phosphoribosylformylglycinamidine synthase subunit PurQ [Lacticaseibacillus paracasei]
Protein Classification
phosphoribosylformylglycinamidine synthase subunit PurQ( domain architecture ID 10012055)
phosphoribosylformylglycinamidine synthase subunit PurQ is part of the complex that catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate; subunit PurQ produces an ammonia molecule by converting glutamine to glutamate
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PRK03619 | PRK03619 | phosphoribosylformylglycinamidine synthase subunit PurQ; |
1-217 | 4.67e-149 | ||||
phosphoribosylformylglycinamidine synthase subunit PurQ; : Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 413.36 E-value: 4.67e-149
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| Name | Accession | Description | Interval | E-value | |||||
| PRK03619 | PRK03619 | phosphoribosylformylglycinamidine synthase subunit PurQ; |
1-217 | 4.67e-149 | |||||
phosphoribosylformylglycinamidine synthase subunit PurQ; Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 413.36 E-value: 4.67e-149
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| PurL2 | COG0047 | Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
1-217 | 2.32e-125 | |||||
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 439817 [Multi-domain] Cd Length: 236 Bit Score: 354.36 E-value: 2.32e-125
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| FGAM_synth_I | TIGR01737 | phosphoribosylformylglycinamidine synthase I; In some species, ... |
1-216 | 1.12e-113 | |||||
phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273782 [Multi-domain] Cd Length: 227 Bit Score: 324.33 E-value: 1.12e-113
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| GATase1_FGAR_AT | cd01740 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
3-216 | 2.06e-102 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 296.06 E-value: 2.06e-102
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| GATase_5 | pfam13507 | CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
2-217 | 3.53e-59 | |||||
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230. Pssm-ID: 463904 [Multi-domain] Cd Length: 260 Bit Score: 186.94 E-value: 3.53e-59
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| Name | Accession | Description | Interval | E-value | |||||
| PRK03619 | PRK03619 | phosphoribosylformylglycinamidine synthase subunit PurQ; |
1-217 | 4.67e-149 | |||||
phosphoribosylformylglycinamidine synthase subunit PurQ; Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 413.36 E-value: 4.67e-149
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| PurL2 | COG0047 | Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
1-217 | 2.32e-125 | |||||
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 439817 [Multi-domain] Cd Length: 236 Bit Score: 354.36 E-value: 2.32e-125
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| FGAM_synth_I | TIGR01737 | phosphoribosylformylglycinamidine synthase I; In some species, ... |
1-216 | 1.12e-113 | |||||
phosphoribosylformylglycinamidine synthase I; In some species, phosphoribosylformylglycinamidine synthase is composed of a single polypeptide chain. This model describes the PurQ protein of Bacillus subtilis (where PurL, PurQ, and PurS are required for phosphoribosylformylglycinamidine synthase activity) and functionally equivalent proteins from other bacteria and archaea. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 273782 [Multi-domain] Cd Length: 227 Bit Score: 324.33 E-value: 1.12e-113
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| GATase1_FGAR_AT | cd01740 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
3-216 | 2.06e-102 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site Pssm-ID: 153211 [Multi-domain] Cd Length: 238 Bit Score: 296.06 E-value: 2.06e-102
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| PRK01175 | PRK01175 | phosphoribosylformylglycinamidine synthase I; Provisional |
1-221 | 2.70e-60 | |||||
phosphoribosylformylglycinamidine synthase I; Provisional Pssm-ID: 234913 [Multi-domain] Cd Length: 261 Bit Score: 189.97 E-value: 2.70e-60
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| GATase_5 | pfam13507 | CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
2-217 | 3.53e-59 | |||||
CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not found in pfam00310, pfam07685 and pfam13230. Pssm-ID: 463904 [Multi-domain] Cd Length: 260 Bit Score: 186.94 E-value: 3.53e-59
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| FGAM_synt | TIGR01735 | phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ... |
2-201 | 3.10e-29 | |||||
phosphoribosylformylglycinamidine synthase, single chain form; This model represents a single-molecule form of phosphoribosylformylglycinamidine synthase, also called FGAM synthase, an enzyme of purine de novo biosynthesis. This form is found mostly in eukaryotes and Proteobacteria. In Bacillus subtilis PurL (FGAM synthase II) and PurQ (FGAM synthase I), homologous to different parts of this model, perform the equivalent function; the unrelated small protein PurS is also required and may be a third subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 188163 [Multi-domain] Cd Length: 1310 Bit Score: 114.88 E-value: 3.10e-29
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| PRK05297 | PRK05297 | phosphoribosylformylglycinamidine synthase; Provisional |
2-199 | 3.01e-25 | |||||
phosphoribosylformylglycinamidine synthase; Provisional Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 103.34 E-value: 3.01e-25
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| PLN03206 | PLN03206 | phosphoribosylformylglycinamidine synthase; Provisional |
