Acyl-CoA binding protein superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: All alpha proteins [ 46456] (258)
• Fold: Acyl-CoA binding protein-like [ 47026] (2)
  • core: 3 helices; bundle, closed, left-handed twist; up-and-down
• Superfamily: Acyl-CoA binding protein [ 47027]
• Families: Acyl-CoA binding protein [ 47028]

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Superfamily statistics

	Genomes (332)	UniProt 15.0	PDB chains (SCOP 1.73)
Domains	1,278	743	2
Proteins	1,273	740	2

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Functional annotation

• General category: Metabolism
• Detailed category: Lipid metabolism and transport

Function annotation of SCOP domain superfamilies

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InterPro annotation

• Cross references: IPR000582 SSF47027 Protein matches
• Abstract:

  Acyl-CoA-binding protein (ACBP) is a small (10 Kd) protein that binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters [1454809]. ACBP is also known as diazepam binding inhibitor (DBI) or endozepine (EP) because of its ability to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor [1649940].

  ACBP is a highly conserved protein of about 90 residues that is found in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and in some eubacterial species [16018771].

  Although ACBP occurs as a completely independent protein, intact ACB domains have been identified in a number of large, multifunctional proteins in a variety of eukaryotic species. These include large membrane-associated proteins with N-terminal ACB domains, multifunctional enzymes with both ACB and peroxisomal enoyl-CoA Delta(3), Delta(2)-enoyl-CoA isomerase domains, and proteins with both an ACB domain and ankyrin repeats [16018771].

  The ACB domain consists of four alpha-helices arranged in a bowl shape with a highly exposed acyl-CoA-binding site. The ligand is bound through specific interactions with residues on the protein, most notably several conserved positive charges that interact with the phosphate group on the adenosine-3'phosphate moiety, and the acyl chain is sandwiched between the hydrophobic surfaces of CoA and the protein [11491287].

  Other proteins containing an ACB domain include:

  • Endozepine-like peptide (ELP) (gene DBIL5) from mouse [8898349]. ELP is a testis- specific ACBP homolog that may be involved in the energy metabolism of the mature sperm.
  • MA-DBI, a transmembrane protein of unknown function which has been found in mammals. MA-DBI contains a N-terminal ACB domain.
  • DRS-1 [10354522], a human protein of unknown function that contains a N-terminal ACB domain and a C-terminal enoyl-CoA isomerase/hydratase domain.

InterPro database

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