|Function||N-acetylmuramic acid 6-phosphate etherase|
|Domain Trusted Cutoff||302.00|
|Domain Noise Cutoff||160.45|
|Mainrole Category||Cell envelope|
|Subrole Category||Biosynthesis and degradation of murein sacculus and peptidoglycan|
|Gene Ontology Term||GO:0006040: amino sugar metabolic process biological_process|
| ||GO:0009254: peptidoglycan turnover biological_process|
| ||GO:0016835: carbon-oxygen lyase activity molecular_function|
|Author||Dodson RJ, Loftus BJ, Haft DH|
|Entry Date||Apr 20 1999 2:05PM|
|Last Modified||Dec 12 2011 10:12PM|
|Comment||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.|
RM PMID: 15983044
RT Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase".
RA Jaeger T, Arsic M, Mayer C.
RL J Biol Chem. 2005 Aug 26;280(34):30100-6.
RT MurQ Etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall.
RA Uehara T, Suefuji K, Jaeger T, Mayer C, Park JT
RL J Bacteriol. 2006 Feb;188(4):1660-2.
DR PROSITE; PDOC00979; GCKR
AL clustalw, belvu
DR HAMAP; MF_00068; 141 of 144|
|Genome Property||GenProp0766: anhydro-N-acetylmuramic acid to N-acetylglucosamine-phosphate (HMM)|
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