N-acetylglucosamine kinase [Sinorhizobium meliloti]
Protein Classification
N-acetylglucosamine kinase( domain architecture ID 10006823)
N-acetylglucosamine kinase of eukaryotic type similar to Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase.
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| ASKHA_NBD_GspK-like | cd24082 | nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
4-281 | 8.16e-98 | |||||
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar. : Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 288.66 E-value: 8.16e-98
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| Name | Accession | Description | Interval | E-value | |||||
| ASKHA_NBD_GspK-like | cd24082 | nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
4-281 | 8.16e-98 | |||||
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar. Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 288.66 E-value: 8.16e-98
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| BadF | COG2971 | BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
4-288 | 1.18e-70 | |||||
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism]; Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 220.14 E-value: 1.18e-70
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| BcrAD_BadFG | pfam01869 | BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
6-252 | 2.32e-19 | |||||
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370. Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 85.48 E-value: 2.32e-19
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| Name | Accession | Description | Interval | E-value | |||||
| ASKHA_NBD_GspK-like | cd24082 | nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
4-281 | 8.16e-98 | |||||
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar. Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 288.66 E-value: 8.16e-98
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| BadF | COG2971 | BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
4-288 | 1.18e-70 | |||||
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism]; Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 220.14 E-value: 1.18e-70
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| ASKHA_NBD_eukNAGK-like | cd24007 | nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
6-281 | 1.56e-45 | |||||
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 155.54 E-value: 1.56e-45
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| ASKHA_NBD_KdgK-like | cd24083 | nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase ... |
5-250 | 5.35e-34 | |||||
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and similar proteins; The family includes a group of uncharacterized proteins similar to Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK; EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase. It catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. Pssm-ID: 466933 [Multi-domain] Cd Length: 284 Bit Score: 125.19 E-value: 5.35e-34
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| ASKHA_NBD_MurK-like | cd24084 | nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid ... |
4-283 | 1.34e-32 | |||||
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK) and similar proteins; The family includes a group of uncharacterized proteins similar to Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK; EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase. It catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. MurK may have a role in the rescue of the murein sugars GlcNAc and MurNAc released from muropeptides during cell wall turnover in C.acetobutylicum. Pssm-ID: 466934 [Multi-domain] Cd Length: 302 Bit Score: 121.70 E-value: 1.34e-32
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| ASKHA_NBD_StHK-like | cd24080 | nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ... |
5-251 | 3.65e-25 | |||||
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and similar proteins; The family includes a group of uncharacterized proteins similar to Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK). Hexokinase (EC 2.7.1.1) catalyzes the phosphorylation of glucose to glucose 6-phosphate by using ATP as a phosphoryl donor. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. It differs from other known hexokinases and glucokinases in that its activity is strongly inhibited by ADP. It is distinct in its broad substrate specificity from the GlcNAc kinases, which are specific for GlcNAc. Pssm-ID: 466930 [Multi-domain] Cd Length: 291 Bit Score: 101.73 E-value: 3.65e-25
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| BcrAD_BadFG | pfam01869 | BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
6-252 | 2.32e-19 | |||||
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370. Pssm-ID: 396441 [Multi-domain] Cd Length: 271 Bit Score: 85.48 E-value: 2.32e-19
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| ASKHA_NBD_DdNAGK-like | cd24081 | nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ... |
6-240 | 2.02e-15 | |||||
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; The family includes a group of uncharacterized proteins similar to Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK). NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, into GlcNAc 6-phosphate. It also has ManNAc kinase activity. Pssm-ID: 466931 [Multi-domain] Cd Length: 311 Bit Score: 75.05 E-value: 2.02e-15
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| ASKHA_NBD_NAGK_meta | cd24078 | nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
4-226 | 1.60e-13 | |||||
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. Members in this family are mainly from metazoa. Pssm-ID: 466928 [Multi-domain] Cd Length: 314 Bit Score: 69.53 E-value: 1.60e-13
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| ASKHA_NBD_PG1100-like | cd24079 | nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine ... |
4-247 | 1.20e-12 | |||||
nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine kinase (PG1100) and similar proteins; The family includes a group of uncharacterized proteins similar to Porphyromonas gingivalis putative N-acetylglucosamine kinase (PG1100; EC 2.7.1.59), which may convert GlcNAc to GlcNAc-6-phosphate, a component utilized in UDP-GlcNAc biosynthesis or energy metabolism. Pssm-ID: 466929 [Multi-domain] Cd Length: 276 Bit Score: 66.47 E-value: 1.20e-12
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| ASKHA_NBD_FGGY | cd00366 | nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-90 | 7.34e-06 | |||||
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains. Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 46.79 E-value: 7.34e-06
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| XylB | COG1070 | Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
4-78 | 1.10e-05 | |||||
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 46.36 E-value: 1.10e-05
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| NagC | COG1940 | Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-76 | 2.25e-05 | |||||
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription]; Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 45.27 E-value: 2.25e-05
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| ASKHA_NBD_FGGY_YgcE-like | cd07779 | nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-68 | 3.86e-05 | |||||
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They 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: 466798 [Multi-domain] Cd Length: 433 Bit Score: 44.82 E-value: 3.86e-05
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| ASKHA_NBD_FGGY_EcLyxK-like | cd07802 | nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-81 | 4.77e-05 | |||||
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA 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: 466805 [Multi-domain] Cd Length: 444 Bit Score: 44.46 E-value: 4.77e-05
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| ASKHA_ATPase_ROK | cd23763 | ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-77 | 1.69e-04 | |||||
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong 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: 466849 [Multi-domain] Cd Length: 239 Bit Score: 42.07 E-value: 1.69e-04
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| ASKHA_NBD_FGGY_BaXK-like | cd07809 | nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
4-78 | 9.64e-04 | |||||
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. 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: 466809 [Multi-domain] Cd Length: 443 Bit Score: 40.23 E-value: 9.64e-04
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| ASKHA_NBD_FGGY_YoaC-like | cd07798 | nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-68 | 2.32e-03 | |||||
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. 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: 466804 [Multi-domain] Cd Length: 448 Bit Score: 39.13 E-value: 2.32e-03
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| ASKHA_NBD_FGGY_EcXK-like | cd07808 | nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-78 | 5.67e-03 | |||||
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. 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: 466808 [Multi-domain] Cd Length: 482 Bit Score: 37.90 E-value: 5.67e-03
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| ASKHA_NBD_FGGY_FK | cd07773 | nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-69 | 6.34e-03 | |||||
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs 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: 466793 [Multi-domain] Cd Length: 443 Bit Score: 37.95 E-value: 6.34e-03
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| FGGY_N | pfam00370 | FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-76 | 7.53e-03 | |||||
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain. Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 37.32 E-value: 7.53e-03
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