anhydro-N-acetylmuramic acid kinase catalyzes hydrolysis of 1,6-anhydro bond of anyhydro-N-acetylmuramic acid (anhMurNAc) and phosphorylates anhMurNAc to produce N-acetyl-muramate-6-phosphate
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
3-363
2.86e-180
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase 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. It is also required for the utilization of anhMurNAc, either imported from the medium, or derived from its own cell wall murein, and in so doing plays a role in cell wall recycling.
Pssm-ID: 397660 Cd Length: 364 Bit Score: 504.23 E-value: 2.86e-180
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
4-362
4.39e-179
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar proteins; ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, 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. It 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.
Pssm-ID: 466900 Cd Length: 369 Bit Score: 501.29 E-value: 4.39e-179
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
3-363
2.86e-180
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase 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. It is also required for the utilization of anhMurNAc, either imported from the medium, or derived from its own cell wall murein, and in so doing plays a role in cell wall recycling.
Pssm-ID: 397660 Cd Length: 364 Bit Score: 504.23 E-value: 2.86e-180
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
4-362
4.39e-179
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar proteins; ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, 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. It 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.
Pssm-ID: 466900 Cd Length: 369 Bit Score: 501.29 E-value: 4.39e-179
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7. ...
5-362
8.18e-62
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7.1.232) catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP. In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom.
Pssm-ID: 466901 Cd Length: 409 Bit Score: 203.55 E-value: 8.18e-62
nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain ...
5-360
1.35e-54
nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain family; The family includes anhydro-N-acetylmuramic acid kinase (ANMK) and levoglucosan kinase (LGK). ANMK (EC 2.7.1.170), also called AnhMurNAc kinase, 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. It 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. LGK (EC 2.7.1.232) catalyzes the transfer of a phosphate group from ATP to levoglucosan (1,6-anhydro-beta-D-glucopyranose, LG) to yield glucose 6-phosphate in the presence of magnesium ion and ATP. In addition to the canonical kinase phosphotransfer reaction, the conversion requires cleavage of the 1,6-anhydro ring to allow ATP-dependent phosphorylation of the sugar O-6 atom. The ANMK-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466855 Cd Length: 358 Bit Score: 183.37 E-value: 1.35e-54
nucleotide-binding domain (NBD) of Methanopyrus kandleri sugar kinase Mk0840 and similar ...
161-306
7.41e-04
nucleotide-binding domain (NBD) of Methanopyrus kandleri sugar kinase Mk0840 and similar proteins; The family includes uncharacterized Methanopyrus kandleri sugar kinase Mk0840 that shows high similarity to bacterial anhydro-N-acetylmuramic acid kinase, which is involved in murein recycling. This family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466864 Cd Length: 313 Bit Score: 41.19 E-value: 7.41e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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