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InterPro: IPR012805 Acetyl-CoA C-acyltransferase FadA

Protein matches Help

UniProtKB

Matches:

273 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
Architectures
Accession List
Matches in BioMart

Accession

IPR012805 FadA

Type

Family

Signatures Help

Database	ID	Name	Proteins
HAMAP	MF_01620	FadA	226
TIGRFAMs	TIGR02445	fadA	273
Signatures in BioMart

InterPro Relationships Help

Parent

IPR002155 Thiolase

Contains

IPR016038 Thiolase-like, subgroup
IPR020610 Thiolase, active site
IPR020613 Thiolase, conserved site
IPR020615 Thiolase, acyl-enzyme intermediate active site
IPR020616 Thiolase, N-terminal
IPR020617 Thiolase, C-terminal

GO Term annotation Help

Process

GO:0006631 fatty acid metabolic process
GO:0016042 lipid catabolic process

Function

GO:0003988 acetyl-CoA C-acyltransferase activity

Component

GO:0005737 cytoplasm

InterPro annotation

Entry Details in BioMart

Abstract

This subunit of the FadBA complex has acetyl-CoA C-acyltransferase (EC:2.3.1.16) activity, and is also known as beta-ketothiolase and fatty oxidation complex, beta subunit. This protein is almost always located adjacent to FadB (IPR012799). The FadBA complex is the major complex active for beta-oxidation of fatty acids in Escherichia coli.

Structural links Help

PDB - click here

SCOP: c.95.1.1

Database links Help

Enzyme: EC:2.3.1.16

CluSTr: ALLvsALL:36768:119.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012805

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0A2H7 3-ketoacyl-CoA thiolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020610	Thiolase, active site
IPR020613	Thiolase, conserved site
IPR002155	Thiolase
IPR020615	Thiolase, acyl-enzyme intermediate active site
IPR020616	Thiolase, N-terminal
IPR020617	Thiolase, C-terminal
IPR016039	Thiolase-like
IPR012805	Acetyl-CoA C-acyltransferase FadA
IPR016038	Thiolase-like, subgroup
	PDB Chain
	ModBase

Publications Help

Additional Reading Open in usermanual
	Yang SY, Yang XY, Healy-Louie G, Schulz H, Elzinga M. Nucleotide sequence of the fadA gene. Primary structure of 3-ketoacyl-coenzyme A thiolase from Escherichia coli and the structural organization of the fadAB operon. J. Biol. Chem. 265 1990 10424-9 [PubMed: 2191949] http://intl.jbc.org/cgi/content/abstract/265/18/10424
	Ishikawa M, Mikami Y, Usukura J, Iwasaki H, Shinagawa H, Morikawa K. Reconstitution, morphology and crystallization of a fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi. Biochem. J. 328 ( Pt 3) 1997 815-20 [PubMed: 9396725]
	Tsuchiya D, Shimizu N, Ishikawa M, Suzuki Y, Morikawa K. Ligand-induced domain rearrangement of fatty acid beta-oxidation multienzyme complex. Structure 14 2006 237-46 [PubMed: 16472743] http://dx.doi.org/10.1016/j.str.2005.10.011
	Ishikawa M, Tsuchiya D, Oyama T, Tsunaka Y, Morikawa K. Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex. EMBO J. 23 2004 2745-54 [PubMed: 15229654] http://dx.doi.org/10.1038/sj.emboj.7600298

InterPro 23.1