phosphoribosylformylglycinamidine synthase subunit PurQ [Bacillus cereus]
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 | 4.83e-167 | ||||
phosphoribosylformylglycinamidine synthase subunit PurQ; : Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 458.81 E-value: 4.83e-167
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| Name | Accession | Description | Interval | E-value | |||||
| PRK03619 | PRK03619 | phosphoribosylformylglycinamidine synthase subunit PurQ; |
1-217 | 4.83e-167 | |||||
phosphoribosylformylglycinamidine synthase subunit PurQ; Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 458.81 E-value: 4.83e-167
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| PurL2 | COG0047 | Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
1-220 | 5.99e-140 | |||||
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: 390.96 E-value: 5.99e-140
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| FGAM_synth_I | TIGR01737 | phosphoribosylformylglycinamidine synthase I; In some species, ... |
1-219 | 5.77e-124 | |||||
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: 350.53 E-value: 5.77e-124
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| GATase1_FGAR_AT | cd01740 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
3-216 | 2.45e-115 | |||||
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: 328.81 E-value: 2.45e-115
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| GATase_5 | pfam13507 | CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
2-214 | 9.19e-62 | |||||
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: 193.48 E-value: 9.19e-62
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| Name | Accession | Description | Interval | E-value | |||||
| PRK03619 | PRK03619 | phosphoribosylformylglycinamidine synthase subunit PurQ; |
1-217 | 4.83e-167 | |||||
phosphoribosylformylglycinamidine synthase subunit PurQ; Pssm-ID: 235140 [Multi-domain] Cd Length: 219 Bit Score: 458.81 E-value: 4.83e-167
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| PurL2 | COG0047 | Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ... |
1-220 | 5.99e-140 | |||||
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: 390.96 E-value: 5.99e-140
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| FGAM_synth_I | TIGR01737 | phosphoribosylformylglycinamidine synthase I; In some species, ... |
1-219 | 5.77e-124 | |||||
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: 350.53 E-value: 5.77e-124
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| GATase1_FGAR_AT | cd01740 | Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ... |
3-216 | 2.45e-115 | |||||
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: 328.81 E-value: 2.45e-115
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| PRK01175 | PRK01175 | phosphoribosylformylglycinamidine synthase I; Provisional |
1-198 | 5.64e-69 | |||||
phosphoribosylformylglycinamidine synthase I; Provisional Pssm-ID: 234913 [Multi-domain] Cd Length: 261 Bit Score: 212.31 E-value: 5.64e-69
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| GATase_5 | pfam13507 | CobB/CobQ-like glutamine amidotransferase domain; This family captures members that are not ... |
2-214 | 9.19e-62 | |||||
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: 193.48 E-value: 9.19e-62
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| PRK05297 | PRK05297 | phosphoribosylformylglycinamidine synthase; Provisional |
10-199 | 2.30e-31 | |||||
phosphoribosylformylglycinamidine synthase; Provisional Pssm-ID: 235394 [Multi-domain] Cd Length: 1290 Bit Score: 121.06 E-value: 2.30e-31
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| FGAM_synt | TIGR01735 | phosphoribosylformylglycinamidine synthase, single chain form; This model represents a ... |
2-199 | 1.13e-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: 116.04 E-value: 1.13e-29
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| PLN03206 | PLN03206 | phosphoribosylformylglycinamidine synthase; Provisional |
2-198 | 5.62e-27 | |||||
phosphoribosylformylglycinamidine synthase; Provisional Pssm-ID: 178745 [Multi-domain] Cd Length: 1307 Bit Score: 108.32 E-value: 5.62e-27
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-93 | 1.32e-16 | |||||
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: 73.02 E-value: 1.32e-16
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
4-92 | 1.81e-15 | |||||
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: 69.15 E-value: 1.81e-15
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| hisH | PRK13141 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
23-221 | 4.07e-12 | |||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 62.84 E-value: 4.07e-12
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| GATase1_PfpI_like | cd03134 | A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ... |
40-100 | 8.95e-12 | |||||
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: 61.02 E-value: 8.95e-12
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| GATase_3 | pfam07685 | CobB/CobQ-like glutamine amidotransferase domain; |
4-92 | 1.95e-11 | |||||
CobB/CobQ-like glutamine amidotransferase domain; Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 60.72 E-value: 1.95e-11
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| YajL | COG0693 | Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ... |
38-100 | 9.28e-11 | |||||
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: 58.58 E-value: 9.28e-11
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| GATase1_CobQ | cd01750 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
4-92 | 1.38e-10 | |||||
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: 58.41 E-value: 1.38e-10
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| GATase | pfam00117 | Glutamine amidotransferase class-I; |
24-196 | 6.20e-10 | |||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 56.48 E-value: 6.20e-10
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| DJ-1_PfpI | pfam01965 | DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
29-100 | 1.21e-09 | |||||
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: 55.34 E-value: 1.21e-09
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| CobQ | COG1492 | Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ... |
4-99 | 3.04e-09 | |||||
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: 56.22 E-value: 3.04e-09
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| GATase1_IGP_Synthase | cd01748 | Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
23-109 | 5.02e-09 | |||||
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: 54.04 E-value: 5.02e-09
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| GATase1_PfpI_1 | cd03169 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
5-100 | 1.83e-08 | |||||
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: 52.27 E-value: 1.83e-08
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| GATase1_CTP_Synthase | cd01746 | Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
24-93 | 2.90e-08 | |||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 52.56 E-value: 2.90e-08
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| HisH | COG0118 | Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
25-109 | 8.12e-08 | |||||
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 50.81 E-value: 8.12e-08
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| PuuD | COG2071 | Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
34-92 | 4.60e-07 | |||||
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism]; Pssm-ID: 441674 [Multi-domain] Cd Length: 231 Bit Score: 49.01 E-value: 4.60e-07
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| PRK00784 | PRK00784 | cobyric acid synthase; |
4-99 | 7.41e-07 | |||||
