MULTISPECIES: cobyric acid synthase [Corynebacterium]
Protein Classification
CobQ family protein( domain architecture ID 11445265)
CobQ family protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| CobQ | COG1492 | Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ... |
3-472 | 0e+00 | ||||||||
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: 686.02 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||||
| CobQ | COG1492 | Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ... |
3-472 | 0e+00 | ||||||||
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: 686.02 E-value: 0e+00
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| PRK00784 | PRK00784 | cobyric acid synthase; |
3-477 | 0e+00 | ||||||||
cobyric acid synthase; Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 672.56 E-value: 0e+00
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| cobQ | TIGR00313 | cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, ... |
7-472 | 4.87e-141 | ||||||||
cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 129413 [Multi-domain] Cd Length: 475 Bit Score: 413.80 E-value: 4.87e-141
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| CobQ_N | cd05389 | N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ... |
7-226 | 1.65e-117 | ||||||||
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid. Pssm-ID: 349774 Cd Length: 223 Bit Score: 344.19 E-value: 1.65e-117
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| CbiA | pfam01656 | CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
8-231 | 2.50e-49 | ||||||||
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family. Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 168.68 E-value: 2.50e-49
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| Name | Accession | Description | Interval | E-value | ||||||||
| CobQ | COG1492 | Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ... |
3-472 | 0e+00 | ||||||||
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: 686.02 E-value: 0e+00
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| PRK00784 | PRK00784 | cobyric acid synthase; |
3-477 | 0e+00 | ||||||||
cobyric acid synthase; Pssm-ID: 234838 [Multi-domain] Cd Length: 488 Bit Score: 672.56 E-value: 0e+00
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| cobQ | TIGR00313 | cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, ... |
7-472 | 4.87e-141 | ||||||||
cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 129413 [Multi-domain] Cd Length: 475 Bit Score: 413.80 E-value: 4.87e-141
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| CobQ_N | cd05389 | N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ... |
7-226 | 1.65e-117 | ||||||||
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid. Pssm-ID: 349774 Cd Length: 223 Bit Score: 344.19 E-value: 1.65e-117
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| GATase1_CobQ | cd01750 | Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ... |
261-433 | 1.42e-49 | ||||||||
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: 168.19 E-value: 1.42e-49
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| CbiA | pfam01656 | CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ... |
8-231 | 2.50e-49 | ||||||||
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family. Pssm-ID: 426369 [Multi-domain] Cd Length: 228 Bit Score: 168.68 E-value: 2.50e-49
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| GATase_3 | pfam07685 | CobB/CobQ-like glutamine amidotransferase domain; |
261-426 | 2.16e-38 | ||||||||
CobB/CobQ-like glutamine amidotransferase domain; Pssm-ID: 429595 [Multi-domain] Cd Length: 189 Bit Score: 138.14 E-value: 2.16e-38
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| GATase1_IGP_Synthase | cd01748 | Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
269-371 | 1.17e-16 | ||||||||
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: 78.31 E-value: 1.17e-16
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| HisH | COG0118 | Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
269-371 | 3.18e-16 | ||||||||
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: 77.00 E-value: 3.18e-16
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| hisH | PRK13181 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
283-370 | 5.10e-16 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 183878 [Multi-domain] Cd Length: 199 Bit Score: 76.44 E-value: 5.10e-16
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| PtaN | COG0857 | BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; |
7-231 | 1.04e-12 | ||||||||
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only]; Pssm-ID: 440618 [Multi-domain] Cd Length: 697 Bit Score: 70.24 E-value: 1.04e-12
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| AAA_26 | pfam13500 | AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ... |
7-231 | 1.38e-12 | ||||||||
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif. Pssm-ID: 433259 [Multi-domain] Cd Length: 198 Bit Score: 66.51 E-value: 1.38e-12
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| DTBS | cd03109 | dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ... |
7-203 | 2.78e-12 | ||||||||
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors. Pssm-ID: 349763 [Multi-domain] Cd Length: 189 Bit Score: 65.28 E-value: 2.78e-12
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| BioD | COG0132 | Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ... |
14-231 | 1.35e-11 | ||||||||
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis Pssm-ID: 439902 [Multi-domain] Cd Length: 222 Bit Score: 64.02 E-value: 1.35e-11
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| hisH | PRK13141 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
269-366 | 1.66e-11 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 63.61 E-value: 1.66e-11
