NAD(+) synthase [Cloacibacillus evryensis]
Protein Classification
glutamine-dependent NAD(+) synthetase( domain architecture ID 11479830)
glutamine-dependent NAD(+) synthetase catalyzes the ATP-dependent amidation of deamido-NAD to form NAD; uses L-glutamine as a nitrogen source
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||||
| nadE | PRK02628 | NAD synthetase; Reviewed |
1-624 | 0e+00 | ||||||||||
NAD synthetase; Reviewed : Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 952.00 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||||
| nadE | PRK02628 | NAD synthetase; Reviewed |
1-624 | 0e+00 | ||||||||||
NAD synthetase; Reviewed Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 952.00 E-value: 0e+00
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| NadE | COG0171 | NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
52-624 | 7.89e-132 | ||||||||||
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 397.68 E-value: 7.89e-132
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| GAT_Gln-NAD-synth | cd07570 | Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
7-284 | 1.29e-102 | ||||||||||
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer. Pssm-ID: 143594 [Multi-domain] Cd Length: 261 Bit Score: 312.48 E-value: 1.29e-102
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| NAD_synthase | pfam02540 | NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
335-569 | 4.01e-24 | ||||||||||
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation. Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 101.69 E-value: 4.01e-24
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| nadE | TIGR00552 | NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
336-544 | 2.07e-19 | ||||||||||
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides] Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 88.21 E-value: 2.07e-19
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| Name | Accession | Description | Interval | E-value | ||||||||||
| nadE | PRK02628 | NAD synthetase; Reviewed |
1-624 | 0e+00 | ||||||||||
NAD synthetase; Reviewed Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 952.00 E-value: 0e+00
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| NadE | COG0171 | NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
52-624 | 7.89e-132 | ||||||||||
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis Pssm-ID: 439941 [Multi-domain] Cd Length: 542 Bit Score: 397.68 E-value: 7.89e-132
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| GAT_Gln-NAD-synth | cd07570 | Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
7-284 | 1.29e-102 | ||||||||||
Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases (class 7 and 8 nitrilases); Glutamine-dependent NAD synthetases are bifunctional enzymes, which have an N-terminal GAT domain and a C-terminal NAD+ synthetase domain. The GAT domain is a glutaminase (EC 3.5.1.2) which hydrolyses L-glutamine to L-glutamate and ammonia. The ammonia is used by the NAD+ synthetase domain in the ATP-dependent amidation of nicotinic acid adenine dinucleotide. Glutamine aminotransferases are categorized depending on their active site residues into different unrelated classes. This class of GAT domain belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to classes 7 and 8. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase forms a homooctamer. Pssm-ID: 143594 [Multi-domain] Cd Length: 261 Bit Score: 312.48 E-value: 1.29e-102
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| NAD_synthase | cd00553 | NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ... |
332-599 | 2.79e-76 | ||||||||||
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source. Pssm-ID: 467484 [Multi-domain] Cd Length: 248 Bit Score: 243.62 E-value: 2.79e-76
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| PRK13981 | PRK13981 | NAD synthetase; Provisional |
17-622 | 6.44e-64 | ||||||||||
NAD synthetase; Provisional Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 220.03 E-value: 6.44e-64
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| Nit2 | COG0388 | Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
6-278 | 2.21e-50 | ||||||||||
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 175.44 E-value: 2.21e-50
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| PRK13980 | PRK13980 | NAD synthetase; Provisional |
336-612 | 4.56e-28 | ||||||||||
NAD synthetase; Provisional Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 113.38 E-value: 4.56e-28
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| nitrilase | cd07197 | Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
8-277 | 1.38e-26 | ||||||||||
Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes; This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy. Pssm-ID: 143587 [Multi-domain] Cd Length: 253 Bit Score: 108.95 E-value: 1.38e-26
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| PLN02339 | PLN02339 | NAD+ synthase (glutamine-hydrolysing) |
1-270 | 4.95e-25 | ||||||||||
NAD+ synthase (glutamine-hydrolysing) Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 110.16 E-value: 4.95e-25
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| NAD_synthase | pfam02540 | NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ... |
335-569 | 4.01e-24 | ||||||||||
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation. Pssm-ID: 396888 [Multi-domain] Cd Length: 241 Bit Score: 101.69 E-value: 4.01e-24
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| nadE | TIGR00552 | NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
336-544 | 2.07e-19 | ||||||||||
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides] Pssm-ID: 273132 [Multi-domain] Cd Length: 250 Bit Score: 88.21 E-value: 2.07e-19
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| nitrilase_8 | cd07586 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-197 | 3.21e-19 | ||||||||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143610 Cd Length: 269 Bit Score: 88.11 E-value: 3.21e-19
