acetylglutamate kinase [Clostridioides difficile]
Protein Classification
acetylglutamate kinase( domain architecture ID 10136258)
acetylglutamate kinase catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate to form N-acetyl-L-glutamate 5-phosphate, which is the second step of arginine biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| AAK_NAGK-C | cd04250 | AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
9-281 | 1.35e-152 | |||||
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK). : Pssm-ID: 239783 [Multi-domain] Cd Length: 279 Bit Score: 427.31 E-value: 1.35e-152
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| Name | Accession | Description | Interval | E-value | |||||
| AAK_NAGK-C | cd04250 | AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
9-281 | 1.35e-152 | |||||
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239783 [Multi-domain] Cd Length: 279 Bit Score: 427.31 E-value: 1.35e-152
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| ArgB | COG0548 | N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
3-282 | 1.52e-152 | |||||
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440314 [Multi-domain] Cd Length: 283 Bit Score: 427.14 E-value: 1.52e-152
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| PRK00942 | PRK00942 | acetylglutamate kinase; Provisional |
4-284 | 2.86e-151 | |||||
acetylglutamate kinase; Provisional Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 424.14 E-value: 2.86e-151
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| argB | TIGR00761 | acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
24-258 | 3.71e-84 | |||||
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 273256 [Multi-domain] Cd Length: 231 Bit Score: 252.20 E-value: 3.71e-84
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| AA_kinase | pfam00696 | Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
23-260 | 2.02e-48 | |||||
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2. Pssm-ID: 395565 [Multi-domain] Cd Length: 232 Bit Score: 160.61 E-value: 2.02e-48
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| Name | Accession | Description | Interval | E-value | ||||||
| AAK_NAGK-C | cd04250 | AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the ... |
9-281 | 1.35e-152 | ||||||
AAK_NAGK-C: N-Acetyl-L-glutamate kinase - cyclic (NAGK-C) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in some bacteria and photosynthetic organisms using the non-acetylated, cyclic route of ornithine biosynthesis. In this pathway, glutamate is first N-acetylated and then phosphorylated by NAGK to give phosphoryl NAG, which is converted to NAG-ornithine. There are two variants of this pathway. In one, typified by the pathway in Thermotoga maritima and Pseudomonas aeruginosa, the acetyl group is recycled by reversible transacetylation from acetylornithine to glutamate. The phosphorylation of NAG by NAGK is feedback inhibited by arginine. In photosynthetic organisms, NAGK is the target of the nitrogen-signaling protein PII. Hexameric formation of NAGK domains appears to be essential to both arginine inhibition and NAGK-PII complex formation. NAGK-C are members of the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239783 [Multi-domain] Cd Length: 279 Bit Score: 427.31 E-value: 1.35e-152
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| ArgB | COG0548 | N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is ... |
3-282 | 1.52e-152 | ||||||
N-acetylglutamate kinase [Amino acid transport and metabolism]; N-acetylglutamate kinase is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440314 [Multi-domain] Cd Length: 283 Bit Score: 427.14 E-value: 1.52e-152
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| PRK00942 | PRK00942 | acetylglutamate kinase; Provisional |
4-284 | 2.86e-151 | ||||||
acetylglutamate kinase; Provisional Pssm-ID: 234869 [Multi-domain] Cd Length: 283 Bit Score: 424.14 E-value: 2.86e-151
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| AAK_NAGK-like | cd04238 | AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
25-281 | 5.17e-134 | ||||||
AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the Escherichia coli and Pseudomonas aeruginosa type NAGKs which catalyze the phosphorylation of N-acetyl-L-glutamate (NAG) by ATP in the second step of arginine biosynthesis found in bacteria and photosynthetic organisms using either the acetylated, noncyclic (NC), or non-acetylated, cyclic (C) route of ornithine biosynthesis. Also included in this CD is a distinct group of uncharacterized (UC) bacterial and archeal NAGKs. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239771 [Multi-domain] Cd Length: 256 Bit Score: 379.55 E-value: 5.17e-134
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| PLN02512 | PLN02512 | acetylglutamate kinase |
3-282 | 1.67e-128 | ||||||
acetylglutamate kinase Pssm-ID: 178128 Cd Length: 309 Bit Score: 367.48 E-value: 1.67e-128
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| argB | CHL00202 | acetylglutamate kinase; Provisional |
3-281 | 5.45e-106 | ||||||
acetylglutamate kinase; Provisional Pssm-ID: 133644 [Multi-domain] Cd Length: 284 Bit Score: 309.41 E-value: 5.45e-106
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| argB | TIGR00761 | acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
24-258 | 3.71e-84 | ||||||
acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many prokaryotes and the N-acetylglutamate kinase domains of multifunctional proteins from yeasts. This enzyme is the second step in the "acetylated" ornithine biosynthesis pathway. A related group of enzymes representing the first step of the pathway contain a homologous domain and are excluded from this model. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 273256 [Multi-domain] Cd Length: 231 Bit Score: 252.20 E-value: 3.71e-84
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| PRK14058 | PRK14058 | [LysW]-aminoadipate/[LysW]-glutamate kinase; |
24-284 | 4.73e-65 | ||||||
[LysW]-aminoadipate/[LysW]-glutamate kinase; Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 204.75 E-value: 4.73e-65
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| AAK_NAGS-ABP | cd04237 | AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ... |
12-281 | 5.93e-54 | ||||||
AAK_NAGS-ABP: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. Domain architecture of these NAGS consisted of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences in this CD have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239770 [Multi-domain] Cd Length: 280 Bit Score: 176.59 E-value: 5.93e-54
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| PRK05279 | PRK05279 | N-acetylglutamate synthase; Validated |
12-285 | 2.30e-51 | ||||||
N-acetylglutamate synthase; Validated Pssm-ID: 235386 [Multi-domain] Cd Length: 441 Bit Score: 174.18 E-value: 2.30e-51
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| AAK_NAGK-NC | cd04249 | AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ... |
25-281 | 2.13e-50 | ||||||
AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis using the acetylated, noncyclic route of ornithine biosynthesis. There are two variants of this pathway. In one, typified by the pathway in Escherichia coli, glutamate is acetylated by acetyl-CoA and acetylornithine is deacylated hydrolytically. In this pathway, feedback inhibition by arginine occurs at the initial acetylation of glutamate and not at the phosphorylation of NAG by NAGK. Homodimeric NAGK-NC are members of the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239782 [Multi-domain] Cd Length: 252 Bit Score: 166.43 E-value: 2.13e-50
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| AA_kinase | pfam00696 | Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
23-260 | 2.02e-48 | ||||||
Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino acid substrates, as well as uridylate kinase and carbamate kinase. This family includes: Aspartokinase EC:2.7.2.4. Acetylglutamate kinase EC:2.7.2.8. Glutamate 5-kinase EC:2.7.2.11. Uridylate kinase EC:2.7.4.-. Carbamate kinase EC:2.7.2.2. Pssm-ID: 395565 [Multi-domain] Cd Length: 232 Bit Score: 160.61 E-value: 2.02e-48
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| AAK_NAGK-UC | cd04251 | AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
25-281 | 2.41e-47 | ||||||
AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar to Escherichia coli and Pseudomonas aeruginosa NAGKs which catalyze the phosphorylation of the gamma-COOH group of N-acetyl-L-glutamate (NAG) by ATP in the second step of microbial arginine biosynthesis. These uncharacterized domain sequences are found in some bacteria (Deinococci and Chloroflexi) and archea and belong to the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239784 [Multi-domain] Cd Length: 257 Bit Score: 158.69 E-value: 2.41e-47
