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Search results 1 to 20 out of 20 for Sis

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Domain
Description: The sugar isomerase (SIS) domain is a phosphosugar-binding module that is found in a variety of eubacterial, archaebacterial and eukaryotic proteinsthat have a role in phosphosugar isomerization or regulation []. In enzymes, the SIS domain can have a catalytic function as an isomerase and bind to phosphorylated sugars. In bacterial transcriptional regulators of the rpiR family, the domain seems to bind substrates implicated in the genes for sugar metabolism that are controlled by the regulator. The SIS domain is found in one or two copies and can be linked to additional domains, such as helix-turn-helix (HTH), CBS, glutamine amidotransferases type 2, or phosphopantetheine-attachment [, ].The SIS domain has an α-β structure and is dominated by a five-stranded parallel β-sheet flanked on either side by α-helices forming a three-layer α-β-α sandwich []. The fold shows similarities to that of glucose-6-phosphate isomerase.
Protein Domain
Type: Domain
Description: AgaS contains a SIS (Sugar ISomerase) domain which is found in many phosphosugar isomerases and phosphosugar binding proteins. AgaS is a putative isomerase in Escherichia coli [].
Protein Domain
Type: Domain
Description: AgaS is a putative isomerase in Escherichia coli []. It is similar to glucosamine-6-phosphate synthases (GlmS), which catalyzes the first step in hexosamine metabolism. GlmS converts fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source [].GlmS contains a N-terminal glutaminase domain and two C-terminal SIS (Sugar ISomerase) domains. This domain is the first SIS domain found in GlmS and AgaS.
Protein Domain
Type: Domain
Description: KpsF is an arabinose-5-phosphate isomerase which contains a SIS (Sugar ISomerase) domain. SIS domains are found in many phosphosugar isomerases and phosphosugar binding proteins. KpsF catalyzes the reversible reaction of ribulose 5-phosphate to arabinose 5-phosphate. This is the second step in the CMP-Kdo biosynthesis pathway [, ].
Protein Domain
Type: Homologous_superfamily
Description: The sugar isomerase (SIS) domain is a phosphosugar-binding module that is found in a variety of eubacterial, archaebacterial and eukaryotic proteinsthat have a role in phosphosugar isomerization or regulation []. In enzymes, the SIS domain can have a catalytic function as an isomerase and bind to phosphorylated sugars. In bacterial transcriptional regulators of the rpiR family, the domain seems to bind substrates implicated in the genes for sugar metabolism that are controlled by the regulator. The SIS domain is found in one or two copies and can be linked to additional domains, such as helix-turn-helix (HTH), CBS, glutamine amidotransferases type 2, or phosphopantetheine-attachment [, ].The SIS domain has an α-β structure and is dominated by a five-stranded parallel β-sheet flanked on either side by α-helices forming a three-layer α-β-α sandwich []. The fold shows similarities to that of glucose-6-phosphate isomerase.
Protein Domain
Type: Domain
Description: This entry represents the SIS (Sugar ISomerase) domain 2 found in glucosamine 6-phosphate synthase (GlmS) and fructosamine deglycase FrlB.GlmS contains a N-terminal glutaminase domain and C-terminal isomerase domain (consisting of two SIS domains) []and catalyzes the first step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate using glutamine as nitrogen source []. The glutaminase domain hydrolyzes glutamine to glutamate and ammonia. Ammonia is transferred through a channel to the isomerase domain for glucosamine 6-phosphate synthesis. In the absence of glutamine, GlmS catalyzes the isomerization of fructose 6-phosphate into glucose 6- phosphate [, , ].FrlB catalyses the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid [].
Protein Domain
Type: Domain
Description: RpiR contains a SIS (Sugar ISomerase) domain, which is found in many phosphosugar isomerases and phosphosugar binding proteins. In E. coli, RpiR negatively regulates the expression of rpiB gene. Both rpiB and rpiA are ribose phosphate isomerases that catalyze the reversible reactions of ribose 5-phosphate into ribulose 5-phosphate [].This domain is also found in other members of the RpiR family of transcriptional regulators, such as MurR []and in uncharacterised proteins of the UPF0309 family.