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| CN_hydrolase | pfam00795 | Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
7-276 | 1.70e-17 | ||||||||||
Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. The family includes: Nitrilase EC:3.5.5.1, Aliphatic amidase EC:3.5.1.4, Biotidinase EC:3.5.1.12, Beta-ureidopropionase EC:3.5.1.6. Nitrilase-related proteins generally have a conserved E-K-C catalytic triad, and are multimeric alpha-beta-beta-alpha sandwich proteins. Pssm-ID: 425873 [Multi-domain] Cd Length: 257 Bit Score: 82.79 E-value: 1.70e-17
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| nitrilase_7 | cd07585 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-277 | 1.14e-16 | ||||||||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143609 Cd Length: 261 Bit Score: 80.44 E-value: 1.14e-16
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| nitrilase_2 | cd07580 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-192 | 1.30e-14 | ||||||||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143604 Cd Length: 268 Bit Score: 74.30 E-value: 1.30e-14
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| R-amidase_like | cd07576 | Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
7-279 | 3.85e-12 | ||||||||||
Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); Pseudomonas sp. MCI3434 R-amidase hydrolyzes (R,S)-piperazine-2-tert-butylcarboxamide to form (R)-piperazine-2-carboxylic acid. It does so with strict R-stereoselectively. Its preferred substrates are carboxamide compounds which have the amino or imino group connected to their beta- or gamma-carbon. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group. It has been suggested that this subgroup represents a new class. Members of the nitrilase superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Native R-amidase however appears to be a monomer. Pssm-ID: 143600 Cd Length: 254 Bit Score: 66.83 E-value: 3.85e-12
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| Ph0642_like | cd07577 | Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
41-192 | 6.47e-10 | ||||||||||
Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases); Uncharacterized subgroup of the nitrilase superfamily. This superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. Pyrococcus horikoshii Ph0642 is a hypothetical protein belonging to this subgroup. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). This subgroup was classified as belonging to class 13, which represents proteins that at the time were difficult to place in a distinct similarity group. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143601 Cd Length: 259 Bit Score: 60.01 E-value: 6.47e-10
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| nitrilase_6 | cd07584 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-278 | 7.62e-09 | ||||||||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143608 Cd Length: 258 Bit Score: 56.99 E-value: 7.62e-09
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| nitrilase_5 | cd07583 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-191 | 5.63e-07 | ||||||||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143607 Cd Length: 253 Bit Score: 51.38 E-value: 5.63e-07
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| nadE | PRK00876 | NAD(+) synthase; |
316-417 | 1.30e-06 | ||||||||||
NAD(+) synthase; Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 50.72 E-value: 1.30e-06
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| CPA | cd07573 | N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ... |
6-191 | 3.03e-06 | ||||||||||
N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known as N-carbamoylputrescine amidase and carbamoylputrescine hydrolase) converts N-carbamoylputrescine to putrescine, a step in polyamine biosynthesis in plants and bacteria. This subgroup includes Arabidopsis thaliana CPA, also known as nitrilase-like 1 (NLP1), and Pseudomonas aeruginosa AguB. This subgroup belongs to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), this subgroup corresponds to class 11. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer; P. aeruginosa AugB is a homohexamer, Arabidopsis thaliana NLP1 is a homooctomer. Pssm-ID: 143597 Cd Length: 284 Bit Score: 49.48 E-value: 3.03e-06
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| nitrilase_1_R2 | cd07579 | Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ... |
6-192 | 1.06e-03 | ||||||||||
Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); Members of this subgroup have two nitrilase domains. This is the second of those two domains. The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143603 Cd Length: 279 Bit Score: 41.39 E-value: 1.06e-03
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| nitrilase_3 | cd07581 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
23-196 | 1.38e-03 | ||||||||||
Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The nitrilase superfamily is comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13). Class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup represents either a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143605 Cd Length: 255 Bit Score: 41.02 E-value: 1.38e-03
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| TilS | COG0037 | tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ... |
349-462 | 5.12e-03 | ||||||||||
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification Pssm-ID: 439807 [Multi-domain] Cd Length: 235 Bit Score: 39.05 E-value: 5.12e-03
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| AANH_WbpG-like | cd01996 | Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ... |
348-407 | 8.66e-03 | ||||||||||
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus. Pssm-ID: 467500 [Multi-domain] Cd Length: 158 Bit Score: 37.35 E-value: 8.66e-03
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