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0FUMH_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionFumarate hydratase, mitochondrial precursor (ec (fumarase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (TAS)
0004333 fumarate hydratase activity (TAS)
0006106 fumarate metabolism (TAS)

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Domain Architecture (Details)
InterPro domains unassigned to SynO:
A number of enzymes.elonging to the lyase class.or which fumarate is asubstrate.ave been shown to share a short conserved sequence around amethionine which is probably involved in the catalytic activity of this typeof enzymes . The following are examples of members of this family: P32427 (PCAB_PSEPU): 3-carboxymuconate lactonizing cycloisomerase).n enzyme involved in aromatic acids catabolism . P24057 (CRD1_ANAPL): Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase.howing that it is an example of a hijacked enzyme - accumulated mutations have.owever.endered the protein enzymatically inactive. P05042 (FUMC_ECOLI): Class I Fumarase enzyme.fumarate hydratase).hich catalyzes the reversible hydration of fumarate to L-malate. Class I enzymes are thermolabile dimeric enzymes (as for example: Escherichia coli fumC). P04424 (ARLY_HUMAN): Arginosuccinase.argininosuccinate lyase).hich catalyzes the formation of arginine and fumarate from argininosuccinate.he last step in the biosynthesis of arginine. P04422 (ASPA_ECOLI): Aspartate ammonia-lyase.aspartase).hich catalyzes the reversible conversion of aspartate to fumarate and ammonia. This reaction is analogous to that catalyzed by fumarase.xcept that ammonia rather than water is involved in the trans-elimination reaction. P00923 (FUMA_ECOLI): class II Fumarase enzyme are thermostable and tetrameric and are found in prokaryotes (as for example: Escherichia coli fumA and fumB) as well as in eukaryotes. The sequence of the two classes of fumarases are not closely related. P25739 (PUR8_ECOLI): Adenylosuccinase.adenylosuccinate lyase) .hich catalyzes the eighth step in the de novo biosynthesis of purines.he 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.
  IPR000362:Fumarate lyase
The vertebrate lens is a transparent tissue containing high levels ofsoluble protein.acked with short-range order in precisely aligned.longated cells . In birds.he main lens proteins are the alpha-.eta- and delta-crystallins. Mammalian lenses have a lower watercontent than their avian counterparts.nd contain gamma- insteadof delta-crystallins. Delta-crystallin evolved in a common ancestor of reptiles and birds.y the overexpression of arginosuccinate lyase in the lens. At this time. gene duplication took place.ince when the lens gene has accumulatedmutations in the coding sequence.endering it enzymatically inactive.The proteins belong to a superfamily of distantly-related metabolicenzymes.ll of which are active as homotetramers: they include fumarase.spartase.denylosuccinase and lactonisingenzyme. The structure of delta-crystallin comprises mainly alpha-helical domains . One domain is a bundle of 5 long helices.hich forms a 20-helixbundle at the core of the tetramer. The structure reveals a putativeactive-site cleft.ocated on the boundary between 3 subunits of thetetramer.
  IPR003031:Delta crystallin
Fumarase C catalyzes the stereospecific interconversion of fumarate to L-malate as part of the metabolic citric acid or Krebs cycle. The recent three-dimensional structure of fumarase C from Escherichia coli has identified a binding site for anions which is generated by side chains from three of the four subunits within the tetramer. These same side chains are found in the three most highly conserved regions within the class II fumarate hydratase family. Putative fumarases from several species (Mycobacterium tuberculosis.treptomyces coelicolor.seudomonas aeruginosa) branch deeply.lthough within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences.
  IPR005677:Fumarate hydratase, class II
The enzyme L-aspartate ammonia-lyase (aspartase) catalyses the reversible deamination of the amino acid L-aspartic acid.sing a carbanion mechanism to produce fumaric acid and ammonium ion. Aspartases from different organisms show high sequence homology.nd this homology extends to functionally related enzymes such as the class II fumarases.he argininosuccinate and adenylosuccinate lyases. The high-resolution structure of aspartase reveals a monomer that is composed of three domains oriented in an elongated S-shape . The central domain.omprised of five-helices.rovides the subunit contacts in the functionally active tetramer. The active sites are located in clefts between the subunits and structural and mutagenic studies have identified several of the active site functional groups. A separate regulatory site has been identified. The substrate.spartic also play the role of an activator.inding at this site along with a required divalent metal ion.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
SequencesProtein: FUMH_HUMAN (510 aa)
mRNA: NM_000143
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentK01679
  Level 3 annotation:
    fumarate hydratase
  Level 2 annotation:
    Citrate cycle (TCA cycle)
    Reductive carboxylate cycle (CO2 fixation)
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 123 residues, 239727527-239727893Exon2: 53 residues, 239730359-239730513Exon3: 44 residues, 239732365-239732493Exon4: 70 residues, 239733964-239734168Exon5: 57 residues, 239735925-239736091Exon6: 63 residues, 239738525-239738708Exon7: 61 residues, 239741889-239742066Exon8: 39 residues, 239743525-239743636Exon9: 47 residues, 239747104-239747239Exon10: 56 residues, 239749513-239749677Exon11: 2 residues, -Jump to FUMH_HUMAN  
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Loci Cluster (Details)Loci: 3873 239823075-239870324 ~-47K 4227(OPN3)(-)Loci: 3872 239727527-239749677 ~-22K 4224(FH)(-)Link out to UCSC