Identification
Name:Anhydro-N-acetylmuramic acid kinase
Synonyms:
  • AnhMurNAc kinase
Gene Name:anmK
Enzyme Class:
Biological Properties
General Function:Involved in ATP binding
Specific Function:Catalyzes the specific phosphorylation of 1,6-anhydro-N- acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of 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 III PW000895
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Adenosine diphosphate+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.01,6-Anhydro-N-acetylmuramate ↔ 1.0Adenosine diphosphate + 1.0MurNAc-6-P + 1.0ADP
ReactionCard
1.0anhydro-n-acetylmuramic acid+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0anhydro-n-acetylmuramic acid + 1.0Adenosine triphosphate + 1.0Water → 1.0N-Acetylmuramate 6-phosphate + 1.0ADP + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB232201,6-Anhydro-N-acetyl-beta-muramateMetaboCard
ECMDB205191,6-Anhydro-N-acetylmuramateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB24235MurNAc-6-PMetaboCard
ECMDB20518N-Acetylmuramate 6-phosphateMetaboCard
ECMDB20177N-Acetylmuramic acid 6-phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
nucleoside binding
phosphotransferase activity, alcohol group as acceptor
purine nucleoside binding
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolic process
amino sugar metabolic process
aminoglycan metabolic process
carbohydrate metabolic process
glycosaminoglycan metabolic process
metabolic process
monosaccharide metabolic process
peptidoglycan metabolic process
peptidoglycan turnover
polysaccharide metabolic process
primary metabolic process
small molecule metabolic process
Gene Properties
Blattner:b1640
Gene OrientationCounterclockwise
Centisome Percentage:37.00
Left Sequence End1716517
Right Sequence End1717626
Gene Sequence:
>1110 bp
ATGAAATCGGGCCGCTTTATTGGCGTTATGTCAGGCACCAGCCTTGATGGTGTTGATGTT
GTGTTGGCGACAATTGATGAACACCGGGTCGCACAGCTGGCAAGTTTGAGTTGGCCGATC
CCGGTATCTCTGAAACAGGCTGTACTGGATATTTGCCAGGGCCAGCAGCTTACACTTTCG
CAGTTTGGACAGCTTGATACTCAACTCGGGCAACTTTTTGCTGATGCGGTCAATGCCTTG
CTTAAGGAACAAAATCTGCAGGCAAGAGATATAGTTGCGATCGGTTGTCACGGTCAAACC
GTCTGGCATGAACCGACGGGCGTGGCACCACACACTTTACAGATTGGCGATAACAATCAA
ATTGTGGCACGCACCGGAATTACGGTTGTCGGTGATTTTCGCCGTCGCGATATTGCCTTG
GGAGGACAAGGCGCACCGCTGGTACCTGCGTTCCATCATGCGCTGCTGGCTCACCCAACC
GAGCGACGAATGGTGCTCAATATTGGCGGCATCGCCAATCTGTCACTGCTCATTCCTGGG
CAGCCGGTTGGGGGCTACGATACCGGTCCTGGTAACATGCTGATGGATGCCTGGATCTGG
CGTCAGGCCGGTAAACCTTACGATAAAGATGCCGAGTGGGCACGGGCGGGTAAAGTTATT
CTCCCACTGCTGCAAAATATGCTCAGCGACCCGTATTTCTCGCAACCTGCACCGAAAAGC
ACCGGACGCGAATACTTTAACTATGGTTGGCTGGAGCGCCATTTGCGCCATTTTCCGGGT
GTTGATCCCCGAGATGTGCAGGCGACACTGGCAGAACTCACCGCCGTGACCATTTCTGAA
CAAGTTTTGTTGAGCGGTGGCTGCGAACGATTGATGGTATGTGGTGGAGGTAGTCGTAAT
CCGCTACTCATGGCGCGTCTGGCGGCATTACTGCCAGGCACAGAAGTCACCACCACCGAT
GCCGTTGGCATTAGTGGCGATGACATGGAAGCATTGGCTTTCGCCTGGCTTGCCTGGCGG
ACGCTGGCGGGATTACCAGGAAATCTGCCTTCCGTCACTGGCGCAAGCCAGGAGACGGTA
CTGGGGGCTATTTTCCCCGCTAACCCGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:369
Protein Molecular Weight:39496
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Anhydro-N-acetylmuramic acid kinase
MKSGRFIGVMSGTSLDGVDVVLATIDEHRVAQLASLSWPIPVSLKQAVLDICQGQQLTLS
QFGQLDTQLGQLFADAVNALLKEQNLQARDIVAIGCHGQTVWHEPTGVAPHTLQIGDNNQ
IVARTGITVVGDFRRRDIALGGQGAPLVPAFHHALLAHPTERRMVLNIGGIANLSLLIPG
QPVGGYDTGPGNMLMDAWIWRQAGKPYDKDAEWARAGKVILPLLQNMLSDPYFSQPAPKS
TGREYFNYGWLERHLRHFPGVDPRDVQATLAELTAVTISEQVLLSGGCERLMVCGGGSRN
PLLMARLAALLPGTEVTTTDAVGISGDDMEALAFAWLAWRTLAGLPGNLPSVTGASQETV
LGAIFPANP
References
External Links:
ResourceLink
Uniprot ID:P77570
Uniprot Name:ANMK_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742706
Ecogene ID:EG13942
Ecocyc:EG13942
ColiBase:b1640
Kegg Gene:b1640
EchoBASE ID:EB3700
CCDB:ANMK_ECOLI
BacMap:16129598
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • 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
  • 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
  • Uehara, T., Suefuji, K., Valbuena, N., Meehan, B., Donegan, M., Park, J. T. (2005). "Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate." J Bacteriol 187:3643-3649. Pubmed: 15901686