bifunctional anthranilate synthase/indole-3-glycerol-phosphate synthase [Saccharomyces cerevisiae PE-2]
Protein Classification
anthranilate synthase component II( domain architecture ID 11423518)
anthranilate synthase component II is part of a complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| IGPS | pfam00218 | Indole-3-glycerol phosphate synthase; |
217-481 | 1.09e-137 | |||||
Indole-3-glycerol phosphate synthase; : Pssm-ID: 395163 Cd Length: 252 Bit Score: 396.67 E-value: 1.09e-137
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| PabA | COG0512 | Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
14-203 | 8.78e-111 | |||||
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: 325.45 E-value: 8.78e-111
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| Name | Accession | Description | Interval | E-value | |||||
| IGPS | pfam00218 | Indole-3-glycerol phosphate synthase; |
217-481 | 1.09e-137 | |||||
Indole-3-glycerol phosphate synthase; Pssm-ID: 395163 Cd Length: 252 Bit Score: 396.67 E-value: 1.09e-137
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| IGPS | cd00331 | Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
257-482 | 1.43e-114 | |||||
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis. Pssm-ID: 238203 Cd Length: 217 Bit Score: 336.36 E-value: 1.43e-114
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| TrpC | COG0134 | Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
214-482 | 5.71e-112 | |||||
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 439904 Cd Length: 257 Bit Score: 331.22 E-value: 5.71e-112
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| PabA | COG0512 | Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
14-203 | 8.78e-111 | |||||
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: 325.45 E-value: 8.78e-111
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| trpC | PRK00278 | indole-3-glycerol phosphate synthase TrpC; |
215-482 | 2.18e-108 | |||||
indole-3-glycerol phosphate synthase TrpC; Pssm-ID: 234710 Cd Length: 260 Bit Score: 322.11 E-value: 2.18e-108
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| PRK05670 | PRK05670 | anthranilate synthase component II; Provisional |
13-199 | 5.73e-104 | |||||
anthranilate synthase component II; Provisional Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 308.21 E-value: 5.73e-104
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| GATase1_Anthranilate_Synthase | cd01743 | Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
14-198 | 1.52e-101 | |||||
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: 301.76 E-value: 1.52e-101
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| trpG_papA | TIGR00566 | glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
13-199 | 8.22e-75 | |||||
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase. Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 233.53 E-value: 8.22e-75
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| GATase | pfam00117 | Glutamine amidotransferase class-I; |
15-198 | 3.66e-69 | |||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 219.03 E-value: 3.66e-69
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| Anth_synII_Halo | NF041322 | anthranilate synthase component II; |
17-198 | 1.66e-66 | |||||
anthranilate synthase component II; Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 212.20 E-value: 1.66e-66
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| Name | Accession | Description | Interval | E-value | |||||
| IGPS | pfam00218 | Indole-3-glycerol phosphate synthase; |
217-481 | 1.09e-137 | |||||
Indole-3-glycerol phosphate synthase; Pssm-ID: 395163 Cd Length: 252 Bit Score: 396.67 E-value: 1.09e-137
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| IGPS | cd00331 | Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ... |
257-482 | 1.43e-114 | |||||
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis. Pssm-ID: 238203 Cd Length: 217 Bit Score: 336.36 E-value: 1.43e-114
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| TrpC | COG0134 | Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol ... |
214-482 | 5.71e-112 | |||||
Indole-3-glycerol phosphate synthase [Amino acid transport and metabolism]; Indole-3-glycerol phosphate synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis Pssm-ID: 439904 Cd Length: 257 Bit Score: 331.22 E-value: 5.71e-112
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| PabA | COG0512 | Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
14-203 | 8.78e-111 | |||||
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: 325.45 E-value: 8.78e-111
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| trpC | PRK00278 | indole-3-glycerol phosphate synthase TrpC; |
215-482 | 2.18e-108 | |||||
indole-3-glycerol phosphate synthase TrpC; Pssm-ID: 234710 Cd Length: 260 Bit Score: 322.11 E-value: 2.18e-108
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| PRK05670 | PRK05670 | anthranilate synthase component II; Provisional |
13-199 | 5.73e-104 | |||||
anthranilate synthase component II; Provisional Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 308.21 E-value: 5.73e-104
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| GATase1_Anthranilate_Synthase | cd01743 | Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
14-198 | 1.52e-101 | |||||
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: 301.76 E-value: 1.52e-101
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| PRK14607 | PRK14607 | bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
14-199 | 5.30e-83 | |||||
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 266.20 E-value: 5.30e-83
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| PRK08007 | PRK08007 | aminodeoxychorismate synthase component 2; |
14-199 | 1.25e-78 | |||||
aminodeoxychorismate synthase component 2; Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 243.29 E-value: 1.25e-78
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| trpG_papA | TIGR00566 | glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
13-199 | 8.22e-75 | |||||
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase. Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 233.53 E-value: 8.22e-75
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| PRK07649 | PRK07649 | aminodeoxychorismate/anthranilate synthase component II; |
