hypothetical protein B1J91_J02882g [Nakaseomyces glabratus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| AAK super family | cl00452 | Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
10-324 | 0e+00 | |||||
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. The actual alignment was detected with superfamily member cd04247: Pssm-ID: 444912 [Multi-domain] Cd Length: 306 Bit Score: 547.80 E-value: 0e+00
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| PRK07431 super family | cl35582 | aspartate kinase; Provisional |
229-499 | 3.38e-36 | |||||
aspartate kinase; Provisional The actual alignment was detected with superfamily member PRK07431: Pssm-ID: 236018 [Multi-domain] Cd Length: 587 Bit Score: 141.98 E-value: 3.38e-36
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| Name | Accession | Description | Interval | E-value | ||||||||
| AAK_AK-Hom3 | cd04247 | AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ... |
10-324 | 0e+00 | ||||||||
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single aspartokinase isoenzyme type, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies show that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Pssm-ID: 239780 [Multi-domain] Cd Length: 306 Bit Score: 547.80 E-value: 0e+00
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| asp_kinases | TIGR00657 | aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ... |
10-501 | 1.87e-143 | ||||||||
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273201 [Multi-domain] Cd Length: 441 Bit Score: 420.22 E-value: 1.87e-143
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| MetL1 | COG0527 | Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ... |
10-500 | 1.22e-105 | ||||||||
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: 322.03 E-value: 1.22e-105
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| PRK09084 | PRK09084 | aspartate kinase III; Validated |
12-503 | 2.26e-91 | ||||||||
aspartate kinase III; Validated Pssm-ID: 236376 [Multi-domain] Cd Length: 448 Bit Score: 286.72 E-value: 2.26e-91
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| PRK07431 | PRK07431 | aspartate kinase; Provisional |
229-499 | 3.38e-36 | ||||||||
aspartate kinase; Provisional Pssm-ID: 236018 [Multi-domain] Cd Length: 587 Bit Score: 141.98 E-value: 3.38e-36
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| AA_kinase | pfam00696 | Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
10-310 | 1.61e-33 | ||||||||
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: 127.10 E-value: 1.61e-33
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| ACT_AK-Hom3_1 | cd04934 | CT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a ... |
362-435 | 9.09e-32 | ||||||||
CT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains; This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains. AK is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single AK, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies shown that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153206 Cd Length: 73 Bit Score: 116.79 E-value: 9.09e-32
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| ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
430-498 | 3.19e-05 | ||||||||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 41.75 E-value: 3.19e-05
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| Name | Accession | Description | Interval | E-value | ||||||||
| AAK_AK-Hom3 | cd04247 | AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal ... |
10-324 | 0e+00 | ||||||||
AAK_AK-Hom3: Amino Acid Kinase Superfamily (AAK), AK-Hom3; this CD includes the N-terminal catalytic domain of the aspartokinase HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae and other related AK domains. Aspartokinase, the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single aspartokinase isoenzyme type, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies show that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Pssm-ID: 239780 [Multi-domain] Cd Length: 306 Bit Score: 547.80 E-value: 0e+00
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| asp_kinases | TIGR00657 | aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys ... |
10-501 | 1.87e-143 | ||||||||
aspartate kinase; Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer.The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. This may be a feature of a number of closely related forms, including a paralog from B. subtilis. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273201 [Multi-domain] Cd Length: 441 Bit Score: 420.22 E-value: 1.87e-143
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| MetL1 | COG0527 | Aspartate kinase [Amino acid transport and metabolism]; Aspartate kinase is part of the ... |
10-500 | 1.22e-105 | ||||||||
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: 322.03 E-value: 1.22e-105
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| PRK09084 | PRK09084 | aspartate kinase III; Validated |
12-503 | 2.26e-91 | ||||||||
aspartate kinase III; Validated Pssm-ID: 236376 [Multi-domain] Cd Length: 448 Bit Score: 286.72 E-value: 2.26e-91
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| PRK06291 | PRK06291 | aspartate kinase; Provisional |
12-499 | 4.99e-87 | ||||||||
aspartate kinase; Provisional Pssm-ID: 235773 [Multi-domain] Cd Length: 465 Bit Score: 276.04 E-value: 4.99e-87
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| thrA | PRK09436 | bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional |
11-497 | 1.86e-84 | ||||||||
bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional Pssm-ID: 181856 [Multi-domain] Cd Length: 819 Bit Score: 278.58 E-value: 1.86e-84
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| AAK_AK | cd04234 | AAK_AK: Amino Acid Kinase Superfamily (AAK), Aspartokinase (AK); this CD includes the ... |
11-321 | 1.74e-74 | ||||||||
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: 235.45 E-value: 1.74e-74
