5-(carboxyamino)imidazole ribonucleotide mutase; phosphoribosylaminoimidazolesuccinocarboxamide synthase( domain architecture ID 10619781)
5-(carboxyamino)imidazole ribonucleotide mutase (PurE) catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR)| phosphoribosylaminoimidazolesuccinocarboxamide synthase catalyzes the conversion of 5-aminoimidazole-4-carboxyribonucleotide (CAIR) to 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) in the de novo biosynthesis of purine nucleotides
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic group of SAICAR synthetases represented by the Drosophila melanogaster, N-terminal, SAICAR synthetase domain of bifunctional Ade5. The Ade5 gene product (CAIR-SAICARs) catalyzes the sixth and seventh steps of the de novo biosynthesis of purine nucleotides (also reported as seventh and eighth steps). SAICAR synthetase converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.
:
Pssm-ID: 133471 Cd Length: 252 Bit Score: 496.04 E-value: 1.52e-172
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
629-782
6.73e-63
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
:
Pssm-ID: 273474 Cd Length: 156 Bit Score: 207.86 E-value: 6.73e-63
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
151-235
1.59e-18
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
:
Pssm-ID: 463994 Cd Length: 84 Bit Score: 80.77 E-value: 1.59e-18
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-91
4.39e-16
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
:
Pssm-ID: 463994 Cd Length: 84 Bit Score: 73.84 E-value: 4.39e-16
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic group of SAICAR synthetases represented by the Drosophila melanogaster, N-terminal, SAICAR synthetase domain of bifunctional Ade5. The Ade5 gene product (CAIR-SAICARs) catalyzes the sixth and seventh steps of the de novo biosynthesis of purine nucleotides (also reported as seventh and eighth steps). SAICAR synthetase converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.
Pssm-ID: 133471 Cd Length: 252 Bit Score: 496.04 E-value: 1.52e-172
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
629-782
6.73e-63
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273474 Cd Length: 156 Bit Score: 207.86 E-value: 6.73e-63
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
361-594
1.86e-57
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole-succinocarboxamide synthase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439922 Cd Length: 245 Bit Score: 196.07 E-value: 1.86e-57
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
629-765
2.88e-53
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 459917 Cd Length: 147 Bit Score: 181.03 E-value: 2.88e-53
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
627-774
1.22e-47
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyse the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 214965 Cd Length: 152 Bit Score: 165.78 E-value: 1.22e-47
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
151-235
1.59e-18
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
Pssm-ID: 463994 Cd Length: 84 Bit Score: 80.77 E-value: 1.59e-18
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-91
4.39e-16
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
Pssm-ID: 463994 Cd Length: 84 Bit Score: 73.84 E-value: 4.39e-16
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
628-712
3.07e-12
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439811 Cd Length: 161 Bit Score: 65.08 E-value: 3.07e-12
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
152-219
7.79e-11
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.
Pssm-ID: 213402 Cd Length: 66 Bit Score: 58.06 E-value: 7.79e-11
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
7-74
1.30e-07
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.
Pssm-ID: 213402 Cd Length: 66 Bit Score: 49.20 E-value: 1.30e-07
Ade5_like 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic group of SAICAR synthetases represented by the Drosophila melanogaster, N-terminal, SAICAR synthetase domain of bifunctional Ade5. The Ade5 gene product (CAIR-SAICARs) catalyzes the sixth and seventh steps of the de novo biosynthesis of purine nucleotides (also reported as seventh and eighth steps). SAICAR synthetase converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.
Pssm-ID: 133471 Cd Length: 252 Bit Score: 496.04 E-value: 1.52e-172
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; SAICAR synthetase (the PurC gene product) catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.
Pssm-ID: 133468 Cd Length: 230 Bit Score: 319.79 E-value: 2.98e-104
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole ...