Protein Domain
Type: Domain
Description: FrlB catalyses the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid [].This entry represents the first SIS domain of FrlB. SIS (Sugar ISomerase) domains are found in many phosphosugar isomerases and phosphosugar binding proteins. SIS domains are also found in proteins that regulate the expression of genes involved in synthesis of phosphosugars [].
Protein Domain
Type: Domain
Description: Bifunctional phosphoglucose/phosphomannose isomerase has both the phosphoglucose isomerase (PGI) and the phosphomannose isomerase (PMI) functions. These functions catalyze the reversible reactions of glucose 6-phosphate to fructose 6-phosphate, and mannose 6-phosphate to fructose 6-phosphate, respectively, at an equal rate [, ].This protein contains two SIS (Sugar ISomerase) domains. This entry represents the first SIS domain.
Protein Domain
Type: Domain
Description: Phosphoglucose isomerase (PGI) is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate []. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF) [, ]. Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.PGI is comprised of two domains; each domain is an α-β-alpha sandwich [], which correspond to a SIS (Sugar ISomerase) domain fold.
Protein Domain
Type: Domain
Description: Phosphoglucose isomerase (PGI) is a multifunctional enzyme which as an intracellular dimer catalyzes the reversible isomerization of glucose 6-phosphate to fructose 6-phosphate []. As an extracellular protein, PGI also has functions equivalent to neuroleukin (NLK), autocrine motility factor (AMF), and maturation factor (MF) [, ]. Evidence suggests that PGI, NLK, AMF, and MF are closely related or identical. NLK is a neurotrophic growth factor that promotes regeneration and survival of neurons. The dimeric form of NLK has isomerase function, whereas its monomeric form carries out neurotrophic activity. AMF is a cytokine that stimulates cell migration and metastasis. MF mediates the differentiation of human myeloid leukemic HL-60 cells to terminal monocytic cells.PGI is comprised of two domains; each domain is an α-β-alpha sandwich [], which correspond to a SIS (Sugar ISomerase) domain fold.
Protein Domain
Type: Domain
Description: This domain is found in the N-terminal region of glucose-6-phosphate isomerase-like protein, just before the phospho-glucose isomerase C-terminal SIS domain.
Protein Domain
Type: Domain
Description: This domain contains a helix-turn-helix motif [].Every member of this family is N-terminal to a SIS domain . Members of this family are probably regulators of genesinvolved in phosphosugar metobolism.
Protein Domain
Type: Family
Description: This is a family of closely related proteins with the phosphosugar-binding domain SIS (Sugar ISomerase) followed by two copies of the CBS (named after Cystathionine Beta Synthase) domain. The group includes GutQ, a protein of the glucitol operon [, ]and KpsF, a virulence factor involved in capsular polysialic acid biosynthesis in some pathogenic strains of Escherichia coli [].
Protein Domain
Type: Domain
Description: This domain is conserved in the Bacillales. The function is not known, but given this domains relationship to the SIS domain it may carry out a sugar isomerase reaction. Several members are annotated as being YWJG, a protein expressed downstream of pyrG, a gene encoding for cytidine triphosphate synthetase.
Protein Domain
Type: Domain
Description: Phosphoglucose isomerase (PGI) catalyses the interconversion of phosphoglucose and phosphofructose, and is a component of many sugar metabolic pathways. In some archaea and bacteria PGI activity occurs via a bifunctional enzyme that also exhibits phosphomannose isomerase (PMI) activity. Though not closely related to eukaryotic PGIs, the bifunctional enzyme is similar enough that the sequence includes the cluster of threonines and serines that forms the sugar phosphate-binding site in conventional PGI.The bifunctional PGI/PMI enzyme contains two SIS (Sugar ISomerase) domains. This entry represents the C-terminal SIS domain, which contains many of the active catalytic site residues. The enzyme is thought to use the same catalytic mechanisms for both glucose ring-opening and isomerisation for the interconversion of glucose 6-phosphate to fructose 6-phosphate [].
