MULTISPECIES: NAD+ synthase [Streptomyces]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| PRK13981 super family | cl36321 | NAD synthetase; Provisional |
4-583 | 0e+00 | |||||||||
NAD synthetase; Provisional The actual alignment was detected with superfamily member PRK13981: Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 720.79 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| PRK13981 | PRK13981 | NAD synthetase; Provisional |
4-583 | 0e+00 | |||||||||
NAD synthetase; Provisional Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 720.79 E-value: 0e+00
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| NadE | COG0171 | NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
4-579 | 4.84e-155 | |||||||||
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: 455.46 E-value: 4.84e-155
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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 ... |
304-554 | 2.30e-96 | |||||||||
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: 294.08 E-value: 2.30e-96
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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 ... |
308-556 | 4.92e-76 | |||||||||
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: 241.52 E-value: 4.92e-76
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| nadE | TIGR00552 | NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
316-561 | 8.49e-62 | |||||||||
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: 204.54 E-value: 8.49e-62
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| Name | Accession | Description | Interval | E-value | |||||||||
| PRK13981 | PRK13981 | NAD synthetase; Provisional |
4-583 | 0e+00 | |||||||||
NAD synthetase; Provisional Pssm-ID: 237577 [Multi-domain] Cd Length: 540 Bit Score: 720.79 E-value: 0e+00
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| NadE | COG0171 | NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ... |
4-579 | 4.84e-155 | |||||||||
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: 455.46 E-value: 4.84e-155
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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 ... |
304-554 | 2.30e-96 | |||||||||
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: 294.08 E-value: 2.30e-96
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| GAT_Gln-NAD-synth | cd07570 | Glutamine aminotransferase (GAT, glutaminase) domain of glutamine-dependent NAD synthetases ... |
5-262 | 6.22e-94 | |||||||||
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: 288.60 E-value: 6.22e-94
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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 ... |
308-556 | 4.92e-76 | |||||||||
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: 241.52 E-value: 4.92e-76
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| PRK13980 | PRK13980 | NAD synthetase; Provisional |
316-565 | 5.66e-70 | |||||||||
NAD synthetase; Provisional Pssm-ID: 184435 [Multi-domain] Cd Length: 265 Bit Score: 226.63 E-value: 5.66e-70
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| nadE | TIGR00552 | NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ... |
316-561 | 8.49e-62 | |||||||||
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: 204.54 E-value: 8.49e-62
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| Nit2 | COG0388 | Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
3-259 | 1.95e-60 | |||||||||
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 201.24 E-value: 1.95e-60
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| nadE | PRK02628 | NAD synthetase; Reviewed |
14-499 | 9.55e-45 | |||||||||
NAD synthetase; Reviewed Pssm-ID: 235057 [Multi-domain] Cd Length: 679 Bit Score: 168.89 E-value: 9.55e-45
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| nitrilase_8 | cd07586 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
5-267 | 3.07e-38 | |||||||||
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: 142.04 E-value: 3.07e-38
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| nitrilase | cd07197 | Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
6-259 | 9.22e-32 | |||||||||
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: 123.59 E-value: 9.22e-32
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| R-amidase_like | cd07576 | Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
5-266 | 2.10e-26 | |||||||||
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: 108.44 E-value: 2.10e-26
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| CN_hydrolase | pfam00795 | Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
5-259 | 1.41e-24 | |||||||||
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: 103.20 E-value: 1.41e-24
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| nitrilase_7 | cd07585 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
5-259 | 1.18e-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: 80.05 E-value: 1.18e-16
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| nitrilase_5 | cd07583 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