14-199 | 1.81e-73 | |||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 230.46 E-value: 1.81e-73
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| PRK08857 | PRK08857 | aminodeoxychorismate/anthranilate synthase component II; |
14-199 | 8.23e-72 | |||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 225.91 E-value: 8.23e-72
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| GATase | pfam00117 | Glutamine amidotransferase class-I; |
15-198 | 3.66e-69 | |||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 219.03 E-value: 3.66e-69
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| PLN02335 | PLN02335 | anthranilate synthase |
2-200 | 4.16e-69 | |||||
anthranilate synthase Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 220.05 E-value: 4.16e-69
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| PRK07765 | PRK07765 | aminodeoxychorismate/anthranilate synthase component II; |
14-202 | 8.21e-69 | |||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 218.77 E-value: 8.21e-69
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| trpG | CHL00101 | anthranilate synthase component 2 |
14-201 | 1.87e-68 | |||||
anthranilate synthase component 2 Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 217.29 E-value: 1.87e-68
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| PRK06774 | PRK06774 | aminodeoxychorismate synthase component II; |
14-198 | 9.50e-67 | |||||
aminodeoxychorismate synthase component II; Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 212.80 E-value: 9.50e-67
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| Anth_synII_Halo | NF041322 | anthranilate synthase component II; |
17-198 | 1.66e-66 | |||||
anthranilate synthase component II; Pssm-ID: 469219 [Multi-domain] Cd Length: 190 Bit Score: 212.20 E-value: 1.66e-66
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| PRK09427 | PRK09427 | bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ... |
211-482 | 2.63e-64 | |||||
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF; Pssm-ID: 236509 [Multi-domain] Cd Length: 454 Bit Score: 215.06 E-value: 2.63e-64
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| PRK09522 | PRK09522 | bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate ... |
14-234 | 9.54e-51 | |||||
bifunctional anthranilate synthase glutamate amidotransferase component TrpG/anthranilate phosphoribosyltransferase TrpD; Pssm-ID: 181927 [Multi-domain] Cd Length: 531 Bit Score: 180.61 E-value: 9.54e-51
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| PRK13566 | PRK13566 | anthranilate synthase component I; |
2-198 | 3.24e-50 | |||||
anthranilate synthase component I; Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 182.42 E-value: 3.24e-50
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| PRK13802 | PRK13802 | bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
270-482 | 2.36e-46 | |||||
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 171.37 E-value: 2.36e-46
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| PRK13957 | PRK13957 | indole-3-glycerol-phosphate synthase; Provisional |
270-482 | 3.71e-45 | |||||
indole-3-glycerol-phosphate synthase; Provisional Pssm-ID: 140013 Cd Length: 247 Bit Score: 158.12 E-value: 3.71e-45
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| PLN02460 | PLN02460 | indole-3-glycerol-phosphate synthase |
251-482 | 1.58e-44 | |||||
indole-3-glycerol-phosphate synthase Pssm-ID: 215254 Cd Length: 338 Bit Score: 159.17 E-value: 1.58e-44
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| PRK05637 | PRK05637 | anthranilate synthase component II; Provisional |
11-194 | 7.66e-37 | |||||
anthranilate synthase component II; Provisional Pssm-ID: 180178 [Multi-domain] Cd Length: 208 Bit Score: 134.59 E-value: 7.66e-37
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| PRK06895 | PRK06895 | anthranilate synthase component II; |
11-201 | 1.94e-31 | |||||
anthranilate synthase component II; Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 119.46 E-value: 1.94e-31
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| PabB-fungal | TIGR01823 | aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a ... |
9-215 | 9.41e-31 | |||||
aminodeoxychorismate synthase, fungal clade; This model represents the fungal clade of a para-aminobenzoate synthesis enzyme, aminodeoxychorismate synthase, which acts on chorismate in a pathway that yields PABA, a precursor of folate. Pssm-ID: 273821 [Multi-domain] Cd Length: 742 Bit Score: 126.17 E-value: 9.41e-31
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| PLN02889 | PLN02889 | oxo-acid-lyase/anthranilate synthase |
15-238 | 1.88e-30 | |||||
oxo-acid-lyase/anthranilate synthase Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 125.35 E-value: 1.88e-30
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| GATase1_GMP_Synthase | cd01742 | Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
46-198 | 2.30e-26 | |||||
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 105.31 E-value: 2.30e-26
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| guaA_Nterm | TIGR00888 | GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
47-196 | 1.16e-22 | |||||
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis] Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 95.07 E-value: 1.16e-22
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| guaA | PRK00074 | GMP synthase; Reviewed |
46-220 | 4.62e-22 | |||||
GMP synthase; Reviewed Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 98.97 E-value: 4.62e-22
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| GATase1_CPSase | cd01744 | Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
25-184 | 3.76e-19 | |||||
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: 84.86 E-value: 3.76e-19
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| PRK00758 | PRK00758 | GMP synthase subunit A; Validated |
13-203 | 7.21e-19 | |||||
GMP synthase subunit A; Validated Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 84.13 E-value: 7.21e-19
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| GuaA1 | COG0518 | GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
15-183 | 2.04e-16 | |||||
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: 78.06 E-value: 2.04e-16
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| PRK12564 | PRK12564 | carbamoyl-phosphate synthase small subunit; |
