Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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CoA_binding CoA binding domain

SMART accession number:	SM00881
Description:	This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
Interpro abstract (IPR003781):	This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.
GO function:	cofactor binding (GO:0048037)
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 3632 CoA_binding domains in 3632 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a CoA_binding domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with CoA_binding domain is also avaliable.

  Useful shortcuts: Expand all nodes or Collapse tree
  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Wolodko WT, Fraser ME, James MN, Bridger WA
  • The crystal structure of succinyl-CoA synthetase from Escherichia coli at2.5-A resolution.
  • J Biol Chem. 1994; 269: 10883-90
  • Display abstract

  • The x-ray crystal structure of succinyl-CoA synthetase (SCS) fromEscherichia coli has been determined by the method of multiple isomorphousreplacement to a resolution of 2.5 A. Crystals of SCS are tetragonal witha space group of P4(3)22 and unit cell dimensions of a = b = 98.47 A and c= 400.6 A. One molecule of SCS (142 kDa) is contained in the asymmetricunit. The current model has been refined to a conventional R factor of21.6% with root mean square deviations from ideal stereochemistry of 0.022A for bond lengths and 3.25 degrees for bond angles. The quaternaryorganization of the E. coli enzyme is an alpha 2 beta 2 heterotetramer. Inthis tetramer, the alpha-subunits interact only with the beta-subunits,whereas the beta-subunits interact to form the dimer of alpha beta-dimers.The two active site pockets are located at regions of contact betweenalpha- and beta-subunits. One molecule of coenzyme A is bound to eachalpha-subunit at a typical nucleotide-binding motif, and His-246 of eachalpha-subunit is phosphorylated. This phosphohistidine, a catalyticintermediate, is stabilized by two helix dipoles (the "power" helices),one from each of the two subunit types. A short segment of thebeta-subunit from one alpha beta-dimer is in close proximity to theCoA-binding site of the other alpha beta-dimer, providing a possiblerationale for the overall tetrameric structure.

• Structure (3D structures containing this domain)

• 3D Structures of CoA_binding domains in PDB

  PDB code	Main view	Title
  1cqi		Crystal structure of the complex of adp and mg2+ with dephosphorylated e. coli succinyl-coa synthetase
  1cqj		Crystal structure of dephosphorylated e. coli succinyl-coa synthetase
  1euc		Crystal structure of dephosphorylated pig heart, gtp- specific succinyl-coa synthetase
  1eud		Crystal structure of phosphorylated pig heart, gtp-specific succinyl-coa synthetase
  1iuk		The structure of native id.343 from thermus thermophilus
  1iul		The structure of cell-free id.343 from thermus thermophilus
  1jkj		E. coli scs
  1jll		Crystal structure analysis of the e197betaa mutant of e. coli scs
  1oi7		The crystal structure of succinyl-coa synthetase alpha subunit from thermus thermophilus
  1scu		The crystal structure of succinyl-coa synthetase from escherichia coli at 2.5 angstroms resolution
  1xcb		X-ray structure of a rex-family repressor/nadh complex from thermus aquaticus
  1y81		Conserved hypothetical protein pfu-723267-001 from pyrococcus furiosus
  2csu		Crystal structure of ph0766 from pyrococcus horikoshii ot3
  2d59		Hypothetical protein from pyrococcus horikoshii ot3
  2d5a		Hypothetical protein from pyrococcus horikoshii ot3
  2dt5		Crystal structure of ttha1657 (at-rich dna-binding protein) from thermus thermophilus hb8
  2duw		Solution structure of putative coa-binding protein of klebsiella pneumoniae
  2e6u		Crystal structure of hypothetical protein ph1109 from pyrococcus horikoshii
  2fp4		Crystal structure of pig gtp-specific succinyl-coa synthetase in complex with gtp
  2fpg		Crystal structure of pig gtp-specific succinyl-coa synthetase in complex with gdp
  2fpi		Crystal structure of pig gtp-specific succinyl-coa synthetase from polyethylene glycol
  2fpp		Crystal structure of pig gtp-specific succinyl-coa synthetase from polyethylene glycol with chloride ions
  2nu6		C123aa mutant of e. coli succinyl-coa synthetase
  2nu7		C123as mutant of e. coli succinyl-coa synthetase
  2nu8		C123at mutant of e. coli succinyl-coa synthetase
  2nu9		C123at mutant of e. coli succinyl-coa synthetase orthorhombic crystal form
  2nua		C123av mutant of e. coli succinyl-coa synthetase
  2scu		A detailed description of the structure of succinyl-coa synthetase from escherichia coli
  2vt2		Structure and functional properties of the bacillus subtilis transcriptional repressor rex
  2vt3		Structure and functional properties of the bacillus subtilis transcriptional repressor rex
  2yv1		Crystal structure of succinyl-coa synthetase alpha chain from methanocaldococcus jannaschii dsm 2661
  2yv2		Crystal structure of succinyl-coa synthetase alpha chain from aeropyrum pernix k1

• Links (links to other resources describing this domain)

• PFAM	CoA_binding
  INTERPRO	IPR003781

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