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InterPro: IPR001347 Sugar isomerase (SIS)

Protein matchesHelp
UniProtKB
Matches:
10316 proteins
AccessionHelp IPR001347 SIS
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR004515 Phosphoheptose isomerase, subgroup
IPR004800 KpsF/GutQ
IPR005488 Glucokinase regulatory-like protein
IPR005855 Glucosamine-fructose-6-phosphate aminotransferase, isomerising
IPR011857 Bifunctional glucose-6-phosphate/mannose-6-phosphate isomerase
IPR014180 Sugar isomerase, AgaS
IPR017552 6-phospho 3-hexuloisomerase
IPR020620 Phosphoheptose isomerase
Contains IPR005486 Glucokinase regulatory, conserved site
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0005529 sugar binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The SIS (Sugar ISomerase) domain is a phosphosugar-binding domain [1] 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 possibly by binding to the end-product of the pathway.

Structural linksHelp
SCOP: c.80.1.1 , c.80.1.3
Database linksHelp
PANDIT: PF01380
Blocks: IPB001347
Pfam Clan: CL0067.9

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001347 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
A6ZME2 Putative glucosamine--fructose-6-phosphate aminotransferase [isomerizing]

O32157 Fructosamine deglycase frlB

P47856 Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1

P72720 Glucosamine--fructose-6-phosphate aminotransferase [isomerizing]

Q06210 Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR000583 Glutamine amidotransferase, class-II
IPR005855 Glucosamine-fructose-6-phosphate aminotransferase, isomerising
IPR001347 Sugar isomerase (SIS)
IPR017932 Glutamine amidotransferase, type II
SWISS-MODEL
PDB Chain
ModBase

PublicationsHelp
1. Bateman A.
The SIS domain: a phosphosugar-binding domain.
Trends Biochem. Sci. 24 94-5 1999 [PubMed: 10203754]
http://dx.doi.org/10.1016/S0968-0004(99)01357-2

Additional ReadingHelp
Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B, Polikarpov I.
Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain.
Structure 6 1998 1047-55 [PubMed: 9739095]
http://dx.doi.org/10.1016/S0969-2126(98)00105-1
Mouilleron S, Golinelli-Pimpaneau B.
Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation.
Protein Sci. 16 2007 485-93 [PubMed: 17322533]
http://dx.doi.org/10.1110/ps.062598107
Keyamura K, Fujikawa N, Ishida T, Ozaki S, Su'etsugu M, Fujimitsu K, Kagawa W, Yokoyama S, Kurumizaka H, Katayama T.
The interaction of DiaA and DnaA regulates the replication cycle in E. coli by directly promoting ATP DnaA-specific initiation complexes.
Genes Dev. 21 2007 2083-99 [PubMed: 17699754]
http://dx.doi.org/10.1101/gad.1561207
Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS.
Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants.
J. Biol. Chem. 283 2008 2835-45 [PubMed: 18056714]
http://dx.doi.org/10.1074/jbc.M706163200
Seetharaman J, Rajashankar KR, Solorzano V, Kniewel R, Lima CD, Bonanno JB, Burley SK, Swaminathan S.
Crystal structures of two putative phosphoheptose isomerases.
Proteins 63 2006 1092-6 [PubMed: 16477602]
http://dx.doi.org/10.1002/prot.20908
Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B.
Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel.
J. Mol. Biol. 377 2008 1174-85 [PubMed: 18295797]
http://dx.doi.org/10.1016/j.jmb.2008.01.077
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