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| PLN02551 | PLN02551 | aspartokinase |
12-518 | 8.02e-73 | ||||||||
aspartokinase Pssm-ID: 178166 [Multi-domain] Cd Length: 521 Bit Score: 240.79 E-value: 8.02e-73
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| asp_kin_monofn | TIGR00656 | aspartate kinase, monofunctional class; This model describes a subclass of aspartate kinases. ... |
12-500 | 1.29e-63 | ||||||||
aspartate kinase, monofunctional class; This model describes a subclass of aspartate kinases. These are mostly Lys-sensitive and not fused to homoserine dehydrogenase, unlike some Thr-sensitive and Met-sensitive forms. Homoserine dehydrogenase is part of Thr and Met but not Lys biosynthetic pathways. Aspartate kinase catalyzes a first step in the biosynthesis from Asp of Lys (and its precursor diaminopimelate), Met, and Thr. In E. coli, a distinct isozyme is inhibited by each of the three amino acid products. The Met-sensitive (I) and Thr-sensitive (II) forms are bifunctional enzymes fused to homoserine dehydrogenases and form homotetramers, while the Lys-sensitive form (III) is a monofunctional homodimer. The Lys-sensitive enzyme of Bacillus subtilis resembles the E. coli form but is an alpha 2/beta 2 heterotetramer, where the beta subunit is translated from an in-phase alternative initiator at Met-246. The protein slr0657 from Synechocystis PCC6803 is extended by a duplication of the C-terminal region corresponding to the beta chain. Incorporation of a second copy of the C-terminal domain may be quite common in this subgroup of aspartokinases. [Amino acid biosynthesis, Aspartate family] Pssm-ID: 273200 [Multi-domain] Cd Length: 400 Bit Score: 213.02 E-value: 1.29e-63
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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 ... |
11-321 | 2.30e-63 | ||||||||
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: 208.56 E-value: 2.30e-63
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| AAK_AK-LysC-like | cd04244 | AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the ... |
12-321 | 9.40e-61 | ||||||||
AAK_AK-LysC-like: Amino Acid Kinase Superfamily (AAK), AK-LysC-like; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive AK isoenzyme found in higher plants. The lysine-sensitive AK isoenzyme is a monofunctional protein. It is involved in the overall regulation of the aspartate pathway and can be synergistically inhibited by S-adenosylmethionine. Also included in this CD is an uncharacterized LysC-like AK found in Euryarchaeota and some bacteria. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Pssm-ID: 239777 [Multi-domain] Cd Length: 298 Bit Score: 202.22 E-value: 9.40e-61
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| PRK08961 | PRK08961 | bifunctional aspartate kinase/diaminopimelate decarboxylase; |
7-505 | 1.53e-58 | ||||||||
bifunctional aspartate kinase/diaminopimelate decarboxylase; Pssm-ID: 236358 [Multi-domain] Cd Length: 861 Bit Score: 208.40 E-value: 1.53e-58
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| AAK_AK-HSDH | cd04257 | AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal ... |
11-321 | 5.24e-58 | ||||||||
AAK_AK-HSDH: Amino Acid Kinase Superfamily (AAK), AK-HSDH; this CD includes the N-terminal catalytic domain of aspartokinase (AK) of the bifunctional enzyme AK - homoserine dehydrogenase (HSDH). These aspartokinases are found in bacteria (E. coli AKI-HSDHI, ThrA and E. coli AKII-HSDHII, MetL) and 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. Pssm-ID: 239790 [Multi-domain] Cd Length: 294 Bit Score: 194.72 E-value: 5.24e-58
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| PRK09034 | PRK09034 | aspartate kinase; Reviewed |
13-496 | 2.42e-52 | ||||||||
aspartate kinase; Reviewed Pssm-ID: 236364 [Multi-domain] Cd Length: 454 Bit Score: 184.23 E-value: 2.42e-52
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| AAK | cd02115 | Amino Acid Kinases (AAK) superfamily, catalytic domain; present in such enzymes like ... |
13-321 | 1.63e-50 | ||||||||
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: 173.40 E-value: 1.63e-50
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| PRK06635 | PRK06635 | aspartate kinase; Reviewed |
12-502 | 1.67e-50 | ||||||||
aspartate kinase; Reviewed Pssm-ID: 235843 [Multi-domain] Cd Length: 404 Bit Score: 178.00 E-value: 1.67e-50
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| AAK_AKiii-LysC-EC | cd04258 | AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the ... |
12-321 | 7.36e-49 | ||||||||
AAK_AKiii-LysC-EC: Amino Acid Kinase Superfamily (AAK), AKiii-LysC-EC: this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine-sensitive aspartokinase isoenzyme AKIII. AKIII is a monofunctional class enzyme (LysC) found in some bacteria such as E. coli. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In E. coli, LysC is reported to be a homodimer of 50 kD subunits. Pssm-ID: 239791 [Multi-domain] Cd Length: 292 Bit Score: 170.62 E-value: 7.36e-49
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| PRK08210 | PRK08210 | aspartate kinase I; Reviewed |
133-499 | 5.92e-41 | ||||||||
aspartate kinase I; Reviewed Pssm-ID: 236188 [Multi-domain] Cd Length: 403 Bit Score: 152.31 E-value: 5.92e-41
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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 ... |
12-321 | 2.13e-36 | ||||||||
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: 135.31 E-value: 2.13e-36
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| PRK07431 | PRK07431 | aspartate kinase; Provisional |
229-499 | 3.38e-36 | ||||||||
aspartate kinase; Provisional Pssm-ID: 236018 [Multi-domain] Cd Length: 587 Bit Score: 141.98 E-value: 3.38e-36
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| AAK_AKiii-YclM-BS | cd04245 | AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the ... |
