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InterPro: IPR017659 Formyl-CoA transferase

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UniProtKB

Matches:

161 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
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Accession

IPR017659 Formyl-CoA_transferase

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR03253	oxalate_frc	161
Signatures in BioMart

InterPro Relationships Help

Parent

IPR003673 CoA-transferase family III

GO Term annotation Help

Process

GO:0008152 metabolic process

Function

GO:0033608 formyl-CoA transferase activity

InterPro annotation

Entry Details in BioMart

Abstract

Formyl-CoA transferase, transfers coenzyme A from formyl-CoA to oxalate. It forms a pathway, together with oxalyl-CoA decarboxylase, for oxalate degradation; decarboxylation by the latter gene regenerates formyl-CoA. The two enzymes typically are encoded by a two-gene operon [1].

Structural links Help

PDB - click here

SCOP: c.123.1.1

Database links Help

Enzyme: EC:2.8.3.16

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR017659

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O06644 Formyl-coenzyme A transferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003673	CoA-transferase family III
IPR017659	Formyl-CoA transferase
	PDB Chain
	ModBase
	SCOP Domain

Publications Open in usermanual
1.	Azcarate-Peril MA, Bruno-Barcena JM, Hassan HM, Klaenhammer TR. Transcriptional and functional analysis of oxalyl-coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes from Lactobacillus acidophilus. Appl. Environ. Microbiol. 72 1891-9 2006 [PubMed: 16517636] http://dx.doi.org/10.1128/AEM.72.3.1891-1899.2006

Additional Reading Open in usermanual
	Gruez A, Roig-Zamboni V, Valencia C, Campanacci V, Cambillau C. The crystal structure of the Escherichia coli YfdW gene product reveals a new fold of two interlaced rings identifying a wide family of CoA transferases. J. Biol. Chem. 278 2003 34582-6 [PubMed: 12844490] http://dx.doi.org/10.1074/jbc.C300282200
	Jonsson S, Ricagno S, Lindqvist Y, Richards NG. Kinetic and mechanistic characterization of the formyl-CoA transferase from Oxalobacter formigenes. J. Biol. Chem. 279 2004 36003-12 [PubMed: 15213226] http://dx.doi.org/10.1074/jbc.M404873200
	Berthold CL, Toyota CG, Richards NG, Lindqvist Y. Reinvestigation of the catalytic mechanism of formyl-CoA transferase, a class III CoA-transferase. J. Biol. Chem. 283 2008 6519-29 [PubMed: 18162462] http://dx.doi.org/10.1074/jbc.M709353200
	Gogos A, Gorman J, Shapiro L. Structure of Escherichia coli YfdW, a type III CoA transferase. Acta Crystallogr. D Biol. Crystallogr. 60 2004 507-11 [PubMed: 14993676] http://dx.doi.org/10.1107/S0907444904000034
	Ricagno S, Jonsson S, Richards N, Lindqvist Y. Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer. EMBO J. 22 2003 3210-9 [PubMed: 12839984] http://dx.doi.org/10.1093/emboj/cdg333

InterPro 23.1