| Accession | TIGR00274 |
| Name | TIGR00274 |
| Function | N-acetylmuramic acid 6-phosphate etherase |
| Gene Symbol | murQ |
| Trusted Cutoff | 302.00 |
| Domain Trusted Cutoff | 302.00 |
| Noise Cutoff | 160.45 |
| Domain Noise Cutoff | 160.45 |
| Isology Type | equivalog |
| EC Number | 4.2.1.126 |
| HMM Length | 291 |
| 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. |
| References | RN [1]
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.
RN [2]
RM PMID:16452451
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) |