5-259 | 2.02e-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: 143607 Cd Length: 253 Bit Score: 79.12 E-value: 2.02e-16
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| PLN02339 | PLN02339 | NAD+ synthase (glutamine-hydrolysing) |
17-505 | 8.38e-15 | |||||||||
NAD+ synthase (glutamine-hydrolysing) Pssm-ID: 177973 [Multi-domain] Cd Length: 700 Bit Score: 77.80 E-value: 8.38e-15
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| nitrilase_6 | cd07584 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
5-259 | 1.70e-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: 143608 Cd Length: 258 Bit Score: 73.56 E-value: 1.70e-14
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| nadE | PRK00876 | NAD(+) synthase; |
328-508 | 2.60e-14 | |||||||||
NAD(+) synthase; Pssm-ID: 179150 [Multi-domain] Cd Length: 326 Bit Score: 74.22 E-value: 2.60e-14
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| nitrilase_3 | cd07581 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
7-259 | 3.47e-12 | |||||||||
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: 66.83 E-value: 3.47e-12
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| PTZ00323 | PTZ00323 | NAD+ synthase; Provisional |
316-539 | 3.52e-12 | |||||||||
NAD+ synthase; Provisional Pssm-ID: 185554 [Multi-domain] Cd Length: 294 Bit Score: 67.49 E-value: 3.52e-12
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| nitrilase_2 | cd07580 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
5-262 | 1.23e-11 | |||||||||
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: 65.45 E-value: 1.23e-11
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| DCase | cd07569 | N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses ... |
30-164 | 2.57e-09 | |||||||||
N-carbamyl-D-amino acid amidohydrolase (DCase, class 6 nitrilases); DCase hydrolyses N-carbamyl-D-amino acids to produce D-amino acids. It is an important biocatalyst in the pharmaceutical industry, producing useful D-amino acids for example in the preparation of beta-lactam antibiotics. 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 6. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Agrobacterium radiobacter DCase forms a tetramer (dimer of dimers). Some DCases may form trimers. Pssm-ID: 143593 Cd Length: 302 Bit Score: 58.86 E-value: 2.57e-09
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| COG1606 | COG1606 | ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; |
324-391 | 2.04e-07 | |||||||||
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only]; Pssm-ID: 441214 [Multi-domain] Cd Length: 265 Bit Score: 52.42 E-value: 2.04e-07
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| Lnt | COG0815 | Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-165 | 2.27e-06 | |||||||||
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 50.23 E-value: 2.27e-06
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| nit | cd07572 | Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ... |
5-165 | 7.07e-06 | |||||||||
Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); This subgroup includes mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, and various uncharacterized bacterial and archaeal Nit-like proteins. Nit1 and Nit2 are candidate tumor suppressor proteins. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumor suppressor, fragile histidine triad (Fhit). Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis. Nit1 is a negative regulator in T cells. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2. These Nit proteins and the Nit1-like domain of NitFhit belong 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 10. Pssm-ID: 143596 Cd Length: 265 Bit Score: 47.81 E-value: 7.07e-06
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| nitrilase_1_R2 | cd07579 | Second nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ... |
5-172 | 1.39e-05 | |||||||||
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: 47.17 E-value: 1.39e-05
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| nitrilase_Rim1_like | cd07574 | Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ... |
27-261 | 5.69e-05 | |||||||||
Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an N-terminal RimI domain (class 12 nitrilases); Some members of this subgroup are implicated in post-translational modification, as they contain an N-terminal GCN5-related N-acetyltransferase (GNAT) protein RimI family domain. 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), this subgroup corresponds to class 12. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143598 Cd Length: 280 Bit Score: 45.27 E-value: 5.69e-05
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| ML_beta-AS_like | cd07568 | mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ... |
30-164 | 1.21e-03 | |||||||||
mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This family includes mammalian-like beta-AS (EC 3.5.1.6, also known as beta-ureidopropionase or N-carbamoyl-beta-alanine amidohydrolase). This enzyme catalyzes the third and final step in the catabolic pyrimidine catabolic pathway responsible for the degradation of uracil and thymine, the hydrolysis of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate to the beta-amino acids, beta-alanine and beta-aminoisobutyrate respectively. This family 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 5. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Beta-ASs from this subgroup are found in various oligomeric states, dimer (human), hexamer (calf liver), decamer (Arabidopsis and Zea mays), and in the case of Drosophila melanogaster beta-AS, as a homooctamer assembled as a left-handed helical turn, with the possibility of higher order oligomers formed by adding dimers at either end. Rat beta-AS changes its oligomeric state (hexamer, trimer, dodecamer) in response to allosteric effectors. Eukaryotic Saccharomyces kluyveri beta-AS belongs to a different superfamily. Pssm-ID: 143592 Cd Length: 287 Bit Score: 41.33 E-value: 1.21e-03
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| PRK05711 | PRK05711 | DNA polymerase III subunit epsilon; Provisional |
216-265 | 1.61e-03 | |||||||||
DNA polymerase III subunit epsilon; Provisional Pssm-ID: 235574 [Multi-domain] Cd Length: 240 Bit Score: 40.61 E-value: 1.61e-03
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| LarE-like | cd01990 | Lactate racemization operon protein LarE and similar proteins; This subfamily includes ... |
327-393 | 1.85e-03 | |||||||||
Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus. Pssm-ID: 467494 [Multi-domain] Cd Length: 222 Bit Score: 39.93 E-value: 1.85e-03
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| GMP_synthase_C | cd01997 | C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP ... |
328-357 | 2.86e-03 | |||||||||
C-terminal domain of GMP synthetase (glutamine-hydrolyzing); The C-terminal domain of GMP synthetase (glutamine-hydrolyzing, EC 6.3.5.2) contains two subdomains: the ATP pyrophosphatase domain at the N-terminal and the dimerization domain at the C-terminal end. The ATP-PPase domain is a twisted, five-stranded parallel beta-sheet sandwiched between helical layers. It has a signature nucleotide-binding motif, or PP-loop, at the end of the first-beta strand. GMP synthetase is a homodimer, but in some archaea, it is a heterodimer made up of ATP pyrophosphatase (ATP-PPase) and a GATase subunit. In eukaryotes and bacteria, the two catalytic units are encoded by a single gene producing a two-domain-type GMP with a GATase domain in the N-terminus and an ATP-PPase domain in the C-terminus. Pssm-ID: 467501 [Multi-domain] Cd Length: 311 Bit Score: 40.22 E-value: 2.86e-03
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| MnmA_TRMU-like | cd01998 | MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ... |
328-402 | 4.32e-03 | |||||||||
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Pssm-ID: 467502 [Multi-domain] Cd Length: 349 Bit Score: 39.80 E-value: 4.32e-03
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| Asn_synthase_B_C | cd01991 | C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ... |
332-390 | 5.13e-03 | |||||||||
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase. Pssm-ID: 467495 [Multi-domain] Cd Length: 224 Bit Score: 38.79 E-value: 5.13e-03
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| nitrilases_CHs | cd07564 | Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ... |
17-51 | 9.70e-03 | |||||||||
Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases (nitrile aminohydrolases, EC:3.5.5.1) hydrolyze nitriles (RCN) to ammonia and the corresponding carboxylic acid. Most nitrilases prefer aromatic nitriles, some prefer arylacetonitriles and others aliphatic nitriles. This group includes the nitrilase cyanide dihydratase (CDH), which hydrolyzes inorganic cyanide (HCN) to produce formate. It also includes cyanide hydratase (CH), which hydrolyzes HCN to formamide. This group includes four Arabidopsis thaliana nitrilases (Ath)NIT1-4. AthNIT1-3 have a strong substrate preference for phenylpropionitrile (PPN) and other nitriles which may originate from the breakdown of glucosinolates. The product of PPN hydrolysis, phenylacetic acid has auxin activity. AthNIT1-3 can also convert indoacetonitrile to indole-3-acetic acid (IAA, auxin), but with a lower affinity and velocity. From their expression patterns, it has been speculated that NIT3 may produce IAA during the early stages of germination, and that NIT3 may produce IAA during embryo development and maturation. AthNIT4 has a strong substrate specificity for the nitrile, beta-cyano-L-alanine (Ala(CN)), an intermediate of cyanide detoxification. AthNIT4 has both a nitrilase activity and a nitrile hydratase (NHase) activity, which generate aspartic acid and asparagine respectively from Ala(CN). NHase catalyzes the hydration of nitriles to their corresponding amides. This subgroup belongs to a larger nitrilase superfamily comprised of belong 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 1. Pssm-ID: 143588 Cd Length: 297 Bit Score: 38.24 E-value: 9.70e-03
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