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pantetheine-phosphate adenylyltransferase [Priestia koreensis]
pantetheine-phosphate adenylyltransferase( domain architecture ID 10786277)
pantetheine-phosphate adenylyltransferase catalyzes the reversible transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to form dephospho-CoA (dPCoA) and pyrophosphate in the Coenzyme A (CoA) biosynthetic pathway
List of domain hits
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Name | Accession | Description | Interval | E-value | |||
CoaD | COG0669 | Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ... |
4-159 | 2.47e-102 | |||
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis : Pssm-ID: 440433 Cd Length: 159 Bit Score: 289.98 E-value: 2.47e-102
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Name | Accession | Description | Interval | E-value | ||||
CoaD | COG0669 | Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ... |
4-159 | 2.47e-102 | ||||
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis Pssm-ID: 440433 Cd Length: 159 Bit Score: 289.98 E-value: 2.47e-102
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PPAT | cd02163 | Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ... |
4-156 | 1.61e-93 | ||||
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli. Pssm-ID: 173914 [Multi-domain] Cd Length: 153 Bit Score: 267.41 E-value: 1.61e-93
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coaD_prev_kdtB | TIGR01510 | pantetheine-phosphate adenylyltransferase, bacterial; This model describes ... |
4-158 | 3.65e-75 | ||||
pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A] Pssm-ID: 273663 [Multi-domain] Cd Length: 155 Bit Score: 221.38 E-value: 3.65e-75
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CTP_transf_like | pfam01467 | Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
6-135 | 9.18e-30 | ||||
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases. Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 105.48 E-value: 9.18e-30
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nadD | PRK07152 | nicotinate-nucleotide adenylyltransferase; |
4-152 | 3.79e-07 | ||||
nicotinate-nucleotide adenylyltransferase; Pssm-ID: 235947 [Multi-domain] Cd Length: 342 Bit Score: 48.40 E-value: 3.79e-07
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Citrate_ly_lig | smart00764 | Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ... |
13-78 | 1.38e-06 | ||||
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22. Pssm-ID: 129003 Cd Length: 182 Bit Score: 45.70 E-value: 1.38e-06
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Name | Accession | Description | Interval | E-value | ||||
CoaD | COG0669 | Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine ... |
4-159 | 2.47e-102 | ||||
Phosphopantetheine adenylyltransferase [Coenzyme transport and metabolism]; Phosphopantetheine adenylyltransferase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis Pssm-ID: 440433 Cd Length: 159 Bit Score: 289.98 E-value: 2.47e-102
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PPAT | cd02163 | Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is ... |
4-156 | 1.61e-93 | ||||
Phosphopantetheine adenylyltransferase; Phosphopantetheine adenylyltransferase (PPAT). PPAT is an essential enzyme in bacteria, responsible for catalyzing the rate-limiting step in coenzyme A (CoA) biosynthesis. The dinucleotide-binding fold of PPAT is homologous to class I aminoacyl-tRNA synthetases. CoA has been shown to inhibit PPAT and competes with ATP, PhP, and dPCoA. PPAT is a homohexamer in E. coli. Pssm-ID: 173914 [Multi-domain] Cd Length: 153 Bit Score: 267.41 E-value: 1.61e-93
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coaD_prev_kdtB | TIGR01510 | pantetheine-phosphate adenylyltransferase, bacterial; This model describes ... |
4-158 | 3.65e-75 | ||||
