glutamate 5-kinase [Bacillus cereus]
Protein Classification
glutamate 5-kinase( domain architecture ID 11415724)
glutamate 5-kinase catalyzes glutamate-dependent ATP cleavage, and transfers the terminal phosphoryl group of ATP to the gamma-carboxyl group of glutamate, in the first and controlling step of proline (or ornithine) biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| ProB | COG0263 | Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
2-367 | 0e+00 | ||||||
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis : Pssm-ID: 440033 [Multi-domain] Cd Length: 371 Bit Score: 535.39 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| ProB | COG0263 | Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
2-367 | 0e+00 | ||||||
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis Pssm-ID: 440033 [Multi-domain] Cd Length: 371 Bit Score: 535.39 E-value: 0e+00
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| proB | TIGR01027 | glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
4-365 | 4.06e-162 | ||||||
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 162163 [Multi-domain] Cd Length: 363 Bit Score: 458.31 E-value: 4.06e-162
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| AAK_G5K_ProB | cd04242 | AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
5-253 | 3.98e-132 | ||||||
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: 377.55 E-value: 3.98e-132
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| PRK12314 | PRK12314 | gamma-glutamyl kinase; Provisional |
1-260 | 2.03e-95 | ||||||
gamma-glutamyl kinase; Provisional Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 285.21 E-value: 2.03e-95
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| AA_kinase | pfam00696 | Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
4-232 | 2.32e-43 | ||||||
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: 150.21 E-value: 2.32e-43
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| PUA | smart00359 | Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
277-341 | 5.01e-12 | ||||||
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 60.73 E-value: 5.01e-12
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| IPPK_Arch | NF040647 | isopentenyl phosphate kinase; |
161-232 | 1.20e-07 | ||||||
isopentenyl phosphate kinase; Pssm-ID: 468614 [Multi-domain] Cd Length: 258 Bit Score: 52.22 E-value: 1.20e-07
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| Name | Accession | Description | Interval | E-value | ||||||
| ProB | COG0263 | Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
2-367 | 0e+00 | ||||||
Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the Pathway/BioSystem: Proline biosynthesis Pssm-ID: 440033 [Multi-domain] Cd Length: 371 Bit Score: 535.39 E-value: 0e+00
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| proB | TIGR01027 | glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ... |
4-365 | 4.06e-162 | ||||||
glutamate 5-kinase; Bacterial ProB proteins hit the full length of this model, but the ProB-like domain of delta 1-pyrroline-5-carboxylate synthetase does not hit the C-terminal 100 residues of this model. The noise cutoff is set low enough to hit delta 1-pyrroline-5-carboxylate synthetase and other partial matches to this family. [Amino acid biosynthesis, Glutamate family] Pssm-ID: 162163 [Multi-domain] Cd Length: 363 Bit Score: 458.31 E-value: 4.06e-162
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| AAK_G5K_ProB | cd04242 | AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
5-253 | 3.98e-132 | ||||||
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: 377.55 E-value: 3.98e-132
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| PRK12314 | PRK12314 | gamma-glutamyl kinase; Provisional |
1-260 | 2.03e-95 | ||||||
gamma-glutamyl kinase; Provisional Pssm-ID: 183430 [Multi-domain] Cd Length: 266 Bit Score: 285.21 E-value: 2.03e-95
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| AAK_P5CS_ProBA | cd04256 | AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
4-253 | 2.05e-51 | ||||||
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: 172.62 E-value: 2.05e-51
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| PTZ00489 | PTZ00489 | glutamate 5-kinase; Provisional |
4-247 | 6.84e-45 | ||||||
glutamate 5-kinase; Provisional Pssm-ID: 240438 [Multi-domain] Cd Length: 264 Bit Score: 155.17 E-value: 6.84e-45
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| PUA_G5K | cd21157 | PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl ... |
266-365 | 1.77e-43 | ||||||
PUA domain of gamma-glutamyl kinase, found in archaea, bacteria, and eukarya; Gamma glutamyl kinase (G5K) is an enzyme essential for the biosynthesis of L-proline; it catalyzes the transfer of a phosphate group to glutamate. The resulting glutamate 5-phosphate cyclizes spontaneously to form 5-oxoproline. The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain functions as an RNA binding domain in many other proteins; however, its role in G5K is not understood. It might play a role in modulating the enzymatic properties of bacterial G5Ks. Pssm-ID: 409299 [Multi-domain] Cd Length: 104 Bit Score: 146.07 E-value: 1.77e-43
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| AA_kinase | pfam00696 | Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
4-232 | 2.32e-43 | ||||||
