pantetheine hydrolase VNN2 isoform X3 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| biotinidase_like | cd07567 | biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ... |
1-276 | 4.30e-150 | |||||
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. 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 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. : Pssm-ID: 143591 Cd Length: 299 Bit Score: 429.36 E-value: 4.30e-150
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| Vanin_C | pfam19018 | Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ... |
291-434 | 5.47e-36 | |||||
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins. : Pssm-ID: 465946 Cd Length: 165 Bit Score: 130.56 E-value: 5.47e-36
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| Name | Accession | Description | Interval | E-value | |||||
| biotinidase_like | cd07567 | biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ... |
1-276 | 4.30e-150 | |||||
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. 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 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143591 Cd Length: 299 Bit Score: 429.36 E-value: 4.30e-150
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| Vanin_C | pfam19018 | Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ... |
291-434 | 5.47e-36 | |||||
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins. Pssm-ID: 465946 Cd Length: 165 Bit Score: 130.56 E-value: 5.47e-36
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| Nit2 | COG0388 | Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
3-231 | 4.78e-24 | |||||
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 100.71 E-value: 4.78e-24
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| CN_hydrolase | pfam00795 | Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
3-231 | 1.26e-13 | |||||
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: 70.46 E-value: 1.26e-13
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| PLN02747 | PLN02747 | N-carbamolyputrescine amidase |
3-252 | 7.62e-08 | |||||
N-carbamolyputrescine amidase Pssm-ID: 215398 Cd Length: 296 Bit Score: 53.62 E-value: 7.62e-08
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| lnt | TIGR00546 | apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
2-163 | 2.04e-04 | |||||
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair] Pssm-ID: 273129 [Multi-domain] Cd Length: 391 Bit Score: 43.50 E-value: 2.04e-04
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| Name | Accession | Description | Interval | E-value | |||||
| biotinidase_like | cd07567 | biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin ... |
1-276 | 4.30e-150 | |||||
biotinidase and vanins (class 4 nitrilases); These secondary amidases participate in vitamin recycling. Biotinidase (EC 3.5.1.12) has both a hydrolase and a transferase activity. It hydrolyzes free biocytin or small biotinyl-peptides produced during the proteolytic degradation of biotin-dependent carboxylases, to release free biotin (vitamin H), and it can transfer biotin to acceptor molecules such as histones. Biotinidase deficiency in humans is an autosomal recessive disorder characterized by neurological and cutaneous symptoms. This subgroup includes the three human vanins, vanin1-3. Vanins are ectoenzymes, Vanin-1, and -2 are membrane associated, vanin-3 is secreted. They are pantotheinases (EC 3.5.1.92, pantetheine hydrolase), which convert pantetheine, to pantothenic acid (vitamin B5) and cysteamine (2-aminoethanethiol, a potent anti-oxidant). They are potential targets for therapeutic intervention in inflammatory disorders. Vanin-1 deficient mice lacking free cysteamine are less susceptible to intestinal inflammation, and expression of vanin-1 and -3 is induced as part of the inflammatory-regenerative differentiation program of human epidermis. 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 4. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. Pssm-ID: 143591 Cd Length: 299 Bit Score: 429.36 E-value: 4.30e-150
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| Vanin_C | pfam19018 | Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related ... |
291-434 | 5.47e-36 | |||||
Vanin C-terminal domain; This domain is found at the C terminus of Vanin 1 and related proteins. Pssm-ID: 465946 Cd Length: 165 Bit Score: 130.56 E-value: 5.47e-36
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| nitrilase | cd07197 | Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing ... |
1-252 | 2.56e-33 | |||||
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: 126.29 E-value: 2.56e-33
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| Nit2 | COG0388 | Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; |
3-231 | 4.78e-24 | |||||
Omega-amidase YafV/Nit2, hydrolyzes alpha-ketoglutaramate [Energy production and conversion]; Pssm-ID: 440157 [Multi-domain] Cd Length: 264 Bit Score: 100.71 E-value: 4.78e-24
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| nit | cd07572 | Nit1, Nit 2, and related proteins, and the Nit1-like domain of NitFhit (class 10 nitrilases); ... |
3-163 | 2.41e-20 | |||||
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: 90.18 E-value: 2.41e-20
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| nitrilase_3 | cd07581 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
