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InterPro: IPR018951 Fumarase C, C-terminal

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UniProtKB

Matches:

2266 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR018951 Fumarase_C_C

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF10415	FumaraseC_C	2266
Signatures in BioMart

InterPro Relationships Help

Found in

IPR004708 Aspartate ammonia-lyase
IPR005677 Fumarate hydratase, class II
IPR008948 L-Aspartase-like

GO Term annotation Help

Process

GO:0006099 tricarboxylic acid cycle

Function

GO:0016829 lyase activity

InterPro annotation

Entry Details in BioMart

Abstract

Fumarase C catalyses the stereo-specific interconversion of fumarate to L-malate as part of the Krebs cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit [1]. This entry does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.

Structural links Help

PDB - click here

SCOP: a.127.1.1

CATH: 1.10.40.30

Database links Help

Enzyme: EC:4.2.1.2

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018951

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O17214 Probable fumarate hydratase, mitochondrial

P07954 Fumarate hydratase, mitochondrial

P08417 Fumarate hydratase, mitochondrial

P93033 Fumarate hydratase 1, mitochondrial

P97807 Fumarate hydratase, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018951	Fumarase C, C-terminal
IPR000362	Fumarate lyase
IPR005677	Fumarate hydratase, class II
IPR020557	Fumarate lyase, conserved site
IPR003031	Delta crystallin
IPR008948	L-Aspartase-like
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Weaver T, Banaszak L. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry 35 13955-65 1996 [PubMed: 8909293] http://dx.doi.org/10.1021/bi9614702

Additional Reading Open in usermanual
	Weaver T, Lees M, Zaitsev V, Zaitseva I, Duke E, Lindley P, McSweeny S, Svensson A, Keruchenko J, Keruchenko I, Gladilin K, Banaszak L. Crystal structures of native and recombinant yeast fumarase. J. Mol. Biol. 280 1998 431-42 [PubMed: 9665847] http://dx.doi.org/10.1006/jmbi.1998.1862
	Shi W, Dunbar J, Jayasekera MM, Viola RE, Farber GK. The structure of L-aspartate ammonia-lyase from Escherichia coli. Biochemistry 36 1997 9136-44 [PubMed: 9230045] http://dx.doi.org/10.1021/bi9704515
	Estevez M, Skarda J, Spencer J, Banaszak L, Weaver TM. X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation. Protein Sci. 11 2002 1552-7 [PubMed: 12021453] http://dx.doi.org/10.1110/ps.0201502
	Weaver T. Structure of free fumarase C from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 61 2005 1395-401 [PubMed: 16204892] http://dx.doi.org/10.1107/S0907444905024194
	Fujii T, Sakai H, Kawata Y, Hata Y. Crystal structure of thermostable aspartase from Bacillus sp. YM55-1: structure-based exploration of functional sites in the aspartase family. J. Mol. Biol. 328 2003 635-54 [PubMed: 12706722] http://dx.doi.org/10.1016/S0022-2836(03)00310-3

InterPro 23.1