13-321 | 1.77e-34 | ||||||||
AAK_AKiii-YclM-BS: Amino Acid Kinase Superfamily (AAK), AKiii-YclM-BS; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in Bacilli (Bacillus subtilis YclM) and Clostridia species. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. In Bacillus subtilis (BS), YclM is reported to be a single polypeptide of 50 kD. The Bacillus subtilis 168 AKIII is induced by lysine and repressed by threonine, and it is synergistically inhibited by lysine and threonine. Pssm-ID: 239778 [Multi-domain] Cd Length: 288 Bit Score: 131.24 E-value: 1.77e-34
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| AAK_AK-DapDC | cd04259 | AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal ... |
11-321 | 2.36e-34 | ||||||||
AAK_AK-DapDC: Amino Acid Kinase Superfamily (AAK), AK-DapDC; this CD includes the N-terminal catalytic aspartokinase (AK) domain of the bifunctional enzyme AK - DAP decarboxylase (DapDC) found in some bacteria. Aspartokinase is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. DapDC, which is the lysA gene product, catalyzes the decarboxylation of DAP to lysine. Pssm-ID: 239792 [Multi-domain] Cd Length: 295 Bit Score: 131.12 E-value: 2.36e-34
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| AA_kinase | pfam00696 | Amino acid kinase family; This family includes kinases that phosphorylate a variety of amino ... |
10-310 | 1.61e-33 | ||||||||
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: 127.10 E-value: 1.61e-33
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| AAK_AKi-DapG-BS | cd04260 | AAK_AKi-DapG-BS: Amino Acid Kinase Superfamily (AAK), AKi-DapG; this CD includes the ... |
133-321 | 6.84e-33 | ||||||||
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: 125.58 E-value: 6.84e-33
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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 ... |
12-321 | 8.32e-32 | ||||||||
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: 122.64 E-value: 8.32e-32
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| ACT_AK-Hom3_1 | cd04934 | CT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a ... |
362-435 | 9.09e-32 | ||||||||
CT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains; This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains. AK is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single AK, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies shown that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153206 Cd Length: 73 Bit Score: 116.79 E-value: 9.09e-32
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| ACT_AK-Hom3_2 | cd04919 | ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3; This CD ... |
437-502 | 1.62e-31 | ||||||||
ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3; This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the aspartokinase (AK) HOM3, a monofunctional class enzyme found in Saccharomyces cerevisiae, and other related ACT domains. AK is the first enzyme in the aspartate metabolic pathway, catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and in fungi, is responsible for the production of threonine, isoleucine and methionine. S. cerevisiae has a single AK, which is regulated by feedback, allosteric inhibition by L-threonine. Recent studies shown that the allosteric transition triggered by binding of threonine to AK involves a large change in the conformation of the native hexameric enzyme that is converted to an inactive one of different shape and substantially smaller hydrodynamic size. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153191 Cd Length: 66 Bit Score: 116.08 E-value: 1.62e-31
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| PRK05925 | PRK05925 | aspartate kinase; Provisional |
12-444 | 1.88e-26 | ||||||||
aspartate kinase; Provisional Pssm-ID: 235646 [Multi-domain] Cd Length: 440 Bit Score: 111.83 E-value: 1.88e-26
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| ACT_AKiii-LysC-EC-like_1 | cd04912 | ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase ... |
362-435 | 3.21e-24 | ||||||||
ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII; This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in bacteria (Escherichia coli (EC) LysC) and plants, (Zea mays Ask1, Ask2, and Arabidopsis thaliana AK1). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Like the A. thaliana AK1 (AK1-AT), the E. coli AKIII (LysC) has two bound feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. The lysine-sensitive plant isoenzyme is synergistically inhibited by S-adenosylmethionine. A homolog of this group appears to be the Saccharomyces cerevisiae AK (Hom3) which clusters with this group as well. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153184 Cd Length: 75 Bit Score: 96.12 E-value: 3.21e-24
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| PRK09181 | PRK09181 | aspartate kinase; Validated |
13-500 | 3.53e-24 | ||||||||
aspartate kinase; Validated Pssm-ID: 236396 [Multi-domain] Cd Length: 475 Bit Score: 105.39 E-value: 3.53e-24
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| PRK08841 | PRK08841 | aspartate kinase; Validated |
12-498 | 3.64e-24 | ||||||||
aspartate kinase; Validated Pssm-ID: 181563 [Multi-domain] Cd Length: 392 Bit Score: 104.45 E-value: 3.64e-24
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| PRK08373 | PRK08373 | aspartate kinase; Validated |
12-306 | 1.71e-23 | ||||||||
aspartate kinase; Validated Pssm-ID: 236250 [Multi-domain] Cd Length: 341 Bit Score: 101.67 E-value: 1.71e-23
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| ACT_AK-like_2 | cd04892 | ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ... |
438-500 | 3.63e-22 | ||||||||
