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 ...
4-365
0e+00
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: 583.58 E-value: 0e+00
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
4-365
0e+00
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: 583.58 E-value: 0e+00
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
6-365
0e+00
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: 511.69 E-value: 0e+00
microcompartment protein PduM; Members of this family are PduM, a protein essential for ...
64-154
7.12e-03
microcompartment protein PduM; Members of this family are PduM, a protein essential for forming functional microcompartments in which a trimeric B12-dependent enzyme acts as a dehydratase for 1,2-propanediol (Salmonella enterica) or glycerol (Lactobacillus reuteri).
Pssm-ID: 275286 Cd Length: 153 Bit Score: 36.83 E-value: 7.12e-03
Anhydro-N-acetylmuramic acid kinase; Anhydro-N-acetylmuramic acid kinase catalyzes the ...
4-365
0e+00
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: 583.58 E-value: 0e+00
nucleotide-binding domain (NBD) of anhydro-N-acetylmuramic acid kinase (ANMK) and similar ...
6-365
0e+00
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: 511.69 E-value: 0e+00
nucleotide-binding domain (NBD) of levoglucosan kinase (LGK) and similar proteins; LGK (EC 2.7. ...
7-361
5.69e-59
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: 196.23 E-value: 5.69e-59
nucleotide-binding domain (NBD) of the anhydro-N-acetylmuramic acid kinase (ANMK)-like domain ...
7-335
5.54e-49
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: 168.74 E-value: 5.54e-49
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
224-321
5.48e-04
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 41.84 E-value: 5.48e-04
nucleotide-binding domain (NBD) of Methanopyrus kandleri sugar kinase Mk0840 and similar ...
165-321
2.05e-03
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: 39.65 E-value: 2.05e-03
microcompartment protein PduM; Members of this family are PduM, a protein essential for ...
64-154
7.12e-03
microcompartment protein PduM; Members of this family are PduM, a protein essential for forming functional microcompartments in which a trimeric B12-dependent enzyme acts as a dehydratase for 1,2-propanediol (Salmonella enterica) or glycerol (Lactobacillus reuteri).
Pssm-ID: 275286 Cd Length: 153 Bit Score: 36.83 E-value: 7.12e-03
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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