629-782
6.73e-63
phosphoribosylaminoimidazole carboxylase, PurE protein; Phosphoribosylaminoimidazole carboxylase is a fusion protein in plants and fungi, but consists of two non-interacting proteins in bacteria, PurK and PurE. This model represents PurK, an N5-CAIR mutase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273474 Cd Length: 156 Bit Score: 207.86 E-value: 6.73e-63
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; ...
361-594
1.86e-57
Phosphoribosylaminoimidazole-succinocarboxamide synthase [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole-succinocarboxamide synthase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439922 Cd Length: 245 Bit Score: 196.07 E-value: 1.86e-57
bacterial and archaeal 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) ...
366-619
9.32e-55
bacterial and archaeal 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; A subfamily of SAICAR synthetases represented by the Thermotoga maritima (Tm) enzyme and E. coli PurC. SAICAR synthetase catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.
Pssm-ID: 133470 Cd Length: 230 Bit Score: 188.43 E-value: 9.32e-55
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl) ...
629-765
2.88e-53
AIR carboxylase; Members of this family catalyze the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyze the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 459917 Cd Length: 147 Bit Score: 181.03 E-value: 2.88e-53
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl) ...
627-774
1.22e-47
AIR carboxylase; Members of this family catalyse the decarboxylation of 1-(5-phosphoribosyl)-5-amino-4-imidazole-carboxylate (AIR). This family catalyse the sixth step of de novo purine biosynthesis. Some members of this family contain two copies of this domain.
Pssm-ID: 214965 Cd Length: 152 Bit Score: 165.78 E-value: 1.22e-47
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
151-235
1.59e-18
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
Pssm-ID: 463994 Cd Length: 84 Bit Score: 80.77 E-value: 1.59e-18
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb ...
6-91
4.39e-16
Myb/SANT-like DNA-binding domain; This presumed domain appears to be related to other Myb/SANT-like DNA binding domains. In particular pfam10545 seems most related. This family is greatly expanded in plants and appears in several proteins annotated as transposon proteins.
Pssm-ID: 463994 Cd Length: 84 Bit Score: 73.84 E-value: 4.39e-16
non-metazoan 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR) synthase; Eukaryotic, bacterial, and archaeal group of SAICAR synthetases represented by the Saccharomyces cerevisiae (Sc) enzyme, mostly absent in metazoans. SAICAR synthetase catalyzes the seventh step of the de novo biosynthesis of purine nucleotides (also reported as eighth step). It converts 5-aminoimidazole-4-carboxyribonucleotide (CAIR), ATP, and L-aspartate into 5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide (SAICAR), ADP, and phosphate.
Pssm-ID: 133469 [Multi-domain] Cd Length: 279 Bit Score: 73.74 E-value: 3.56e-14
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; ...
628-712
3.07e-12
Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase [Nucleotide transport and metabolism]; Phosphoribosylcarboxyaminoimidazole (NCAIR) mutase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439811 Cd Length: 161 Bit Score: 65.08 E-value: 3.07e-12
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
152-219
7.79e-11
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.
Pssm-ID: 213402 Cd Length: 66 Bit Score: 58.06 E-value: 7.79e-11
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription ...
7-74
1.30e-07
GT1, myb-like, SANT family; GT-1, a myb-like protein, is one of the GT trihelix transcription factors. GT-1 binds the GT cis-element of rbcS-3A, a light-induced gene, as a dimer. Arabidopsis GT-1 is a trans-activator and acts in the stabilization of components of the transcription pre-initiation complex comprised of TFIIA-TBP-TATA. The isolated GT-1 DNA-binding domain is sufficient to bind DNA. This region closely resembles the myb domain, but with longer helices. It has been proposed that GT-1 may respond to light signals via calcium-dependent phosphorylation to create a light-modulated molecular switch. These proteins are members of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of the DNA-binding Myb domains and is found in a diverse set of proteins.
Pssm-ID: 213402 Cd Length: 66 Bit Score: 49.20 E-value: 1.30e-07
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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