Protein Domain
Type: Family
Description: This entry contains MurR, which represses the expression of the murPQ operon involved in the uptake and degradation of N-acetylmuramic acid (MurNAc). It binds to two adjacent inverted repeats within the operator region. MurNAc 6-phosphate, the substrate of MurQ, and is the specific inducer that weakens binding of MurR to the operator.MurR is paralogous to RpiR and has both HTH and SIS phosphosugar binding domains. The divergent murR and murQP transcripts have complementary 5' ends []. It is required for swarming phenotype.
Protein Domain
Type: Conserved_site
Description: The glucokinase regulatory protein (GCKR) []is a vertebrate protein thatinhibits glucokinase by forming a complex with the enzyme, which plays a rolein the control of blood glucose homeostasis. GCKR is a protein of about 70 Kdwhich is evolutionary related to bacterial N-acetylmuramic acid 6-phosphateetherases (MurNAc-6-P etherase, murQ), which are about half the size of GCKRand form active homodimers. MurNAc-6-P etherases catalyse the cleavage of theD-lactyl ether substituent of the bacterial cell wall sugar MurNAc and play arole in recycling of the cell wall []. The 3D structure of the Haemophilusinfluenzae HI0754/murQ protein shows structural relationshipswith other sugar isomerase (SIS) domain proteins. Incontrast to mono-SIS bacterial MurNAc-6-P etherase, mammalian GCKR is composedof two SIS domains.
Protein Domain
Type: Homologous_superfamily
Description: Proteins in this superfamily are approximately 180 amino acids in length found exclusively in epsilon-proteobacteria. The crystal structure of HobA from Helicobacter pylori has been reported at 1.7A resolution; HobA represents a modified Rossmann fold consisting of a five-stranded parallel β-sheet (beta1-5) flanked on one side by alpha-2, alpha-3 and alpha-6 helices and alpha-4 and alpha-5 on the other. The alpha-1 helix is extended away from and has minimal interaction with the globular part of the protein. Four monomers interact to form a tetrameric molecule. Four calcium atoms bind to the tetramer and these binding sites may have functional relevance. The closest structural homologue of HobA is a sugar isomerase (SIS) domain containing protein, the phosphoheptose isomerase from Pseudomonas aeruginosa. The SIS proteins share strong sequence homology with DiaA from Escherichia coli; yet, HobA and DiaA share no sequence homology []. HobA is a novel protein essential for initiation of H. pylori chromosome replication. It interacts specifically via DnaA with the oriC-DnaA complex. It is possible that HobA is essential for the correct formation and stabilisation of the orisome by facilitating the spatial positioning of DnaA at oriC [].
Protein Domain
Type: Family
Description: This family of proteins is found exclusively in epsilon-proteobacteria. Proteins in this family are approximately 180 amino acids in length. The crystal structure of HobA from Helicobacter pylori has been reported at 1.7A resolution; HobA represents a modified Rossmann fold consisting of a five-stranded parallel β-sheet (beta1-5) flanked on one side by alpha-2, alpha-3 and alpha-6 helices and alpha-4 and alpha-5 on the other. The alpha-1 helix is extended away from and has minimal interaction with the globular part of the protein. Four monomers interact to form a tetrameric molecule. Four calcium atoms bind to the tetramer and these binding sites may have functional relevance. The closest structural homologue of HobA is a sugar isomerase (SIS) domain containing protein, the phosphoheptose isomerase from Pseudomonas aeruginosa. The SIS proteins share strong sequence homology with DiaA from Escherichia coli; yet, HobA and DiaA share no sequence homology []. HobA is a novel protein essential for initiation of H. pylori chromosome replication. It interacts specifically via DnaA with the oriC-DnaA complex. It is possible that HobA is essential for the correct formation and stabilisation of the orisome by facilitating the spatial positioning of DnaA at oriC [].