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357  structures 8560  species 0  interactions 32580  sequences 182  architectures

Family: Lyase_1 (PF00206)

Summary: Lyase

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This is the Wikipedia entry entitled "Fumarate lyase". More...

Fumarate lyase Edit Wikipedia article

Symbol Lyase_1
Pfam PF00206
InterPro IPR000362
SCOP 1jsw
CDD cd01362

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:

  • 3-carboxymuconate lactonizing enzyme, EC (3-carboxy-cis,cis-muconate cycloisomerase), an enzyme involved in aromatic acids catabolism.[3]
  • 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.
  • Class I Fumarase enzyme, EC (fumarate hydratase), which catalyzes the reversible hydration of fumarate to L-malate. Class I enzymes are thermolabile dimeric enzymes (as for example: Escherichia coli fumA and fumB).
  • Arginosuccinase, EC (argininosuccinate lyase), which catalyzes the formation of arginine and fumarate from argininosuccinate, the last step in the biosynthesis of arginine.
  • Aspartate ammonia-lyase, EC (aspartase), which catalyzes 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.
  • class II Fumarase enzyme, EC, are thermostable and tetrameric and are found in prokaryotes (as for example: Escherichia coli fumC) as well as in eukaryotes. The sequence of the two classes of fumarases are not closely related.
  • Adenylosuccinase, EC (adenylosuccinate lyase),[4] which catalyzes 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 catalyze the formation of fumarate and AMP from adenylosuccinate.


  1. ^ Guest JR, Woods SA, Schwartzbach SD (1988). "Two biochemically distinct classes of fumarase in Escherichia coli". Biochim. Biophys. Acta. 954 (1): 14–26. doi:10.1016/0167-4838(88)90050-7. PMID 3282546. 
  2. ^ Guest JR, Woods SA, Miles JS (1988). "Sequence homologies between arginosuccinase, aspartase and fumarase - a family of strycturally related enzymes". FEMS Microbiol. Lett. 51: 181–186. doi:10.1111/j.1574-6968.1988.tb02994.x. 
  3. ^ Babbitt PC, Ransom SC, Williams SE, Woolridge EM, Landro JA, Kozarich JW (1992). "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 (40): 9768–9776. doi:10.1021/bi00155a033. PMID 1390752. 
  4. ^ Dixon JE, Zalkin H (1992). "De novo purine nucleotide biosynthesis". Prog. Nucleic Acid Res. Mol. Biol. 42: 259–287. doi:10.1016/s0079-6603(08)60578-4. PMID 1574589. 

This article incorporates text from the public domain Pfam and InterPro IPR000362

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Lyase Provide feedback

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This tab holds annotation information from the InterPro database.

InterPro entry IPR022761

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 [ PUBMED:3282546 ]. This entry represents the N-terminal region of fumarate lyase family.

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Seed source: Prosite
Previous IDs: lyase_1;
Type: Domain
Sequence Ontology: SO:0000417
Author: Finn RD
Number in seed: 16
Number in full: 32580
Average length of the domain: 295.10 aa
Average identity of full alignment: 25 %
Average coverage of the sequence by the domain: 64.54 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.7 20.7
Trusted cut-off 20.8 20.7
Noise cut-off 20.6 20.6
Model length: 312
Family (HMM) version: 22
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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Lyase_1 domain has been found. There are 357 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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