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| hisH | PRK13170 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
283-371 | 6.54e-11 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 183877 [Multi-domain] Cd Length: 196 Bit Score: 61.41 E-value: 6.54e-11
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| IMP_synth_hisH | TIGR01855 | imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
283-371 | 1.65e-10 | ||||||||
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: 60.42 E-value: 1.65e-10
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| hisH | PRK13146 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
282-371 | 5.69e-10 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 59.03 E-value: 5.69e-10
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| GAT1_Peptidase_E | cd03146 | Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine ... |
298-409 | 6.21e-08 | ||||||||
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. 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 typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus PepE is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption. Pssm-ID: 153240 [Multi-domain] Cd Length: 212 Bit Score: 53.05 E-value: 6.21e-08
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| CobB | COG1797 | Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ... |
1-381 | 1.20e-07 | ||||||||
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis Pssm-ID: 441402 [Multi-domain] Cd Length: 459 Bit Score: 53.96 E-value: 1.20e-07
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| hisH | PRK13143 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
283-366 | 1.19e-06 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 49.10 E-value: 1.19e-06
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
261-366 | 1.45e-06 | ||||||||
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: 47.21 E-value: 1.45e-06
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| COG3442 | COG3442 | Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ... |
297-421 | 2.84e-06 | ||||||||
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only]; Pssm-ID: 442666 [Multi-domain] Cd Length: 241 Bit Score: 48.63 E-value: 2.84e-06
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| hisH | PRK14004 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
288-381 | 4.15e-06 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 172505 [Multi-domain] Cd Length: 210 Bit Score: 47.59 E-value: 4.15e-06
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| PRK05632 | PRK05632 | phosphate acetyltransferase; Reviewed |
7-231 | 1.77e-05 | ||||||||
phosphate acetyltransferase; Reviewed Pssm-ID: 235537 [Multi-domain] Cd Length: 684 Bit Score: 47.46 E-value: 1.77e-05
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
295-345 | 2.78e-05 | ||||||||
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: 42.57 E-value: 2.78e-05
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| PepE | COG3340 | Peptidase E [Amino acid transport and metabolism]; |
295-367 | 6.25e-05 | ||||||||
Peptidase E [Amino acid transport and metabolism]; Pssm-ID: 442569 [Multi-domain] Cd Length: 212 Bit Score: 44.03 E-value: 6.25e-05
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| CobB_N | cd05388 | N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ... |
4-39 | 7.24e-05 | ||||||||
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain. Pssm-ID: 349773 [Multi-domain] Cd Length: 193 Bit Score: 43.74 E-value: 7.24e-05
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| PRK01077 | PRK01077 | cobyrinate a,c-diamide synthase; |
1-39 | 9.89e-05 | ||||||||
cobyrinate a,c-diamide synthase; Pssm-ID: 234896 [Multi-domain] Cd Length: 451 Bit Score: 44.74 E-value: 9.89e-05
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| PRK13527 | PRK13527 | glutamine amidotransferase subunit PdxT; Provisional |
275-371 | 4.70e-04 | ||||||||
glutamine amidotransferase subunit PdxT; Provisional Pssm-ID: 237412 [Multi-domain] Cd Length: 200 Bit Score: 41.41 E-value: 4.70e-04
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| cobB | TIGR00379 | cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, ... |
7-226 | 4.81e-04 | ||||||||
cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, the cobB (cbiA in Salmonella) protein of cobalamin biosynthesis. It is responsible for the amidation of carboxylic groups at positions A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP hydrogenolyzed for each amidation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin] Pssm-ID: 273044 [Multi-domain] Cd Length: 449 Bit Score: 42.48 E-value: 4.81e-04
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| PRK13525 | PRK13525 | pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; |
299-374 | 5.18e-04 | ||||||||
pyridoxal 5'-phosphate synthase glutaminase subunit PdxT; Pssm-ID: 237411 [Multi-domain] Cd Length: 189 Bit Score: 40.91 E-value: 5.18e-04
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| hisH | CHL00188 | imidazole glycerol phosphate synthase subunit hisH; Provisional |
295-411 | 3.37e-03 | ||||||||
imidazole glycerol phosphate synthase subunit hisH; Provisional Pssm-ID: 214389 [Multi-domain] Cd Length: 210 Bit Score: 39.10 E-value: 3.37e-03
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| FGAM_synth_I | TIGR01737 | phosphoribosylformylglycinamidine synthase I; In some species, ... |
261-346 | 4.87e-03 | ||||||||
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: 38.51 E-value: 4.87e-03
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| GATase1_PB | cd01749 | Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ... |
299-374 | 6.25e-03 | ||||||||
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: 37.89 E-value: 6.25e-03
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