Choline/Carnitine o-acyltransferase, domain 2	CATH (4.3.0)
B	3.30.559.10	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Chloramphenicol acetyltransferase-like domain	CATH (4.3.0)
B	3.30.559.70	Alpha Beta	2-Layer Sandwich	Chloramphenicol Acetyltransferase	Choline/Carnitine o-acyltransferase, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00755	Choline/Carnitine o-acyltransferase (Carn_acyltransf)	Choline/Carnitine o-acyltransferase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Carnitine Acetyltransferase	oxidoreductase activity acyl-CoA oxidase activity oxidoreductase activity, acting on the CH-CH group of donors catalytic activity oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor O-acyltransferase activity acyltransferase activity carnitine O-acyltransferase activity carnitine O-octanoyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity carnitine O-acetyltransferase activity acetyltransferase activity O-acetyltransferase activity	catabolic process oxoacid metabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process fatty acid beta-oxidation using acyl-CoA oxidase monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation small molecule metabolic process lipid oxidation fatty acid metabolic process lipid catabolic process catabolic process oxoacid metabolic process organic acid metabolic process organic acid catabolic process cellular catabolic process fatty acid beta-oxidation using acyl-CoA oxidase monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation small molecule metabolic process lipid oxidation fatty acid metabolic process lipid catabolic process carboxylic acid metabolic process primary metabolic process lipid modification fatty acid catabolic process metabolic process cellular process monocarboxylic acid metabolic process small molecule catabolic process lipid metabolic process carnitine metabolic process modified amino acid metabolic process carnitine metabolic process, CoA-linked amino-acid betaine metabolic process medium-chain fatty acid metabolic process short-chain fatty acid metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle mitochondrial membrane organelle inner membrane membrane mitochondrial inner membrane organelle envelope mitochondrial envelope organelle membrane peroxisome microbody endoplasmic reticulum endomembrane system

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000542	Acyltransferase ChoActase/COT/CPT	Family
A, B	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily	Homologous Superfamily
A, B	IPR039551	Choline/carnitine acyltransferase domain	Domain
A, B	IPR042231	Choline/Carnitine o-acyltransferase, domain 2	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	carnitine O-acetyltransferase M-CSA #629	Carnitine acetyltransferase (CrAT) belongs to the family of choline/carnitine acyltransferases, which catalyse the exchange between acyl-CoA and acylcarnitine (likewise with choline). The enzymes of this family are classified based on their substrate selectivity. CrAT prefers short-chain fatty acids. CrAT maybe involved in the transport of acetyl-CoA across intercellular membranes, in maintaining the acetyl-CoA:CoA balance and in the excretion of excess or harmful acyl molecules as acylcarnitines. Inherited deficiency of CrAT activity can lead to serious neurological and heart problems, and patients suffering from Alzhiemer's disease also have reduced CrAT activity.	Defined by 4 residues: TYR:A-78 [auth A-107]PRO:A-91 [auth A-120]HIS:A-314 [auth A-343]SER:A-525 [auth A-554] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.3.1.7 (PDB Primary Data) Search M-CSA Motif + EC 2.3.1.7 EC: 2.3.1.137 (UniProt) Search M-CSA Motif + EC 2.3.1.137

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.