3-185 | 3.80e-15 | |||||
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: 74.92 E-value: 3.80e-15
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| nitrilase_5 | cd07583 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
3-163 | 4.49e-15 | |||||
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: 74.88 E-value: 4.49e-15
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| nitrilase_1_R1 | cd07578 | First nitrilase domain of an uncharacterized subgroup of the nitrilase superfamily (putative ... |
3-186 | 2.95e-14 | |||||
First 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 first 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: 143602 Cd Length: 258 Bit Score: 72.56 E-value: 2.95e-14
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| nitrilase_6 | cd07584 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
4-254 | 9.91e-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: 70.86 E-value: 9.91e-14
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| CN_hydrolase | pfam00795 | Carbon-nitrogen hydrolase; This family contains hydrolases that break carbon-nitrogen bonds. ... |
3-231 | 1.26e-13 | |||||
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: 70.46 E-value: 1.26e-13
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| CPA | cd07573 | N-carbamoylputrescine amidohydrolase (CPA) (class 11 nitrilases); CPA (EC 3.5.1.53, also known ... |
3-163 | 3.30e-12 | |||||
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: 66.82 E-value: 3.30e-12
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| nitrilase_2 | cd07580 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
4-185 | 8.09e-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: 62.36 E-value: 8.09e-11
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| R-amidase_like | cd07576 | Pseudomonas sp. MCI3434 R-amidase and related proteins (putative class 13 nitrilases); ... |
3-186 | 4.33e-09 | |||||
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: 57.20 E-value: 4.33e-09
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| Ph0642_like | cd07577 | Pyrococcus horikoshii Ph0642 and related proteins, members of the nitrilase superfamily ... |
8-231 | 7.64e-09 | |||||
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: 56.54 E-value: 7.64e-09
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| nitrilase_7 | cd07585 | Uncharacterized subgroup of the nitrilase superfamily (putative class 13 nitrilases); The ... |
4-163 | 3.23e-08 | |||||
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: 54.63 E-value: 3.23e-08
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| PLN02747 | PLN02747 | N-carbamolyputrescine amidase |
3-252 | 7.62e-08 | |||||
N-carbamolyputrescine amidase Pssm-ID: 215398 Cd Length: 296 Bit Score: 53.62 E-value: 7.62e-08
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| ML_beta-AS_like | cd07568 | mammalian-like beta-alanine synthase (beta-AS) and similar proteins (class 5 nitrilases); This ... |
5-163 | 9.73e-08 | |||||
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: 53.27 E-value: 9.73e-08
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| PLN02798 | PLN02798 | nitrilase |
4-184 | 1.06e-06 | |||||
nitrilase Pssm-ID: 215428 Cd Length: 286 Bit Score: 50.13 E-value: 1.06e-06
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| nitrilases_CHs | cd07564 | Nitrilases, cyanide hydratase (CH)s, and similar proteins (class 1 nitrilases); Nitrilases ... |
5-154 | 7.74e-06 | |||||
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: 47.48 E-value: 7.74e-06
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| Lnt | COG0815 | Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; |
3-163 | 3.72e-05 | |||||
Apolipoprotein N-acyltransferase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440577 [Multi-domain] Cd Length: 472 Bit Score: 45.99 E-value: 3.72e-05
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| ALP_N-acyl_transferase | cd07571 | Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an ... |
3-163 | 6.26e-05 | |||||
Apolipoprotein N-acyl transferase (class 9 nitrilases); ALP N-acyl transferase (Lnt), is an essential membrane-bound enzyme in gram-negative bacteria, which catalyzes the N-acylation of apolipoproteins, the final step in lipoprotein maturation. This is a reverse amidase (i.e. condensation) reaction. 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 9. Pssm-ID: 143595 Cd Length: 270 Bit Score: 44.51 E-value: 6.26e-05
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| nitrilase_Rim1_like | cd07574 | Uncharacterized subgroup of the nitrilase superfamily; some members of this subgroup have an ... |
5-184 | 1.56e-04 | |||||
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: 43.34 E-value: 1.56e-04
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| lnt | TIGR00546 | apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the ... |
2-163 | 2.04e-04 | |||||
apolipoprotein N-acyltransferase; This enzyme transfers the acyl group to lipoproteins in the lgt/lsp/lnt system which is found broadly in bacteria but not in archaea. This model represents one component of the "lipoprotein lgt/lsp/lnt system" genome property. [Protein fate, Protein modification and repair] Pssm-ID: 273129 [Multi-domain] Cd Length: 391 Bit Score: 43.50 E-value: 2.04e-04
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