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| AAK_NAGK-fArgBP | cd04252 | AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic ... |
26-281 | 7.19e-43 | ||||||
AAK_NAGK-fArgBP: N-Acetyl-L-glutamate kinase (NAGK) of the fungal arginine-biosynthetic pathway (fArgBP). The nuclear-encoded, mitochondrial polyprotein precursor with an N-terminal NAGK (ArgB) domain (this CD), a central DUF619 domain, and a C-terminal reductase domain (ArgC, N-Acetylglutamate Phosphate Reductase, NAGPR). The precursor is cleaved in the mitochondria into two distinct enzymes (NAGK-DUF619 and NAGPR). Native molecular weights of these proteins indicate that the kinase is an octamer whereas the reductase is a dimer. This CD also includes some gamma-proteobacteria (Xanthomonas and Xylella) NAG kinases with an N-terminal NAGK (ArgB) domain (this CD) and a C-terminal DUF619 domain. The DUF619 domain is described as a putative distant homolog of the acetyltransferase, ArgA, predicted to function in NAG synthase association in fungi. Eukaryotic sequences have an N-terminal mitochondrial transit peptide. Members of this NAG kinase domain CD belong to the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239785 [Multi-domain] Cd Length: 248 Bit Score: 147.14 E-value: 7.19e-43
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| N-Ac-Glu-synth | TIGR01890 | amino-acid N-acetyltransferase; This model represents a clade of amino-acid ... |
8-284 | 1.81e-40 | ||||||
amino-acid N-acetyltransferase; This model represents a clade of amino-acid N-acetyltransferases acting mainly on glutamate in the first step of the "acetylated" ornithine biosynthesis pathway. For this reason it is also called N-acetylglutamate synthase. The enzyme may also act on aspartate. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 273856 [Multi-domain] Cd Length: 429 Bit Score: 145.32 E-value: 1.81e-40
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| AAK | cd02115 | Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
26-281 | 6.82e-38 | ||||||
Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like N-acetylglutamate kinase (NAGK), carbamate kinase (CK), aspartokinase (AK), glutamate-5-kinase (G5K) and UMP kinase (UMPK). The AAK superfamily includes kinases that phosphorylate a variety of amino acid substrates. These kinases catalyze the formation of phosphoric anhydrides, generally with a carboxylate, and use ATP as the source of the phosphoryl group; are involved in amino acid biosynthesis. Some of these kinases control the process via allosteric feed-back inhibition. Pssm-ID: 239033 [Multi-domain] Cd Length: 248 Bit Score: 134.11 E-value: 6.82e-38
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| PRK04531 | PRK04531 | acetylglutamate kinase; Provisional |
27-285 | 3.81e-30 | ||||||
acetylglutamate kinase; Provisional Pssm-ID: 235306 [Multi-domain] Cd Length: 398 Bit Score: 117.07 E-value: 3.81e-30
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| PLN02825 | PLN02825 | amino-acid N-acetyltransferase |
12-281 | 1.05e-24 | ||||||
amino-acid N-acetyltransferase Pssm-ID: 215441 [Multi-domain] Cd Length: 515 Bit Score: 102.93 E-value: 1.05e-24
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| AAK_FomA-like | cd04241 | AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
24-281 | 3.07e-17 | ||||||
AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar proteins found in a wide range of organisms. Together, the fomA and fomB genes in the fosfomycin biosynthetic gene cluster of Streptomyces wedmorensis confer high-level fosfomycin resistance. FomA and FomB proteins converted fosfomycin to fosfomycin monophosphate and fosfomycin diphosphate in the presence of ATP and a magnesium ion, indicating that FomA and FomB catalyzed phosphorylations of fosfomycin and fosfomycin monophosphate, respectively. FomA and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239774 [Multi-domain] Cd Length: 252 Bit Score: 79.23 E-value: 3.07e-17
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| AAK_G5K_ProB | cd04242 | AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
182-282 | 2.09e-11 | ||||||
AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (and, in mammals, ornithine) biosynthesis. G5K is subject to feedback allosteric inhibition by proline or ornithine. In microorganisms and plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Microbial G5K generally consists of two domains: a catalytic G5K domain and one PUA (pseudo uridine synthases and archaeosine-specific transglycosylases) domain, and some lack the PUA domain. G5K requires free Mg for activity, it is tetrameric, and it aggregates to higher forms in a proline-dependent way. G5K lacking the PUA domain remains tetrameric, active, and proline-inhibitable, but the Mg requirement and the proline-triggered aggregation are greatly diminished and abolished, respectively, and more proline is needed for inhibition. Although plant and animal G5Ks are part of a bifunctional polypeptide, delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR; ProA); bacterial and yeast G5Ks are monofunctional single-polypeptide enzymes. In this CD, all three domain architectures are present: G5K, G5K+PUA, and G5K+G5PR. Pssm-ID: 239775 [Multi-domain] Cd Length: 251 Bit Score: 62.46 E-value: 2.09e-11
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| AAK_CK | cd04235 | AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
151-258 | 1.12e-09 | ||||||
AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and carbamoyl phosphate (CP) utilization with the production of ATP from ADP and CP. Both CK (this CD) and nonhomologous CP synthetase synthesize carbamoyl phosphate, an essential precursor of arginine and pyrimidine bases, in the presence of ATP, bicarbonate, and ammonia. CK is a homodimer of 33 kDa subunits and is a member of the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239768 Cd Length: 308 Bit Score: 57.91 E-value: 1.12e-09
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| AAK_NAGS-Urea | cd04236 | AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the ... |
71-280 | 4.06e-09 | ||||||
AAK_NAGS-Urea: N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the urea cycle found in animals. Ureogenic NAGS is a mitochondrial enzyme catalyzing the formation of NAG from acetylcoenzyme A and L-glutamate; NAG is an essential allosteric activator of carbamylphosphate synthase I, the first and rate limiting enzyme of the urea cycle. Ureogenic NAGS activity is dependent on the concentration of glutamate (substrate) and arginine (activator). Domain architecture of ureogenic NAGS consists of an N-terminal NAG kinase-like (ArgB) domain (this CD) and a C-terminal DUF619 domain. Members of this CD belong to the protein superfamily, the Amino Acid Kinase Family (AAKF). Pssm-ID: 239769 [Multi-domain] Cd Length: 271 Bit Score: 56.00 E-value: 4.06e-09
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| ArcC | COG0549 | Carbamate kinase [Amino acid transport and metabolism]; |
148-258 | 6.46e-09 | ||||||
Carbamate kinase [Amino acid transport and metabolism]; Pssm-ID: 440315 Cd Length: 313 Bit Score: 55.85 E-value: 6.46e-09
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| PRK12353 | PRK12353 | putative amino acid kinase; Reviewed |
145-283 | 1.15e-08 | ||||||
putative amino acid kinase; Reviewed Pssm-ID: 237071 Cd Length: 314 Bit Score: 55.16 E-value: 1.15e-08
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| PRK12454 | PRK12454 | carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
148-260 | 4.00e-08 | ||||||
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed Pssm-ID: 183535 Cd Length: 313 Bit Score: 53.46 E-value: 4.00e-08
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| AAK_P5CS_ProBA | cd04256 | AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
182-280 | 4.61e-08 | ||||||
AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta 1-pyrroline-5-carboxylate synthetase (P5CS), composed of an N-terminal G5K (ProB) and a C-terminal glutamyl 5- phosphate reductase (G5PR, ProA), the first and second enzyme catalyzing proline (and, in mammals, ornithine) biosynthesis. G5K transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, and is subject to feedback allosteric inhibition by proline or ornithine. In plants, proline plays an important role as an osmoprotectant and, in mammals, ornithine biosynthesis is crucial for proper ammonia detoxification, since a G5K mutation has been shown to cause human hyperammonaemia. Pssm-ID: 239789 [Multi-domain] Cd Length: 284 Bit Score: 53.20 E-value: 4.61e-08
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| AAK_AK-DapG-like | cd04246 | AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the ... |