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes the second of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). The exception in this group, is the inclusion of the first ACT domain of the bifunctional aspartokinase - homoserine dehydrogenase-like enzyme group (ACT_AKi-HSDH-ThrA-like_1) which includes the monofunctional, threonine-sensitive, aspartokinase found in Methanococcus jannaschii and other related archaeal species. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. AK is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. One mechanism for the regulation of this pathway is by the production of several isoenzymes of AK 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 (EC), three different AK 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 (BS) 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 is 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, and apparently, unique to cyanobacteria, are AKs with two tandem pairs of ACT domains, C-terminal to the catalytic domain. 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, 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 are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153164 [Multi-domain] Cd Length: 65 Bit Score: 89.86 E-value: 3.63e-22
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| metL | PRK09466 | bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional |
13-500 | 3.01e-21 | ||||||||
bifunctional aspartate kinase II/homoserine dehydrogenase II; Provisional Pssm-ID: 236530 [Multi-domain] Cd Length: 810 Bit Score: 97.69 E-value: 3.01e-21
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| ACT_AK-like | cd04868 | ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ... |
438-497 | 1.70e-18 | ||||||||
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes each of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). Typically, AK consists of two ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Aspartokinase is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. 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 (EC), 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 (BS) 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 is 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, and apparently, unique to cyanobacteria, are aspartokinases with two tandem pairs of ACT domains, C-terminal to the catalytic domain. 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, 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 AK family CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153140 [Multi-domain] Cd Length: 60 Bit Score: 79.46 E-value: 1.70e-18
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| ACT_AKi-HSDH-ThrA_2 | cd04922 | ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH); ... |
437-500 | 5.19e-18 | ||||||||
ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH); This CD includes the second of two ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH). The ACT domains are positioned between the N-terminal catalytic domain of AK and the C-terminal HSDH domain found in bacteria (Escherichia coli (EC) ThrA) and higher plants (Zea 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. HSDH is the first committed reaction in the branch of the pathway that leads to Thr and Met. 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 were shown to be involved in allosteric activation. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153194 [Multi-domain] Cd Length: 66 Bit Score: 78.16 E-value: 5.19e-18
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| ACT_AKiii-YclM-BS_2 | cd04916 | ACT domains located C-terminal to the catalytic domain of the lysine plus threonine-sensitive ... |
437-498 | 6.63e-16 | ||||||||
ACT domains located C-terminal to the catalytic domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII; This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the lysine plus threonine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in Bacilli (Bacillus subtilis (BS) YclM) and Clostridia species. Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. B. subtilis YclM is reported to be a single polypeptide of 50 kD. AKIII from B. subtilis strain 168 is induced by lysine and repressed by threonine and it is synergistically inhibited by lysine and threonine. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153188 [Multi-domain] Cd Length: 66 Bit Score: 72.29 E-value: 6.63e-16
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| ACT_AKii-LysC-BS-like_2 | cd04936 | ACT domains of the lysine-sensitive, aspartokinase (AK) isoenzyme AKII of Bacillus subtilis ... |
440-498 | 1.59e-15 | ||||||||
ACT domains of the lysine-sensitive, aspartokinase (AK) isoenzyme AKII of Bacillus subtilis (BS) strain 168 and related domains; This CD includes the C-terminal of the two ACT domains of the lysine-sensitive, aspartokinase (AK) isoenzyme AKII of Bacillus subtilis (BS) strain 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, and related sequences. In B. subtilis strain 168, the regulation of the diaminopimelate (Dap)-lysine biosynthetic pathway involves dual control by Dap and lysine, effected through separate Dap- and lysine-sensitive AK isoenzymes. The B. subtilis strain 168 AKII is induced by methionine and repressed and inhibited by lysine. Although C. glutamicum is known to contain a single AK, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In corynebacteria and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Conserved residues in the ACT domains have been shown to be involved in this concerted feedback inhibition. Also included in this CD are the AKs of the extreme thermophile, Thermus thermophilus HB27, the Gram-negative obligate methylotroph, Methylophilus methylotrophus AS1, and those single AKs found in Pseudomons, C. glutamicum, and Amycolatopsis lactamdurans. B. subtilis strain 168 AKII, and the C. glutamicum, Streptomyces clavuligerus and A. lactamdurans AKs 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. This CD includes the second ACT domain C-terminal to the AK catalytic domain of the alpha subunit and the second ACT domain of the beta subunit that lacks the AK catalytic domain. Unlike the C. glutamicum AK beta subunit, which is involved in feedback regulation, the B. subtilis AKII beta subunit is not. Cyanobacteria AKs are unique to this CD and they have a unique domain architecture with two tandem pairs of ACT domains, C-terminal to the catalytic AK domain. In this CD, the second and fourth cyanobacteria AK ACT domains are present. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153208 Cd Length: 63 Bit Score: 71.02 E-value: 1.59e-15