pantetheine-phosphate adenylyltransferase, bacterial; This model describes pantetheine-phosphate adenylyltransferase, the penultimate enzyme of coenzyme A (CoA) biosynthesis in bacteria. It does not show any strong homology to eukaryotic enzymes of coenzyme A biosynthesis. This protein was previously designated KdtB and postulated (because of cytidyltransferase homology and proximity to kdtA) to be an enzyme of LPS biosynthesis, a cytidyltransferase for 3-deoxy-D-manno-2-octulosonic acid. However, no activity toward that compound was found with either CTP or ATP. The phylogenetic distribution of this enzyme is more consistent with coenzyme A biosynthesis than with LPS biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A] Pssm-ID: 273663 [Multi-domain] Cd Length: 155 Bit Score: 221.38 E-value: 3.65e-75
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CTP_transf_like | pfam01467 | Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; ... |
6-135 | 9.18e-30 | ||||
Cytidylyltransferase-like; This family includes: Cholinephosphate cytidylyltransferase; glycerol-3-phosphate cytidylyltransferase. It also includes putative adenylyltransferases, and FAD synthases. Pssm-ID: 396172 [Multi-domain] Cd Length: 134 Bit Score: 105.48 E-value: 9.18e-30
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cyt_tran_rel | TIGR00125 | cytidyltransferase-like domain; Protein families that contain at least one copy of this domain ... |
4-64 | 8.24e-17 | ||||
cytidyltransferase-like domain; Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Pssm-ID: 272920 [Multi-domain] Cd Length: 66 Bit Score: 70.03 E-value: 8.24e-17
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TIGR00482 | TIGR00482 | nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the ... |
9-157 | 9.67e-09 | ||||
nicotinate (nicotinamide) nucleotide adenylyltransferase; This model represents the predominant bacterial/eukaryotic adenylyltransferase for nicotinamide-nucleotide, its deamido form nicotinate nucleotide, or both. The first activity, nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1), synthesizes NAD by the salvage pathway, while the second, nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) synthesizes the immediate precursor of NAD by the de novo pathway. In E. coli, NadD activity is biased toward the de novo pathway while salvage activity is channeled through the multifunctional NadR protein, but this division of labor may be exceptional. The given name of this model, nicotinate (nicotinamide) nucleotide adenylyltransferase, reflects the lack of absolute specificity with respect to substrate amidation state in most species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides] Pssm-ID: 273101 [Multi-domain] Cd Length: 193 Bit Score: 51.94 E-value: 9.67e-09
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cytidylyltransferase_like | cd02039 | Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are ... |
4-134 | 1.90e-08 | ||||
Cytidylyltransferase-like domain; Cytidylyltransferase-like domain. Many of these proteins are known to use CTP or ATP and release pyrophosphate. Protein families that contain at least one copy of this domain include citrate lyase ligase, pantoate-beta-alanine ligase, glycerol-3-phosphate cytidyltransferase, ADP-heptose synthase, phosphocholine cytidylyltransferase, lipopolysaccharide core biosynthesis protein KdtB, the bifunctional protein NadR, and a number whose function is unknown. Pssm-ID: 185678 [Multi-domain] Cd Length: 143 Bit Score: 50.13 E-value: 1.90e-08
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NMNAT | cd02165 | Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate ... |
9-157 | 3.78e-08 | ||||
Nicotinamide/nicotinate mononucleotide adenylyltransferase; Nicotinamide/nicotinate mononucleotide (NMN/ NaMN)adenylyltransferase (NMNAT). NMNAT represents the primary bacterial and eukaryotic adenylyltransferases for nicotinamide-nucleotide and for the deamido form, nicotinate nucleotide. It is an indispensable enzyme in the biosynthesis of NAD(+) and NADP(+). Nicotinamide-nucleotide adenylyltransferase synthesizes NAD via the salvage pathway, while nicotinate-nucleotide adenylyltransferase synthesizes the immediate precursor of NAD via the de novo pathway. Human NMNAT displays unique dual substrate specificity toward both NMN and NaMN, and can participate in both de novo and salvage pathways of NAD synthesis. Pssm-ID: 185680 [Multi-domain] Cd Length: 192 Bit Score: 50.32 E-value: 3.78e-08
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nt_trans | cd02156 | nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily ... |