cobyric acid synthase; Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 48.93 E-value: 7.41e-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 | 7.45e-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: 47.55 E-value: 7.45e-07
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| PfpI | TIGR01382 | intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ... |
38-100 | 9.65e-07 | |||||
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides] Pssm-ID: 273591 [Multi-domain] Cd Length: 166 Bit Score: 47.41 E-value: 9.65e-07
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| PRK13527 | PRK13527 | glutamine amidotransferase subunit PdxT; Provisional |
1-88 | 1.75e-06 | |||||
glutamine amidotransferase subunit PdxT; Provisional Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 46.80 E-value: 1.75e-06
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| PRK06186 | PRK06186 | hypothetical protein; Validated |
23-90 | 1.97e-06 | |||||
hypothetical protein; Validated Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 47.27 E-value: 1.97e-06
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| hisH | PRK13143 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
34-109 | 5.44e-06 | |||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 45.63 E-value: 5.44e-06
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| pyrG | PRK05380 | CTP synthetase; Validated |
37-93 | 1.37e-05 | |||||
CTP synthetase; Validated Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 45.40 E-value: 1.37e-05
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| GATase1_PB | cd01749 | Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
20-88 | 1.75e-05 | |||||
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6. Pssm-ID: 153220 [Multi-domain] Cd Length: 183 Bit Score: 43.67 E-value: 1.75e-05
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| IMP_synth_hisH | TIGR01855 | imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
35-221 | 2.00e-05 | |||||
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family] Pssm-ID: 273836 [Multi-domain] Cd Length: 196 Bit Score: 43.85 E-value: 2.00e-05
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| PRK01077 | PRK01077 | cobyrinate a,c-diamide synthase; |
34-100 | 3.68e-05 | |||||
cobyrinate a,c-diamide synthase; Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 43.97 E-value: 3.68e-05
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| PyrG | COG0504 | CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
37-93 | 8.27e-05 | |||||
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 43.07 E-value: 8.27e-05
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| GATase1_CPSase | cd01744 | Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
40-196 | 8.96e-05 | |||||
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I. Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 41.71 E-value: 8.96e-05
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| GATase1_1 | cd01741 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
14-94 | 1.06e-04 | |||||
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: 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. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 41.46 E-value: 1.06e-04
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| hisH | PRK13181 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
35-104 | 1.51e-04 | |||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 41.39 E-value: 1.51e-04
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| GuaA1 | COG0518 | GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
24-94 | 1.65e-04 | |||||
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 41.47 E-value: 1.65e-04
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| GATase1_2 | cd01745 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
35-92 | 2.24e-04 | |||||
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: 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. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 40.64 E-value: 2.24e-04
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| GlxA | COG4977 | Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
1-98 | 2.74e-04 | |||||
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: 40.91 E-value: 2.74e-04
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| PabA | COG0512 | Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
24-94 | 3.63e-04 | |||||
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 40.02 E-value: 3.63e-04
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| GATase1_CobB | cd03130 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ... |
34-101 | 3.65e-04 | |||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB 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 CobB. Pssm-ID: 153224 [Multi-domain] Cd Length: 198 Bit Score: 40.27 E-value: 3.65e-04
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| GATase1_PfpI_3 | cd03140 | Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
29-98 | 6.13e-04 | |||||
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: 153234 [Multi-domain] Cd Length: 170 Bit Score: 39.13 E-value: 6.13e-04
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| COG3442 | COG3442 | Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ... |
25-92 | 7.90e-04 | |||||
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only]; Pssm-ID: 442666 [Multi-domain] Cd Length: 241 Bit Score: 39.39 E-value: 7.90e-04
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| GATase1_Anthranilate_Synthase | cd01743 | Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
24-94 | 1.24e-03 | |||||
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA. Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 38.28 E-value: 1.24e-03
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| hisH | PRK14004 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
30-95 | 1.31e-03 | |||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 38.73 E-value: 1.31e-03
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| GATase1_AraC_2 | cd03138 | AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
32-100 | 1.31e-03 | |||||
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: 38.40 E-value: 1.31e-03
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| hisH | PRK13146 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
26-97 | 1.83e-03 | |||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 38.22 E-value: 1.83e-03
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| PLN02327 | PLN02327 | CTP synthase |
37-93 | 1.94e-03 | |||||
CTP synthase Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 38.85 E-value: 1.94e-03
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| GATase1_Hsp31_like | cd03141 | Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ... |
38-134 | 2.20e-03 | |||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers. Pssm-ID: 153235 [Multi-domain] Cd Length: 221 Bit Score: 37.92 E-value: 2.20e-03
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| GATase1_AraC_ArgR_like | cd03136 | AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ... |
37-100 | 2.41e-03 | |||||
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: 37.57 E-value: 2.41e-03
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| Peptidase_C26 | pfam07722 | Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
39-92 | 2.73e-03 | |||||
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus. Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 37.62 E-value: 2.73e-03
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| PRK13525 | PRK13525 | pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
36-88 | 3.13e-03 | |||||
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 37.45 E-value: 3.13e-03
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