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| ACT_AK-LysC-DapG-like_2 | cd04923 | ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) ... |
440-498 | 3.25e-15 | ||||||||
ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168 and related domains; This CD includes the C-terminal of the two ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, as well as, the second and fourth, of four, ACT domains present in cyanobacteria AK. Also included are the C-terminal of the two ACT domains of the diaminopimelate-sensitive aspartokinase isoenzyme AKI found in Bacilli (B. subtilis strain 168), Clostridia, and Actinobacteria bacterial species. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153195 Cd Length: 63 Bit Score: 70.24 E-value: 3.25e-15
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| AAK_AK-Ectoine | cd04248 | AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the ... |
13-321 | 3.36e-15 | ||||||||
AAK_AK-Ectoine: Amino Acid Kinase Superfamily (AAK), AK-Ectoine; this CD includes the N-terminal catalytic domain of the aspartokinase of the ectoine (1,4,5,6-tetrahydro-2-methyl pyrimidine-4-carboxylate) biosynthetic pathway found in Methylomicrobium alcaliphilum, Vibrio cholerae, and other various halotolerant or halophilic bacteria. Bacteria exposed to hyperosmotic stress accumulate organic solutes called 'compatible solutes' of which ectoine, a heterocyclic amino acid, is one. Apart from its osmotic function, ectoine also exhibits a protective effect on proteins, nucleic acids and membranes against a variety of stress factors. de novo synthesis of ectoine starts with the phosphorylation of L-aspartate and shares its first two enzymatic steps with the biosynthesis of amino acids of the aspartate family: aspartokinase and L-aspartate-semialdehyde dehydrogenase. The M. alcaliphilum and the V. cholerae aspartokinases are encoded on the ectABCask operon. Pssm-ID: 239781 [Multi-domain] Cd Length: 304 Bit Score: 76.33 E-value: 3.36e-15
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| ACT_AK-like_1 | cd04890 | ACT domains found C-terminal to the catalytic domain of aspartokinase (AK; ... |
363-426 | 6.82e-15 | ||||||||
ACT domains found C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes the first of two ACT domains found C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP, and is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids, lysine, threonine, methionine, and isoleucine. This CD, includes the first ACT domain of the Escherichia coli (EC) isoenzyme, AKIII (LysC) and the Arabidopsis isoenzyme, asparate kinase 1, both enzymes monofunctional and involved in lysine synthesis, as well as the the first ACT domain of Bacillus subtilis (BS) isoenzyme, AKIII (YclM), and of the Saccharomyces cerevisiae AK (Hom3). Also included are the first ACT domains of the Methylomicrobium alcaliphilum AK, the first enzyme of the ectoine biosynthetic pathway. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153162 Cd Length: 62 Bit Score: 69.11 E-value: 6.82e-15
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| ACT_AK-Arch_2 | cd04924 | ACT domains of a monofunctional aspartokinase found mostly in Archaea species (ACT_AK-Arch_2); ... |
439-497 | 2.13e-14 | ||||||||
ACT domains of a monofunctional aspartokinase found mostly in Archaea species (ACT_AK-Arch_2); Included in this CD is the second of two ACT domains of a monofunctional aspartokinase found mostly in Archaea species (ACT_AK-Arch_2). The first or N-terminal ACT domain of these proteins cluster with the ThrA-like ACT 1 domains (ACT_AKi-HSDH-ThrA-like_1) which includes the threonine-sensitive archaeal Methanococcus jannaschii aspartokinase ACT 1 domain. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153196 [Multi-domain] Cd Length: 66 Bit Score: 67.91 E-value: 2.13e-14
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| ACT_AKi-HSDH-ThrA-like_1 | cd04921 | ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH); ... |
437-507 | 8.25e-14 | ||||||||
ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH); This CD includes the first of two ACT domains of the bifunctional enzyme aspartokinase (AK) - homoserine dehydrogenase (HSDH). The ACT domains are positioned between the N-terminal catalytic domain of AK and the C-terminal HSDH domain found in bacteria (Escherichia coli (EC) ThrA) and higher plants (Zea 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. HSDH is the first committed reaction in the branch of the pathway that leads to Thr and Met. 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 were shown to be involved in allosteric activation. Also included in this CD is the first of two ACT domains of a tetrameric, monofunctional, threonine-sensitive, AK found in Methanococcus jannaschii and other related archaeal species. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153193 [Multi-domain] Cd Length: 80 Bit Score: 66.47 E-value: 8.25e-14
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| AAK_UMPK-like | cd04239 | AAK_UMPK-like: UMP kinase (UMPK)-like, the microbial/chloroplast uridine monophosphate kinase ... |
205-322 | 1.53e-13 | ||||||||
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: 70.26 E-value: 1.53e-13
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| ACT_AKiii-LysC-EC_2 | cd04917 | ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase ... |
437-502 | 9.02e-12 | ||||||||
ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII; This CD includes the second of two ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in bacteria (Escherichia coli (EC) LysC). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The E. coli AKIII (LysC) binds two feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. The second ACT domain (ACT2), this CD, is not involved in the binding of heterotrophic effectors. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153189 [Multi-domain] Cd Length: 64 Bit Score: 60.28 E-value: 9.02e-12
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| ACT_AKiii-LysC-EC_1 | cd04932 | ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase ... |
363-433 | 2.13e-11 | ||||||||
ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII; This CD includes the first of two ACT domains located C-terminal to the catalytic domain of the lysine-sensitive aspartokinase isoenzyme AKIII, a monofunctional class enzyme found in bacteria (Escherichia coli (EC) LysC). Aspartokinase is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The E. coli AKIII (LysC) binds two feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153204 Cd Length: 75 Bit Score: 59.74 E-value: 2.13e-11
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| pyrH_arch | TIGR02076 | uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most ... |
233-321 | 1.38e-09 | ||||||||
uridylate kinase, putative; This family consists of the archaeal and spirochete proteins most closely related to bacterial uridylate kinases (TIGR02075), an enzyme involved in pyrimidine biosynthesis. Members are likely, but not known, to be functionally equivalent to their bacterial counterparts. However, substantial sequence differences suggest that regulatory mechanisms may be different; the bacterial form is allosterically regulated by GTP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions] Pssm-ID: 273956 [Multi-domain] Cd Length: 221 Bit Score: 58.09 E-value: 1.38e-09
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| AAK_UMPK-PyrH-Pf | cd04253 | AAK_UMPK-PyrH-Pf: UMP kinase (UMPK)-Pf, the mostly archaeal uridine monophosphate kinase ... |
233-321 | 2.83e-09 | ||||||||
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: 57.26 E-value: 2.83e-09
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| PyrH | COG0528 | Uridylate kinase [Nucleotide transport and metabolism]; Uridylate kinase is part of the ... |
206-323 | 1.63e-08 | ||||||||
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: 55.41 E-value: 1.63e-08
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| AAK_UMPK-PyrH-Ec | cd04254 | UMP kinase (UMPK)-Ec, the microbial/chloroplast uridine monophosphate kinase (uridylate kinase) ... |
205-322 | 2.13e-08 | ||||||||
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: 54.80 E-value: 2.13e-08
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| pyrH_bact | TIGR02075 | uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a ... |
205-321 | 2.93e-08 | ||||||||
uridylate kinase; This protein, also called UMP kinase, converts UMP to UDP by adding a phosphate from ATP. It is the first step in pyrimidine biosynthesis. GTP is an allosteric activator. In a large fraction of all bacterial genomes, the gene tends to be located immediately downstream of elongation factor Ts and upstream of ribosome recycling factor. A related protein family, believed to be equivalent in function and found in the archaea and in spirochetes, is described by a separate model, TIGR02076. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions] Pssm-ID: 213681 [Multi-domain] Cd Length: 232 Bit Score: 54.55 E-value: 2.93e-08
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| ACT_AK1-AT_2 | cd04918 | ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, ... |
438-502 | 1.72e-07 | ||||||||
ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1); This CD includes the second of two ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1), which can be synergistically inhibited by S-adenosylmethionine (SAM). This isoenzyme is found in higher plants, Arabidopsis thaliana (AT) and Zea mays, and also in Chlorophyta. In its inactive state, Arabidopsis AK1 binds the effectors lysine and SAM (two molecules each) at the interface of two ACT1 domain subunits. The second ACT domain (ACT2), this CD, does not interact with an effector. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153190 Cd Length: 65 Bit Score: 48.34 E-value: 1.72e-07
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| ACT_AK-like | cd04868 | ACT domains C-terminal to the catalytic domain of aspartokinase (AK; ... |
364-419 | 1.88e-07 | ||||||||
ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase); This CD includes each of two ACT domains C-terminal to the catalytic domain of aspartokinase (AK; 4-L-aspartate-4-phosphotransferase). Typically, AK consists of two ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. AK catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. Aspartokinase is the first enzyme in the pathway of the biosynthesis of the aspartate family of amino acids (lysine, threonine, methionine, and isoleucine) and the bacterial cell wall component, meso-diaminopimelate. 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 (EC), 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 (BS) 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 is 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, and apparently, unique to cyanobacteria, are aspartokinases with two tandem pairs of ACT domains, C-terminal to the catalytic domain. 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, 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 AK family CD are the ACT domains of the Methylomicrobium alcaliphilum AK; the first enzyme of the ectoine biosynthetic pathway found in this bacterium and several other halophilic/halotolerant bacteria. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153140 [Multi-domain] Cd Length: 60 Bit Score: 47.88 E-value: 1.88e-07