93-205 | 1.07e-07 | ||||||
AAK_AK-DapG-like: Amino Acid Kinase Superfamily (AAK), AK-DapG-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional enzymes found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species, as well as, the catalytic AK domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related isoenzymes. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. The role of the AKI isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. In Corynebacterium glutamicum and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinase isoenzyme types found in Pseudomonas, C. glutamicum, and Amycolatopsis lactamdurans. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. The B. subtilis 168 AKII aspartokinase is also described as tetrameric consisting of two alpha and two beta subunits. Some archeal aspartokinases in this group lack recognizable ACT domains. Pssm-ID: 239779 [Multi-domain] Cd Length: 239 Bit Score: 51.73 E-value: 1.07e-07
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| AAK_AKi-DapG-BS | cd04260 | AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ... |
107-207 | 3.64e-07 | ||||||
AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the diaminopimelate-sensitive aspartokinase isoenzyme AKI (DapG), a monofunctional class enzyme found in Bacilli (Bacillus subtilis 168), Clostridia, and Actinobacteria bacterial species. In Bacillus subtilis, the regulation of the diaminopimelate-lysine biosynthetic pathway involves dual control by diaminopimelate and lysine, effected through separate diaminopimelate- and lysine-sensitive aspartokinase isoenzymes. AKI activity is invariant during the exponential and stationary phases of growth and is not altered by addition of amino acids to the growth medium. The role of this isoenzyme is most likely to provide a constant level of aspartyl-beta-phosphate for the biosynthesis of diaminopimelate for peptidoglycan synthesis and dipicolinate during sporulation. The B. subtilis AKI is tetrameric consisting of two alpha and two beta subunits; the alpha (43 kD) and beta (17 kD) subunit formed by two in-phase overlapping genes. The alpha subunit contains the AK catalytic domain and two ACT domains. The beta subunit contains two ACT domains. Pssm-ID: 239793 [Multi-domain] Cd Length: 244 Bit Score: 50.08 E-value: 3.64e-07
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| AAK_AKii-LysC-BS | cd04261 | AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal ... |
111-205 | 1.08e-06 | ||||||
AAK_AKii-LysC-BS: Amino Acid Kinase Superfamily (AAK), AKii; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive aspartokinase isoenzymes. The B. subtilis 168 AKII is induced by methionine, and repressed and inhibited by lysine. Although Corynebacterium glutamicum is known to contain a single aspartokinase isoenzyme type, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In this organism and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and theronine. Also included in this CD are the aspartokinases of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single aspartokinases found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans aspartokinases are described as tetramers consisting of two alpha and two beta subunits; the alpha (44 kD) and beta (18 kD) subunits formed by two in-phase overlapping polypeptides. Pssm-ID: 239794 [Multi-domain] Cd Length: 239 Bit Score: 48.68 E-value: 1.08e-06
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| PRK12686 | PRK12686 | carbamate kinase; Reviewed |
148-283 | 2.04e-06 | ||||||
carbamate kinase; Reviewed Pssm-ID: 183683 Cd Length: 312 Bit Score: 48.11 E-value: 2.04e-06
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| PRK12354 | PRK12354 | carbamate kinase; Reviewed |
148-258 | 3.46e-06 | ||||||
carbamate kinase; Reviewed Pssm-ID: 183466 Cd Length: 307 Bit Score: 47.52 E-value: 3.46e-06
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| PLN02418 | PLN02418 | delta-1-pyrroline-5-carboxylate synthase |
182-284 | 3.96e-06 | ||||||
delta-1-pyrroline-5-carboxylate synthase Pssm-ID: 215230 Cd Length: 718 Bit Score: 47.80 E-value: 3.96e-06
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| P5CS | TIGR01092 | delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
180-284 | 2.34e-05 | ||||||
delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, EC 2.7.2.11) region followed by a gamma-glutamyl phosphate reductase (ProA, EC 1.2.1.41) region. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 130164 [Multi-domain] Cd Length: 715 Bit Score: 45.67 E-value: 2.34e-05
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| AAK_AK | cd04234 | AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ... |
145-205 | 1.45e-04 | ||||||
AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the N-terminal catalytic domain of aspartokinase (4-L-aspartate-4-phosphotransferase;). AK is the first enzyme in the biosynthetic pathway of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. It also catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. One mechanism for the regulation of this pathway is by the production of several isoenzymes of aspartokinase with different repressors and allosteric inhibitors. Pairs of ACT domains are proposed to specifically bind amino acids leading to allosteric regulation of the enzyme. In Escherichia coli, three different aspartokinase isoenzymes are regulated specifically by lysine, methionine, and threonine. AK-HSDHI (ThrA) and AK-HSDHII (MetL) are bifunctional enzymes that consist of an N-terminal AK and a C-terminal homoserine dehydrogenase (HSDH). ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. The third isoenzyme, AKIII (LysC), is monofunctional and is involved in lysine synthesis. The three Bacillus subtilis isoenzymes, AKI (DapG), AKII (LysC), and AKIII (YclM), are feedback-inhibited by meso-diaminopimelate, lysine, and lysine plus threonine, respectively. The E. coli lysine-sensitive AK is described as a homodimer, whereas, the B. subtilis lysine-sensitive AK is described as a heterodimeric complex of alpha- and beta- subunits that are formed from two in-frame overlapping genes. A single AK enzyme type has been described in Pseudomonas, Amycolatopsis, and Corynebacterium. The fungal aspartate pathway is regulated at the AK step, with L-Thr being an allosteric inhibitor of the Saccharomyces cerevisiae AK (Hom3). At least two distinct AK isoenzymes can occur in higher plants, one is a monofunctional lysine-sensitive isoenzyme, which is involved in the overall regulation of the pathway and can be synergistically inhibited by S-adenosylmethionine. The other isoenzyme is a bifunctional, threonine-sensitive AK-HSDH protein. Also included in this CD is the catalytic domain of the Methylomicrobium alcaliphilum ectoine AK, the first enzyme of the ectoine biosynthetic pathway, found in this bacterium, and several other halophilic/halotolerant bacteria. Pssm-ID: 239767 [Multi-domain] Cd Length: 227 Bit Score: 42.08 E-value: 1.45e-04
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| MetL1 | COG0527 | Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ... |
151-205 | 1.07e-03 | ||||||
Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the Pathway/BioSystem: Lysine biosynthesis Pssm-ID: 440293 [Multi-domain] Cd Length: 407 Bit Score: 40.07 E-value: 1.07e-03
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| PRK09411 | PRK09411 | carbamate kinase; Reviewed |
146-202 | 1.26e-03 | ||||||
carbamate kinase; Reviewed Pssm-ID: 181831 Cd Length: 297 Bit Score: 39.78 E-value: 1.26e-03
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| AAK_UC | cd04240 | AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few ... |
26-281 | 1.71e-03 | ||||||
AAK_UC: Uncharacterized (UC) amino acid kinase-like proteins found mainly in archaea and a few bacteria. Sequences in this CD are members of the Amino Acid Kinase (AAK) superfamily. Pssm-ID: 239773 [Multi-domain] Cd Length: 203 Bit Score: 38.88 E-value: 1.71e-03
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| PRK12314 | PRK12314 | gamma-glutamyl kinase; Provisional |
182-285 | 1.86e-03 | ||||||
gamma-glutamyl kinase; Provisional Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 39.07 E-value: 1.86e-03
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| PRK06635 | PRK06635 | aspartate kinase; Reviewed |
145-205 | 6.12e-03 | ||||||
aspartate kinase; Reviewed Pssm-ID: 235843 [Multi-domain] Cd Length: 404 Bit Score: 37.79 E-value: 6.12e-03
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| PRK07431 | PRK07431 | aspartate kinase; Provisional |
145-207 | 7.33e-03 | ||||||
aspartate kinase; Provisional Pssm-ID: 236018 [Multi-domain] Cd Length: 587 Bit Score: 37.59 E-value: 7.33e-03
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