2-198 | 1.32e-19 | |||||
phosphoribosylformylglycinamidine synthase; Provisional Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 87.13 E-value: 1.32e-19
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-92 | 2.23e-10 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 56.07 E-value: 2.23e-10
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-92 | 9.83e-10 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain. Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 53.74 E-value: 9.83e-10
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| YajL | COG0693 | Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
32-100 | 5.80e-08 | |||||
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms]; Pssm-ID: 440457 [Multi-domain] Cd Length: 170 Bit Score: 50.87 E-value: 5.80e-08
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| GATase1_CobQ | cd01750 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
26-92 | 2.12e-07 | |||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ. Pssm-ID: 153221 [Multi-domain] Cd Length: 194 Bit Score: 49.55 E-value: 2.12e-07
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| DJ-1_PfpI | pfam01965 | DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
41-100 | 2.52e-07 | |||||
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators. Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 48.79 E-value: 2.52e-07
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| GATase1_DJ-1 | cd03135 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ... |
35-100 | 5.24e-07 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme. Pssm-ID: 153229 [Multi-domain] Cd Length: 163 Bit Score: 47.93 E-value: 5.24e-07
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| GATase_3 | pfam07685 | CobB/CobQ-like glutamine amidotransferase domain; |
42-94 | 1.01e-06 | |||||
CobB/CobQ-like glutamine amidotransferase domain; Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 47.62 E-value: 1.01e-06
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| GATase1_AraC_2 | cd03138 | AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
38-100 | 3.82e-06 | |||||
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153232 [Multi-domain] Cd Length: 195 Bit Score: 46.10 E-value: 3.82e-06
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| GATase1_PfpI_like | cd03134 | A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ... |
42-100 | 3.96e-06 | |||||
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704. Pssm-ID: 153228 [Multi-domain] Cd Length: 165 Bit Score: 45.61 E-value: 3.96e-06
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| GlxA | COG4977 | Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
38-98 | 8.69e-06 | |||||
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription]; Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 45.53 E-value: 8.69e-06
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| CobQ | COG1492 | Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ... |
4-92 | 1.91e-05 | |||||
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441101 [Multi-domain] Cd Length: 493 Bit Score: 44.66 E-value: 1.91e-05
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| PRK00784 | PRK00784 | cobyric acid synthase; |
4-92 | 4.38e-05 | |||||
cobyric acid synthase; Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 43.92 E-value: 4.38e-05
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| GATase1_AraC_1 | cd03137 | AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
38-100 | 3.17e-04 | |||||
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153231 [Multi-domain] Cd Length: 187 Bit Score: 40.18 E-value: 3.17e-04
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| GATase1_AraC_ArgR_like | cd03136 | AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ... |
37-100 | 5.75e-04 | |||||
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153230 [Multi-domain] Cd Length: 185 Bit Score: 39.49 E-value: 5.75e-04
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| hisH | PRK13141 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
25-197 | 5.81e-04 | |||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 39.73 E-value: 5.81e-04
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| GATase1_PfpI_2 | cd03139 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
37-100 | 1.30e-03 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153233 [Multi-domain] Cd Length: 183 Bit Score: 38.29 E-value: 1.30e-03
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| COG3442 | COG3442 | Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ... |
38-92 | 1.76e-03 | |||||
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only]; Pssm-ID: 442666 [Multi-domain] Cd Length: 241 Bit Score: 38.23 E-value: 1.76e-03
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| GATase1_PfpI_1 | cd03169 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
38-127 | 2.08e-03 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Pssm-ID: 153243 [Multi-domain] Cd Length: 180 Bit Score: 37.63 E-value: 2.08e-03
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| PRK06278 | PRK06278 | cobyrinic acid a,c-diamide synthase; Validated |
43-94 | 2.25e-03 | |||||
cobyrinic acid a,c-diamide synthase; Validated Pssm-ID: 180505 [Multi-domain] Cd Length: 476 Bit Score: 38.48 E-value: 2.25e-03
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| GATase1_IGP_Synthase | cd01748 | Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
25-100 | 6.78e-03 | |||||
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 36.32 E-value: 6.78e-03
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