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IPR020557 is a Fumarate lyase, conserved site.
<p>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 [[cite:PUB00000586]]. The following are examples of members of this family:</p> <ul> <li>[swissprot:P32427]: 3-carboxymuconate lactonizing enzyme, [ec:5.5.1.2] (3-carboxy-cis,cis-muconate cycloisomerase), an enzyme involved in aromatic acids catabolism [[cite:PUB00000374]].</li> <li>[swissprot: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.</li> <li>[swissprot: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).</li> <li>[swissprot: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.</li> <li>[swissprot: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.</li> <li>[swissprot: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.</li> <li>[swissprot:P25739]: Adenylosuccinase, [ec:4.3.2.2] (adenylosuccinate lyase) [[cite:PUB00004940]], 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.</li> <li>[swissprot:A0A0U2UYC4]: Trans-aconitate decarboxylase 1, which decarboxylates trans-aconitate, an intermediate in the biosynthesis of itaconic acid and 2-hydroxyparaconate [[cite:PUB00083219], [cite:PUB00083220]].</li> </ul> <p>This signature contains the conserved methionine which is probably involved in the catalytic activity.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Catalytic activity | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | Argininosuccinate lyase [Medicago truncatula] gi|357465245|ref|XP_003602904.1| | 18 | ||
| – | PREDICTED: argininosuccinate lyase-like [Glycine max] gi|356508027|ref|XP_003522764.1| | 27 | ||
| – | PREDICTED: adenylosuccinate lyase-like [Glycine max] gi|356501123|ref|XP_003519378.1| | 19 | ||
| – | PREDICTED: fumarate hydratase 1, mitochondrial-like [Glycine max] gi|356500262|ref|XP_003518952.1| | 26 | ||
| – | Adenylosuccinate lyase; TAIR: AT1G36280.1 L-Aspartase-like family protein; Swiss-Prot: sp|P44797|PUR8_HAEIN Adenylosuccinate lyase; TrEMBL-Plants: tr|V7B898|V7B898_PHAVU Adenylosuccinate lyase; Found in the gene: LotjaGi1g1v0081500 | 19 | ||
| – | Argininosuccinate lyase; TAIR: AT5G10920.1 L-Aspartase-like family protein; Swiss-Prot: sp|Q9LEU8|ARLY_ARATH Argininosuccinate lyase, chloroplastic; TrEMBL-Plants: tr|I1JV68|I1JV68_SOYBN Uncharacterized protein; Found in the gene: LotjaGi1g1v0346000 | 26 | ||
| – | Fumarate hydratase, class II; TAIR: AT2G47510.1 fumarase 1; Swiss-Prot: sp|P93033|FUM1_ARATH Fumarate hydratase 1, mitochondrial; TrEMBL-Plants: tr|V7BJH7|V7BJH7_PHAVU Uncharacterized protein; Found in the gene: LotjaGi5g1v0248000 | 26 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| cd01362 | CDD | 1 | 14.29 |