4-130 | 3.33e-07 | ||||
nucleotidyl transferase superfamily; nt_trans (nucleotidyl transferase) This superfamily includes the class I amino-acyl tRNA synthetases, pantothenate synthetase (PanC), ATP sulfurylase, and the cytidylyltransferases, all of which have a conserved dinucleotide-binding domain. Pssm-ID: 173912 [Multi-domain] Cd Length: 105 Bit Score: 45.99 E-value: 3.33e-07
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nadD | PRK07152 | nicotinate-nucleotide adenylyltransferase; |
4-152 | 3.79e-07 | ||||
nicotinate-nucleotide adenylyltransferase; Pssm-ID: 235947 [Multi-domain] Cd Length: 342 Bit Score: 48.40 E-value: 3.79e-07
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Citrate_ly_lig | smart00764 | Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain ... |
13-78 | 1.38e-06 | ||||
Citrate lyase ligase C-terminal domain; Proteins of this family contain the C-terminal domain of citrate lyase ligase EC:6.2.1.22. Pssm-ID: 129003 Cd Length: 182 Bit Score: 45.70 E-value: 1.38e-06
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nadD | PRK00071 | nicotinate-nucleotide adenylyltransferase; |
1-69 | 1.98e-06 | ||||
nicotinate-nucleotide adenylyltransferase; Pssm-ID: 234611 [Multi-domain] Cd Length: 203 Bit Score: 45.60 E-value: 1.98e-06
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Citrate_lyase_ligase | cd02169 | Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is ... |
13-78 | 4.51e-06 | ||||
Citrate lyase ligase; Citrate lyase ligase, also known as [Citrate (pro-3S)-lyase] ligase, is responsible for acetylation of the (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) prosthetic group of the gamma subunit of citrate lyase, converting the inactive thiol form of this enzyme to the active form. The acetylation of 1 molecule of deacetyl-citrate lyase to enzymatically active citrate lyase requires 6 molecules of ATP. The Adenylylyltranferase activity of the enzyme involves the formation of AMP and and pyrophosphate in the acetylation reaction. Pssm-ID: 173920 [Multi-domain] Cd Length: 297 Bit Score: 44.95 E-value: 4.51e-06
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NadD | COG1057 | Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; ... |
1-159 | 6.81e-06 | ||||
Nicotinate-nucleotide adenylyltransferase NadD [Coenzyme transport and metabolism]; Nicotinate-nucleotide adenylyltransferase NadD is part of the Pathway/BioSystem: NAD biosynthesis Pssm-ID: 440677 [Multi-domain] Cd Length: 197 Bit Score: 43.96 E-value: 6.81e-06
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cytidylyltransferase | cd02170 | cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate ... |
6-57 | 3.65e-04 | ||||
cytidylyltransferase; The cytidylyltransferase family includes cholinephosphate cytidylyltransferase (CCT), glycerol-3-phosphate cytidylyltransferase, RafE and phosphoethanolamine cytidylyltransferase (ECT). All enzymes catalyze the transfer of a cytidylyl group from CTP to various substrates. Pssm-ID: 173921 [Multi-domain] Cd Length: 136 Bit Score: 38.43 E-value: 3.65e-04
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NMNAT_Archaea | cd02166 | Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal ... |
5-61 | 2.39e-03 | ||||
Nicotinamide/nicotinate mononucleotide adenylyltransferase, archaeal; This family of archaeal proteins exhibits nicotinamide-nucleotide adenylyltransferase (NMNAT) activity utilizing the salvage pathway to synthesize NAD. In some cases, the enzyme was tested and found also to have the activity of nicotinate-nucleotide adenylyltransferase an enzyme of NAD de novo biosynthesis, although with a higher Km. In some archaeal species, a number of proteins which are uncharacterized with respect to activity, are also present. Pssm-ID: 173917 Cd Length: 163 Bit Score: 36.51 E-value: 2.39e-03
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PRK08099 | PRK08099 | multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase ... |
1-67 | 4.39e-03 | ||||
multifunctional transcriptional regulator/nicotinamide-nucleotide adenylyltransferase/ribosylnicotinamide kinase NadR; Pssm-ID: 236151 [Multi-domain] Cd Length: 399 Bit Score: 36.56 E-value: 4.39e-03
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