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| ACT_AKiii-DAPDC_2 | cd04920 | ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate ... |
438-501 | 8.17e-07 | ||||||||
ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC); This CD includes the second of two ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC) bacterial protein. Aspartokinase (AK) is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The lysA gene encodes the enzyme DAPDC, a pyridoxal-5'-phosphate (PLP)-dependent enzyme which catalyzes the final step in the lysine biosynthetic pathway converting meso-diaminopimelic acid (DAP) to l-lysine. Tandem ACT domains are positioned centrally with the AK catalytic domain N-terminal and the DAPDC domains C-terminal. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153192 Cd Length: 63 Bit Score: 46.29 E-value: 8.17e-07
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| ACT_AK-LysC-DapG-like_1 | cd04891 | ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII and related proteins; This CD ... |
440-494 | 2.46e-06 | ||||||||
ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII and related proteins; This CD includes the N-terminal of the two ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168, and the lysine plus threonine-sensitive aspartokinase of Corynebacterium glutamicum, as well as, the first and third, of four, ACT domains present in cyanobacteria AK. Also included are the N-terminal of the two ACT domains of the diaminopimelate-sensitive aspartokinase isoenzyme AKI found in Bacilli (Bacillus subtilis strain 168), Clostridia, and Actinobacteria bacterial species. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153163 [Multi-domain] Cd Length: 61 Bit Score: 44.86 E-value: 2.46e-06
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| ACT_AKii-LysC-BS-like_1 | cd04913 | ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) ... |
440-505 | 4.28e-06 | ||||||||
ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 168 and related proteins; This CD includes the N-terminal of the two ACT domains of the lysine-sensitive aspartokinase isoenzyme AKII of Bacillus subtilis (BS) strain 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, both the succinylase and dehydrogenase variant pathways of DAP-lysine synthesis operate simultaneously in this organism. In corynebacteria and other various Gram-positive bacteria, the DAP-lysine pathway is feedback regulated by the concerted action of lysine and threonine. Conserved residues in the ACT domains have been shown to be involved in this concerted feedback inhibition. 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 Pseudomonas aeruginosa, 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. This CD includes the first ACT domain C-terminal to the AK catalytic domain of the alpha subunit and the first ACT domain of the beta subunit that lacks the AK catalytic domain. Unlike the C. glutamicum AK beta subunit, which is involved in feedback regulation, the B. subtilis AKII beta subunit is not. Cyanobacteria aspartokinases are unique to this CD and they have a unique domain architecture with two tandem pairs of ACT domains, C-terminal to the catalytic AK domain. In this CD, the first and third cyanobacteria AK ACT domains are present. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153185 Cd Length: 75 Bit Score: 44.44 E-value: 4.28e-06
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| AAK_UMPK-MosAB | cd04255 | AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA ... |
206-322 | 2.21e-05 | ||||||||
AAK_UMPK-MosAB: This CD includes the alpha and beta subunits of the Mo storage protein (MosA and MosB) which are related to uridine monophosphate kinase (UMPK) enzymes that catalyze the phosphorylation of UMP by ATP, yielding UDP, and playing a key role in pyrimidine nucleotide biosynthesis. The Mo storage protein from the nitrogen-fixing bacterium, Azotobacter vinelandii, is characterized as an alpha4-beta4 octamer containing a polynuclear molybdenum-oxide cluster which is ATP-dependent to bind Mo and pH-dependent to release Mo. These and related bacterial sequences in this CD are members of the Amino Acid Kinase Superfamily (AAK). Pssm-ID: 239788 [Multi-domain] Cd Length: 262 Bit Score: 46.23 E-value: 2.21e-05
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| ACT_AKiii-DAPDC_1 | cd04935 | ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate ... |
377-434 | 2.30e-05 | ||||||||
ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC) bacterial protein; This CD includes the first of two ACT domains of a bifunctional AKIII (LysC)-like aspartokinase/meso-diaminopimelate decarboxylase (DAPDC) bacterial protein. Aspartokinase (AK) is the first enzyme in the aspartate metabolic pathway and catalyzes the conversion of aspartate and ATP to aspartylphosphate and ADP. The lysA gene encodes the enzyme DAPDC, a pyridoxal-5'-phosphate (PLP)-dependent enzyme which catalyzes the final step in the lysine biosynthetic pathway converting meso-diaminopimelic acid (DAP) to l-lysine. Tandem ACT domains are positioned centrally with the AK catalytic domain N-terminal and the DAPDC domains C-terminal. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153207 Cd Length: 75 Bit Score: 42.50 E-value: 2.30e-05
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| ACT_7 | pfam13840 | ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the ... |
430-498 | 3.19e-05 | ||||||||
ACT domain; The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding. Pssm-ID: 433519 [Multi-domain] Cd Length: 65 Bit Score: 41.75 E-value: 3.19e-05
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| AAK_P5CS_ProBA | cd04256 | AAK_P5CS_ProBA: Glutamate-5-kinase (G5K) domain of the bifunctional delta ... |
195-285 | 4.64e-05 | ||||||||