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: 150.21 E-value: 2.32e-43
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| PLN02418 | PLN02418 | delta-1-pyrroline-5-carboxylate synthase |
4-252 | 2.94e-42 | ||||||
delta-1-pyrroline-5-carboxylate synthase Pssm-ID: 215230 Cd Length: 718 Bit Score: 156.81 E-value: 2.94e-42
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| P5CS | TIGR01092 | delta l-pyrroline-5-carboxylate synthetase; This protein contains a glutamate 5-kinase (ProB, ... |
4-253 | 4.07e-41 | ||||||
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: 153.53 E-value: 4.07e-41
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| AAK | cd02115 | Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
7-254 | 9.37e-27 | ||||||
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: 106.76 E-value: 9.37e-27
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| PUA | pfam01472 | PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, ... |
277-347 | 5.36e-17 | ||||||
PUA domain; The PUA domain named after Pseudouridine synthase and Archaeosine transglycosylase, was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was detected also in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in the regulation of the expression of other genes. It is predicted that the PUA domain is an RNA binding domain. Pssm-ID: 426278 [Multi-domain] Cd Length: 74 Bit Score: 74.83 E-value: 5.36e-17
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| AAK_UMPK-like | cd04239 | AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
5-255 | 4.62e-12 | ||||||
AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis. Regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinases of E. coli (Ec) and Pyrococcus furiosus (Pf) are known to function as homohexamers, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Also included in this CD are the alpha and beta subunits of the Mo storage protein (MosA and MosB) characterized as an alpha4-beta4 octamer containing an ATP-dependent, polynuclear molybdenum-oxide cluster. These and related sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239772 [Multi-domain] Cd Length: 229 Bit Score: 64.87 E-value: 4.62e-12
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| PUA | smart00359 | Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; |
277-341 | 5.01e-12 | ||||||
Putative RNA-binding Domain in PseudoUridine synthase and Archaeosine transglycosylase; Pssm-ID: 214635 [Multi-domain] Cd Length: 76 Bit Score: 60.73 E-value: 5.01e-12
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| AAK_UMPK-PyrH-Pf | cd04253 | AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
149-255 | 2.49e-10 | ||||||
AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase (uridylate kinase) enzymes that catalyze UMP phosphorylation and play a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of Pyrococcus furiosus (Pf) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial UMPKs have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs (this CD) appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239786 [Multi-domain] Cd Length: 221 Bit Score: 59.57 E-value: 2.49e-10
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| AAK_FomA-like | cd04241 | AAK_FomA-like: This CD includes a fosfomycin biosynthetic gene product, FomA, and similar ... |
5-252 | 2.01e-09 | ||||||
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: 57.66 E-value: 2.01e-09
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| PRK14058 | PRK14058 | [LysW]-aminoadipate/[LysW]-glutamate kinase; |
147-249 | 1.54e-08 | ||||||
[LysW]-aminoadipate/[LysW]-glutamate kinase; Pssm-ID: 237599 [Multi-domain] Cd Length: 268 Bit Score: 54.91 E-value: 1.54e-08
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| IPPK_Arch | NF040647 | isopentenyl phosphate kinase; |
161-232 | 1.20e-07 | ||||||
isopentenyl phosphate kinase; Pssm-ID: 468614 [Multi-domain] Cd Length: 258 Bit Score: 52.22 E-value: 1.20e-07
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| PUA | cd07953 | PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) ... |
279-337 | 2.54e-07 | ||||||
PUA RNA binding domain; The PUA (PseudoUridine synthase and Archaeosine transglycosylase) domain was detected in archaeal and eukaryotic pseudouridine synthases, archaeal archaeosine synthases, a family of predicted ATPases that may be involved in RNA modification, and a family of predicted archaeal and bacterial rRNA methylases. Additionally, the PUA domain was detected in a family of eukaryotic proteins that also contain a domain homologous to the translation initiation factor eIF1/SUI1; these proteins may comprise a novel type of translation factors. Unexpectedly, the PUA domain was also found in bacterial and yeast glutamate kinases; this is compatible with the demonstrated role of these enzymes in regulating the expression of other genes. It has been shown that the PUA domain acts as an RNA binding domain in at least some of the proteins involved in RNA metabolism. Pssm-ID: 409289 [Multi-domain] Cd Length: 73 Bit Score: 47.68 E-value: 2.54e-07
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| AAK_NAGK-NC | cd04249 | AAK_NAGK-NC: N-Acetyl-L-glutamate kinase - noncyclic (NAGK-NC) catalyzes the phosphorylation ... |
114-252 | 1.50e-06 | ||||||
