N-acetylmuramic acid 6-phosphate etherase (P76535)

Identification
Name:N-acetylmuramic acid 6-phosphate etherase
Synonyms:
  • MurNAc-6-P etherase
  • N-acetylmuramic acid 6-phosphate hydrolase
  • N-acetylmuramic acid 6-phosphate lyase
Gene Name:murQ
Enzyme Class:
Biological Properties
General Function:Involved in carbon-oxygen lyase activity
Specific Function:Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6- phosphate and D-lactate. Is required for growth on MurNAc as the sole source of carbon and energy. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling
Cellular Location:Not Available
SMPDB Pathways:
  • 1,6-anhydro-<i>N</i>-acetylmuramic acid recycling PW002064
  • Amino sugar and nucleotide sugar metabolism I PW000886
  • Amino sugar and nucleotide sugar metabolism II PW000887
  • Amino sugar and nucleotide sugar metabolism III PW000895
KEGG Pathways:
  • Amino sugar and nucleotide sugar metabolism ec00520
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylmuramic acid 6-phosphate + 1.0Water ↔ 1.0N-Acetyl-D-Glucosamine 6-Phosphate + 1.0D-Lactic acid
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0MurNAc-6-P + 1.0Water → 1.0D-Lactic acid + 1.0N-Acetylglucosamine 6-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylmuramate 6-phosphate + 1.0Water ↔ 1.0N-Acetyl-D-Glucosamine 6-Phosphate + 1.0D-Lactic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0N-Acetylmuramic acid 6-phosphate + 1.0Water ↔ 1.0N-Acetyl-D-Glucosamine 6-Phosphate + 1.0D-Lactic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetylmuramic acid 6-phosphate + 1.0Water → 1.0N-Acetyl-D-Glucosamine 6-Phosphate + 1.0D-Lactic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01311D-Lactic acidMetaboCard
ECMDB24235MurNAc-6-PMetaboCard
ECMDB01062N-Acetyl-D-Glucosamine 6-PhosphateMetaboCard
ECMDB24079N-Acetylglucosamine 6-phosphateMetaboCard
ECMDB20518N-Acetylmuramate 6-phosphateMetaboCard
ECMDB20177N-Acetylmuramic acid 6-phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbohydrate binding
carbon-oxygen lyase activity
catalytic activity
lyase activity
sugar binding
Process
alcohol metabolic process
amino sugar catabolic process
amino sugar metabolic process
carbohydrate metabolic process
metabolic process
monosaccharide metabolic process
primary metabolic process
small molecule metabolic process
Gene Properties
Blattner:b2428
Gene OrientationClockwise
Centisome Percentage:54.83
Left Sequence End2543795
Right Sequence End2544691
Gene Sequence:
>897 bp
ATGCTGGAAAAATCTCTGGCAACACTTTTCGCGTTGTTAATTTTAGCAACGCTGATAAAC
CGTTTTCTGCTATGGCGGTTACCGGAGAGAAAAGGGGGTGAGGTTACATTACGTATTCGT
ACCTGGTGGGGCATCGTCATTTGTTTTTCAATGGTGATTTCAGGTCCACGCTGGATGACG
TTGACGTTTTTTGCGCTGATAAGTTTTCTGGCATTGAAAGAATATTGTACGCTTATATCT
GTACATTTTCCGCGTTGGTTATATTGGGGTATTCCTCTTAACTATTTGCTTATCGGTTTT
AATTGCTTTGAGCTGTTTCTGTTATTTATACCTTTGGCTGGGTTTCTGATATTAGCCACC
GGGCAAGTTTTAGTGGGTGACCCCTCTGGTTTTCTGCATACCGTGAGCGCCATTTTTTGG
GGCTGGATAATGACCGTTTTCGCCTTGAGTCATGCCGCCTGGTTATTAATGTTGCCAACC
ACAAATATCCAGGGCGGGGCGTTACTGGTGTTATTTCTTTTGGCATTAACCGAGTCAAAC
GATATTGCACAGTATTTATGGGGAAAATCCTGCGGCAGAAGAAAAGTGGTCCCTAAAGTC
AGCCCGGGAAAAACATTGGAAGGTCTGATGGGCGGCGTCATCACCATCATGATTGCGTCA
CTGATTATCGGACCGTTACTGACACCGCTAAATACATTACAGGCATTATTAGCGGGTTTG
TTAATTGGTATTAGTGGTTTTTGCGGCGATGTCGTGATGTCAGCCATCAAACGAGATATT
GGTGTTAAAGATAGCGGAAAACTATTGCCAGGACATGGCGGACTCCTTGACAGGATTGAC
TCATTAATTTTCACCGCTCCGGTATTTTTTTATTTTATACGCTACTGCTGTTACTGA
Protein Properties
Pfam Domain Function:
Protein Residues:298
Protein Molecular Weight:31220
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>N-acetylmuramic acid 6-phosphate etherase
MQFEKMITEGSNTASAEIDRVSTLEMCRIINDEDKTVPLAVERVLPDIAAAIDVIHAQVS
GGGRLIYLGAGTSGRLGILDASECPPTYGVKPGLVVGLIAGGEYAIQHAVEGAEDSREGG
VNDLKNINLTAQDVVVGIAASGRTPYVIAGLEYARQLGCRTVGISCNPGSAVSTTAEFAI
TPIVGAEVVTGSSRMKAGTAQKLVLNMLSTGLMIKSGKVFGNLMVDVVATNEKLHVRQVN
IVKNATGCSAEQAEAALIACERNCKTAIVMVLKNLDAAEAKKRLDQHGGFIRQVLDKE
References
External Links:
ResourceLink
Uniprot ID:P76535
Uniprot Name:MURQ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674949
Ecogene ID:EG14162
Ecocyc:EG14162
ColiBase:b2428
Kegg Gene:b2428
EchoBASE ID:EB3914
CCDB:MURQ_ECOLI
BacMap:16130353
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Fountoulakis, M., Takacs, M. F., Berndt, P., Langen, H., Takacs, B. (1999). "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography." Electrophoresis 20:2181-2195. Pubmed: 10493123
  • Hadi, T., Dahl, U., Mayer, C., Tanner, M. E. (2008). "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling." Biochemistry 47:11547-11558. Pubmed: 18837509
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Jaeger, T., Arsic, M., Mayer, C. (2005). "Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase"." J Biol Chem 280:30100-30106. Pubmed: 15983044
  • Jaeger, T., Mayer, C. (2008). "The transcriptional factors MurR and catabolite activator protein regulate N-acetylmuramic acid catabolism in Escherichia coli." J Bacteriol 190:6598-6608. Pubmed: 18723630
  • Uehara, T., Suefuji, K., Jaeger, T., Mayer, C., Park, J. T. (2006). "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." J Bacteriol 188:1660-1662. Pubmed: 16452451
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837