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: 45.50 E-value: 4.64e-05
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| ProB | COG0263 | Glutamate 5-kinase [Amino acid transport and metabolism]; Glutamate 5-kinase is part of the ... |
237-278 | 5.10e-05 | ||||||||
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: 45.41 E-value: 5.10e-05
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| PRK12354 | PRK12354 | carbamate kinase; Reviewed |
234-285 | 9.36e-05 | ||||||||
carbamate kinase; Reviewed Pssm-ID: 183466 Cd Length: 307 Bit Score: 44.44 E-value: 9.36e-05
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| AAK_G5K_ProB | cd04242 | AAK_G5K_ProB: Glutamate-5-kinase (G5K) catalyzes glutamate-dependent ATP cleavage; G5K ... |
237-276 | 9.48e-05 | ||||||||
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: 43.97 E-value: 9.48e-05
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| ACT | pfam01842 | ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to ... |
452-498 | 3.03e-04 | ||||||||
ACT domain; This family of domains generally have a regulatory role. ACT domains are linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The ACT domain is found in: D-3-phosphoglycerate dehydrogenase EC:1.1.1.95, which is inhibited by serine. Aspartokinase EC:2.7.2.4, which is regulated by lysine. Acetolactate synthase small regulatory subunit, which is inhibited by valine. Phenylalanine-4-hydroxylase EC:1.14.16.1, which is regulated by phenylalanine. Prephenate dehydrogenase EC:4.2.1.51. formyltetrahydrofolate deformylase EC:3.5.1.10, which is activated by methionine and inhibited by glycine. GTP pyrophosphokinase EC:2.7.6.5 Pssm-ID: 426468 [Multi-domain] Cd Length: 66 Bit Score: 39.21 E-value: 3.03e-04
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| ACT | cd02116 | ACT domains are commonly involved in specifically binding an amino acid or other small ligand ... |
452-494 | 4.67e-04 | ||||||||
ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme; Members of this CD belong to the superfamily of ACT regulatory domains. Pairs of ACT domains are commonly involved in specifically binding an amino acid or other small ligand leading to regulation of the enzyme. The ACT domain has been detected in a number of diverse proteins; some of these proteins are involved in amino acid and purine biosynthesis, phenylalanine hydroxylation, regulation of bacterial metabolism and transcription, and many remain to be characterized. ACT domain-containing enzymes involved in amino acid and purine synthesis are in many cases allosteric enzymes with complex regulation enforced by the binding of ligands. The ACT domain is commonly involved in the binding of a small regulatory molecule, such as the amino acids L-Ser and L-Phe in the case of D-3-phosphoglycerate dehydrogenase and the bifunctional chorismate mutase-prephenate dehydratase enzyme (P-protein), respectively. Aspartokinases typically consist of two C-terminal ACT domains in a tandem repeat, but the second ACT domain is inserted within the first, resulting in, what is normally the terminal beta strand of ACT2, formed from a region N-terminal of ACT1. ACT domain repeats have been shown to have nonequivalent ligand-binding sites with complex regulatory patterns such as those seen in the bifunctional enzyme, aspartokinase-homoserine dehydrogenase (ThrA). In other enzymes, such as phenylalanine hydroxylases, the ACT domain appears to function as a flexible small module providing allosteric regulation via transmission of conformational changes, these conformational changes are not necessarily initiated by regulatory ligand binding at the ACT domain itself. ACT domains are present either singularly, N- or C-terminal, or in pairs present C-terminal or between two catalytic domains. Unique to cyanobacteria are four ACT domains C-terminal to an aspartokinase domain. A few proteins are composed almost entirely of ACT domain repeats as seen in the four ACT domain protein, the ACR protein, found in higher plants; and the two ACT domain protein, the glycine cleavage system transcriptional repressor (GcvR) protein, found in some bacteria. Also seen are single ACT domain proteins similar to the Streptococcus pneumoniae ACT domain protein (uncharacterized pdb structure 1ZPV) found in both bacteria and archaea. Purportedly, the ACT domain is an evolutionarily mobile ligand binding regulatory module that has been fused to different enzymes at various times. Pssm-ID: 153139 [Multi-domain] Cd Length: 60 Bit Score: 38.43 E-value: 4.67e-04
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| ACT_AK1-AT_1 | cd04933 | ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, ... |
362-407 | 1.20e-03 | ||||||||
ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1); This CD includes the first of two ACT domains located C-terminal to the catalytic domain of a monofunctional, lysine-sensitive, plant aspartate kinase 1 (AK1), which can be synergistically inhibited by S-adenosylmethionine. This isoenzyme is found in higher plants, Arabidopsis thaliana (AT) and Zea mays, and also in Chlorophyta. Like the Escherichia coli AKIII (LysC), Arabidopsis AK1 binds two feedback allosteric inhibitor lysine molecules at the dimer interface located between the ACT1 domain of two subunits. A loop in common is involved in the binding of both Lys and S-adenosylmethionine providing an explanation for the synergistic inhibition by these effectors. Members of this CD belong to the superfamily of ACT regulatory domains. Pssm-ID: 153205 Cd Length: 78 Bit Score: 37.66 E-value: 1.20e-03
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| PRK12454 | PRK12454 | carbamate kinase-like carbamoyl phosphate synthetase; Reviewed |
218-286 | 4.17e-03 | ||||||||
carbamate kinase-like carbamoyl phosphate synthetase; Reviewed Pssm-ID: 183535 Cd Length: 313 Bit Score: 39.21 E-value: 4.17e-03
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