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: 48.95 E-value: 1.50e-06
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| AAK_NAGK-UC | cd04251 | AAK_NAGK-UC: N-Acetyl-L-glutamate kinase - uncharacterized (NAGK-UC). This domain is similar ... |
147-249 | 1.74e-06 | ||||||
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: 48.90 E-value: 1.74e-06
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| AAK_AK | cd04234 | AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ... |
5-207 | 1.99e-06 | ||||||
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: 48.24 E-value: 1.99e-06
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| PRK12454 | PRK12454 | carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
129-254 | 1.01e-04 | ||||||
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed Pssm-ID: 183535 Cd Length: 313 Bit Score: 43.83 E-value: 1.01e-04
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| MetL1 | COG0527 | Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ... |
5-201 | 1.14e-04 | ||||||
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: 43.92 E-value: 1.14e-04
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| AAK_NAGK-like | cd04238 | AAK_NAGK-like: N-Acetyl-L-glutamate kinase (NAGK)-like . Included in this CD are the ... |
149-252 | 2.50e-04 | ||||||
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: 42.11 E-value: 2.50e-04
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| AAK_CK | cd04235 | AAK_CK: Carbamate kinase (CK) catalyzes both the ATP-phosphorylation of carbamate and ... |
147-252 | 1.02e-03 | ||||||
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: 40.57 E-value: 1.02e-03
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| PyrH | COG0528 | Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ... |
161-187 | 1.48e-03 | ||||||
Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 440294 [Multi-domain] Cd Length: 238 Bit Score: 39.61 E-value: 1.48e-03
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| AAK_UMPK-PyrH-Ec | cd04254 | UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ... |
161-187 | 2.87e-03 | ||||||
UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) enzyme that catalyzes UMP phosphorylation and plays a key role in pyrimidine nucleotide biosynthesis; regulation of this process is via feed-back control and via gene repression of carbamoyl phosphate synthetase (the first enzyme of the pyrimidine biosynthesis pathway). The UMP kinase of E. coli (Ec) is known to function as a homohexamer, with GTP and UTP being allosteric effectors. Like other related enzymes (carbamate kinase, aspartokinase, and N-acetylglutamate kinase) the E. coli and most bacterial and chloroplast UMPKs (this CD) have a conserved, N-terminal, lysine residue proposed to function in the catalysis of the phosphoryl group transfer, whereas most archaeal UMPKs appear to lack this residue and the Pyrococcus furiosus structure has an additional Mg ion bound to the ATP molecule which is proposed to function as the catalysis instead. Members of this CD belong to the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239787 [Multi-domain] Cd Length: 231 Bit Score: 38.63 E-value: 2.87e-03
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| PRK05925 | PRK05925 | aspartate kinase; Provisional |
146-208 | 5.06e-03 | ||||||
aspartate kinase; Provisional Pssm-ID: 235646 [Multi-domain] Cd Length: 440 Bit Score: 38.64 E-value: 5.06e-03
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| argB | TIGR00761 | acetylglutamate kinase; This model describes N-acetylglutamate kinases (ArgB) of many ... |
118-229 | 6.19e-03 | ||||||
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: 37.65 E-value: 6.19e-03
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| AAK_AK-HSDH-like | cd04243 | AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the ... |
80-201 | 7.64e-03 | ||||||
AAK_AK-HSDH-like: Amino Acid Kinase Superfamily (AAK), AK-HSDH-like; this family includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK- homoserine dehydrogenase (HSDH). These aspartokinases are found in such bacteria as E. coli (AKI-HSDHI, ThrA and AKII-HSDHII, MetL) and in higher plants (Z. mays AK-HSDH). AK and HSDH are the first and third enzymes in the biosynthetic pathway of the aspartate family of amino acids. AK catalyzes the phosphorylation of Asp to P-aspartyl phosphate. HSDH catalyzes the NADPH-dependent conversion of Asp 3-semialdehyde to homoserine. ThrA and MetL are involved in threonine and methionine biosynthesis, respectively. In E. coli, ThrA is subject to allosteric regulation by the end product L-threonine and the native enzyme is reported to be tetrameric. As with bacteria, plant AK and HSDH are feedback inhibited by pathway end products. Maize AK-HSDH is a Thr-sensitive 180-kD enzyme. Arabidopsis AK-HSDH is an alanine-activated, threonine-sensitive enzyme whose ACT domains, located C-terminal to the AK catalytic domain, were shown to be involved in allosteric activation. Also included in this CD is the catalytic domain of the aspartokinase (AK) of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Also included in this CD is the catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine. Pssm-ID: 239776 [Multi-domain] Cd Length: 293 Bit Score: 37.92 E-value: 7.64e-03
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