Protein Family Models

This domain is found N-terminal in glucokinase regulatory protein (GKRP) and related proteins. GKRP regulates glucokinase and it is activated by fructose 6-phosphate and inactivated by fructose 1-phosphate. It consists of two topologically identical SIS domains and and alpha-helical lid domain [1-4]. Paper describing PDB structure 3w0l. [1]. 23733961. Molecular basis for the role of glucokinase regulatory protein as the allosteric switch for glucokinase. Choi JM, Seo MH, Kyeong HH, Kim E, Kim HS;. Proc Natl Acad Sci U S A. 2013;110:10171-10176. Paper describing PDB structure 4bb9. [2]. 23621087. Crystal structure of glucokinase regulatory protein. Pautsch A, Stadler N, Lohle A, Rist W, Berg A, Glocker L, Nar H, Reinert D, Lenter M, Heckel A, Schnapp G, Kauschke SG;. Biochemistry. 2013;52:3523-3531. Paper describing PDB structure 4lc9. [3]. 23957911. Structural basis for regulation of human glucokinase by glucokinase regulatory protein. Beck T, Miller BG;. Biochemistry. 2013;52:6232-6239. Paper describing PDB structure 4ly9. [4]. 24226772. Antidiabetic effects of glucokinase regulatory protein small-molecule disruptors. Lloyd DJ, St Jean DJ Jr, Kurzeja RJ, Wahl RC, Michelsen K, Cupples R, Chen M, Wu J, Sivits G, Helmering J, Komorowski R, Ashton KS, Pennington LD, Fotsch C, Vazir M, Chen K, Chmait S, Zhang J, Liu L, Norman MH, Andrews KL, Bartberger MD, Van G, Galbreath EJ, Vonderfecht SL, Wang M, Jordan SR, Veniant MM, Hale C;. Nature. 2013;504:437-440. Paper describing PDB structure 4lzj. [5]. 24251551. Structure of MurNAc 6-phosphate hydrolase (MurQ) from Haemophilus influenzae with a bound inhibitor. Hadi T, Hazra S, T. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Glucokinase regulatory protein (GKRP) binds glucokinase (GK) mainly through hydrophobic interactions, functioning as an allosteric switch in blood glucose control by the liver [1]. GKRP is trilobal in shape, consisting of two topologically identical sugar isomerase (SIS) domains capped by an alpha-helical lid domain (Pfam:PF20741). This entry represents the second SIS domain from GKRP [1]. Paper describing PDB structure 3w0l. [1]. 23733961. Molecular basis for the role of glucokinase regulatory protein as the allosteric switch for glucokinase. Choi JM, Seo MH, Kyeong HH, Kim E, Kim HS;. Proc Natl Acad Sci U S A. 2013;110:10171-10176. Paper describing PDB structure 4bb9. [2]. 23621087. Crystal structure of glucokinase regulatory protein. Pautsch A, Stadler N, Lohle A, Rist W, Berg A, Glocker L, Nar H, Reinert D, Lenter M, Heckel A, Schnapp G, Kauschke SG;. Biochemistry. 2013;52:3523-3531. Paper describing PDB structure 4lc9. [3]. 23957911. Structural basis for regulation of human glucokinase by glucokinase regulatory protein. Beck T, Miller BG;. Biochemistry. 2013;52:6232-6239. Paper describing PDB structure 4ly9. [4]. 24226772. Antidiabetic effects of glucokinase regulatory protein small-molecule disruptors. Lloyd DJ, St Jean DJ Jr, Kurzeja RJ, Wahl RC, Michelsen K, Cupples R, Chen M, Wu J, Sivits G, Helmering J, Komorowski R, Ashton KS, Pennington LD, Fotsch C, Vazir M, Chen K, Chmait S, Zhang J, Liu L, Norman MH, Andrews KL, Bartberger MD, Van G, Galbreath EJ, Vonderfecht SL, Wang M, Jordan SR, Veniant MM, Hale C;. Nature. 2013;504:437-440. (from Pfam)

Date:

2024-10-16

This domain is found at the C terminus of Glucokinase regulatory protein (GKRP) from animals and N-acetylmuramic acid 6-phosphate etherase (MurQ) from bacteria. GKRP binds Glucokinase (GK) mainly through hydrophobic interactions, functioning as an allosteric switch in blood glucose control by the liver [1]. GKRP is trilobal in shape, consisting of two topologically identical sugar isomerase (SIS) domains (Pfam:PF01380 and Pfam:PF13580) capped by an alpha helical C-terminal domain (this entry). The Lid domain consists of a bundle of seven alpha helices with a core that shows a UBA-like fold [2]. MurQ, which also shows a SIS domain, plays a key role in the peptidoglycane recycling pathway. Its crystal structure shows each monomer have an alpha-beta-alpha sandwich fold commonly found in regulatory proteins controlling the expression of genes involved in the synthesis of phosphosugars. The C-terminal domain of this protein (this entry) is comprised of five alpha helices [4]. Paper describing PDB structure 3w0l. [1]. 23733961. Molecular basis for the role of glucokinase regulatory protein as the allosteric switch for glucokinase. Choi JM, Seo MH, Kyeong HH, Kim E, Kim HS;. Proc Natl Acad Sci U S A. 2013;110:10171-10176. Paper describing PDB structure 4bb9. [2]. 23621087. Crystal structure of glucokinase regulatory protein. Pautsch A, Stadler N, Lohle A, Rist W, Berg A, Glocker L, Nar H, Reinert D, Lenter M, Heckel A, Schnapp G, Kauschke SG;. Biochemistry. 2013;52:3523-3531. Paper describing PDB structure 4lc9. [3]. 23957911. Structural basis for regulation of human glucokinase by glucokinase regulatory protein. Beck T, Miller . TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

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. [1]. 10203754. The SIS domain: a phosphosugar-binding domain. Bateman A;. Trends Biochem Sci 1999;24:94-95. (from Pfam)

Date:

2024-10-16

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. Presumably the SIS domains bind to the end-product of the pathway. Structure of SIS domain. [1]. 9739095. 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. Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B, Polikarpov I;. Structure 1998;6:1047-1055. [2]. 10203754. The SIS domain: a phosphosugar-binding domain. Bateman A;. Trends Biochem Sci 1999;24:94-95. (from Pfam)

Date:

2024-10-16

N-acetylmuramic acid 6-phosphate etherase catalyzes the cleavage of the lactyl ether bond of N-acetylmuramic acid 6-phosphate, a bacterial cell wall sugar.

Date:

2017-02-03

Catalyzes the cleavage of the lactyl ether moiety of N-acetylmuramic acid-6-phosphate (MurNAc-6-P) to form N-acetylglucosamine-6-phosphate (GlcNAc-6-P) and lactate; involved in MurNAc dissimilation pathway

Date:

2020-10-26

Catalyzes the cleavage of the lactyl ether moiety of N-acetylmuramic acid-6-phosphate (MurNAc-6-P) to form N-acetylglucosamine-6-phosphate (GlcNAc-6-P) and lactate; involved in MurNAc dissimilation pathway

Date:

2020-10-26

This protein, MurQ, is involved in recycling components of the bacterial murein sacculus turned over during cell growth. The cell wall metabolite anhydro-N-acetylmuramic acid (anhMurNAc) is converted by a kinase, AnmK, to MurNAc-phosphate, then converted to N-acetylglucosamine-phosphate by this etherase, called MurQ. This family of proteins is similar to the C-terminal half of a number of vertebrate glucokinase regulator proteins and contains a Prosite pattern which is shared by this group of proteins in a region of local similarity.

Gene:

murQ

Date:

2024-06-24