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InterPro: IPR000362 Fumarate lyase

Protein matchesHelp
UniProtKB
Matches:
6524 proteins
AccessionHelp IPR000362 Fumarate_lyase
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR008948 L-Aspartase-like
Children IPR003031 Delta crystallin
Found in IPR004708 Aspartate ammonia-lyase
IPR004769 Adenylosuccinate lyase
IPR005677 Fumarate hydratase, class II
IPR011244 Bifunctional argininosuccinate lyase/acetyltransferase
IPR012789 3-carboxy-cis,cis-muconate cycloisomerase
Contains IPR020557 Fumarate lyase, conserved site
GO Term annotationHelp
Function GO:0003824 catalytic activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

A number of enzymes, belonging to the lyase class, for which fumarate is a substrate, have been shown to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes [1, 2]. The following are examples of members of this family:

  • P32427: 3-carboxymuconate lactonizing enzyme, EC:5.5.1.2 (3-carboxy-cis,cis-muconate cycloisomerase), an enzyme involved in aromatic acids catabolism [3].
  • P24057: Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase, showing that it is an example of a 'hijacked' enzyme - accumulated mutations have, however, rendered the protein enzymatically inactive.
  • P05042: Class I Fumarase enzyme, EC:4.2.1.2 (fumarate hydratase), which catalyses the reversible hydration of fumarate to L-malate. Class I enzymes are thermolabile dimeric enzymes (as for example: Escherichia coli fumC).
  • P04424: Arginosuccinase, EC:4.3.2.1 (argininosuccinate lyase), which catalyses the formation of arginine and fumarate from argininosuccinate, the last step in the biosynthesis of arginine.
  • P04422: Aspartate ammonia-lyase, EC:4.3.1.1 (aspartase), which catalyses the reversible conversion of aspartate to fumarate and ammonia. This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans-elimination reaction.
  • P00923: class II Fumarase enzyme, EC:4.2.1.2, are thermostable and tetrameric and are found in prokaryotes (as for example: E. coli fumA and fumB) as well as in eukaryotes. The sequence of the two classes of fumarases are not closely related.
  • P25739: Adenylosuccinase, EC:4.3.2.2 (adenylosuccinate lyase) [4], which catalyses the eighth step in the de novo biosynthesis of purines, the formation of 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide and fumarate from 1-(5-phosphoribosyl)-4-(N-succino-carboxamide). That enzyme can also catalyse the formation of fumarate and AMP from adenylosuccinate.

Structural linksHelp
SCOP: a.127.1.1
Database linksHelp
PDBe-motif: PS00163
Enzyme: EC:4.3.2
PROSITE doc: PDOC00147
PANDIT: PF00206
Blocks: IPB000362

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR000362 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P04424 Argininosuccinate lyase

P08417 Fumarate hydratase, mitochondrial

P54822 Adenylosuccinate lyase

P93033 Fumarate hydratase 1, mitochondrial

Q21774 Adenylosuccinate lyase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR019468 Adenylosuccinate lyase, C-terminal
IPR020557 Fumarate lyase, conserved site
IPR003031 Delta crystallin
IPR008948 L-Aspartase-like
IPR018951 Fumarase C, C-terminal
IPR004769 Adenylosuccinate lyase
IPR000362 Fumarate lyase
IPR005677 Fumarate hydratase, class II
IPR009049 Argininosuccinate lyase
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Woods SA, Schwartzbach SD, Guest JR.
Two biochemically distinct classes of fumarase in Escherichia coli.
Biochim. Biophys. Acta 954 14-26 1988 [PubMed: 3282546]
2. Guest JR, Woods SA, Miles JS.
Sequence homologies between arginosuccinase, aspartase and fumarase - a family of strycturally related enzymes.
FEMS Microbiol. Lett. 51 181-6 1988
3. Williams SE, Woolridge EM, Ransom SC, Landro JA, Babbitt PC, Kozarich JW.
3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif.
Biochemistry 31 9768-76 1992 [PubMed: 1390752]
http://dx.doi.org/10.1021/bi00155a033
4. Zalkin H, Dixon JE.
De novo purine nucleotide biosynthesis.
Prog. Nucleic Acid Res. Mol. Biol. 42 259-87 1992 [PubMed: 1574589]

Additional ReadingHelp
Sampaleanu LM, Codding PW, Lobsanov YD, Tsai M, Smith GD, Horvatin C, Howell PL.
Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis.
Biochem. J. 384 2004 437-47 [PubMed: 15320872]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=15320872&action=stream&blobtype=pdf
Simpson A, Bateman O, Driessen H, Lindley P, Moss D, Mylvaganam S, Narebor E, Slingsby C.
The structure of avian eye lens delta-crystallin reveals a new fold for a superfamily of oligomeric enzymes.
Nat. Struct. Biol. 1 1994 724-34 [PubMed: 7634077]
http://dx.doi.org/10.1038/nsb1094-724
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
Yang J, Wang Y, Woolridge EM, Arora V, Petsko GA, Kozarich JW, Ringe D.
Crystal structure of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: enzyme evolution in parallel pathways.
Biochemistry 43 2004 10424-34 [PubMed: 15301541]
http://dx.doi.org/10.1021/bi036205c
Bhaumik P, Koski MK, Bergmann U, Wierenga RK.
Structure determination and refinement at 2.44 A resolution of argininosuccinate lyase from Escherichia coli.
Acta Crystallogr. D Biol. Crystallogr. 60 2004 1964-70 [PubMed: 15502303]
http://dx.doi.org/10.1107/S0907444904021912
Rath VL, Fletterick RJ.
Parallel evolution in two homologues of phosphorylase.
Nat. Struct. Biol. 1 1994 681-90 [PubMed: 7634071]
http://dx.doi.org/10.1038/nsb1094-681
Lee HJ, Lai YH, Wu SY, Chen YH.
The effect of N-terminal truncation on double-dimer assembly of goose delta-crystallin.
Biochem. J. 392 2005 545-54 [PubMed: 16101585]
http://dx.doi.org/10.1042/BJ20050860

Real and artificial histories.
Nat. Struct. Biol. 1 1994 655-6 [PubMed: 7543359]
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InterPro 23.1