12-184 | 4.71e-16 | |||||
carbamoyl-phosphate synthase small subunit; Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 79.35 E-value: 4.71e-16
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| CPSaseIIsmall | TIGR01368 | carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
11-184 | 6.14e-16 | |||||
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis] Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 79.21 E-value: 6.14e-16
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| PLN02347 | PLN02347 | GMP synthetase |
51-202 | 5.03e-14 | |||||
GMP synthetase Pssm-ID: 215197 [Multi-domain] Cd Length: 536 Bit Score: 74.34 E-value: 5.03e-14
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| PRK12838 | PRK12838 | carbamoyl phosphate synthase small subunit; Reviewed |
10-183 | 7.71e-12 | |||||
carbamoyl phosphate synthase small subunit; Reviewed Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 66.45 E-value: 7.71e-12
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| CarA | COG0505 | Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
12-184 | 8.77e-12 | |||||
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 66.58 E-value: 8.77e-12
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| PLN02771 | PLN02771 | carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
26-184 | 9.98e-12 | |||||
carbamoyl-phosphate synthase (glutamine-hydrolyzing) Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 66.54 E-value: 9.98e-12
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| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
14-99 | 4.43e-11 | |||||
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: 59.92 E-value: 4.43e-11
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| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
14-98 | 7.38e-11 | |||||
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: 58.75 E-value: 7.38e-11
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| carA | CHL00197 | carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
25-184 | 7.39e-09 | |||||
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 57.50 E-value: 7.39e-09
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| GATase1_2 | cd01745 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
85-183 | 1.90e-08 | |||||
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: 54.12 E-value: 1.90e-08
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| PuuD | COG2071 | Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
85-183 | 3.07e-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: 51.32 E-value: 3.07e-07
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| TIM_phosphate_binding | cd04722 | TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
282-466 | 6.56e-07 | |||||
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN. Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 49.89 E-value: 6.56e-07
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| Peptidase_C26 | pfam07722 | Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
85-183 | 2.38e-06 | |||||
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: 48.41 E-value: 2.38e-06
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| PRK09065 | PRK09065 | glutamine amidotransferase; Provisional |
87-183 | 1.23e-05 | |||||
glutamine amidotransferase; Provisional Pssm-ID: 181635 [Multi-domain] Cd Length: 237 Bit Score: 46.49 E-value: 1.23e-05
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| IMP_synth_hisH | TIGR01855 | imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ... |
58-183 | 4.37e-04 | |||||
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: 41.54 E-value: 4.37e-04
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| hisH | PRK13141 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
83-183 | 1.83e-03 | |||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 39.73 E-value: 1.83e-03
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| PRK04302 | PRK04302 | triosephosphate isomerase; Provisional |
427-482 | 2.67e-03 | |||||
triosephosphate isomerase; Provisional Pssm-ID: 235274 Cd Length: 223 Bit Score: 39.47 E-value: 2.67e-03
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| QPRTase_NadC | cd01568 | Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
391-472 | 2.75e-03 | |||||
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other. Pssm-ID: 238802 [Multi-domain] Cd Length: 269 Bit Score: 39.38 E-value: 2.75e-03
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| QPRTase | cd01572 | Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called ... |
391-460 | 3.45e-03 | |||||
Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other. Pssm-ID: 238806 [Multi-domain] Cd Length: 268 Bit Score: 39.38 E-value: 3.45e-03
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| HisH | COG0118 | Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
80-183 | 3.88e-03 | |||||
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: 38.48 E-value: 3.88e-03
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| QRPTase_C | pfam01729 | Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl ... |
382-466 | 5.28e-03 | |||||
Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase (QPRTase) or nicotinate-nucleotide pyrophosphorylase EC:2.4.2.19 is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyzes the reaction of quinolinic acid with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to give rise to nicotinic acid mononucleotide (NaMN), pyrophosphate and carbon dioxide. The QA substrate is bound between the C-terminal domain of one subunit, and the N-terminal domain of the other. The C-terminal domain has a 7 beta-stranded TIM barrel-like fold. Pssm-ID: 396337 Cd Length: 169 Bit Score: 37.68 E-value: 5.28e-03
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| TalA | COG0176 | Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
291-377 | 5.48e-03 | |||||
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway Pssm-ID: 439946 [Multi-domain] Cd Length: 214 Bit Score: 38.13 E-value: 5.48e-03
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| HisA_HisF | cd04723 | Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ... |
422-469 | 8.63e-03 | |||||
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria. Pssm-ID: 240074 [Multi-domain] Cd Length: 233 Bit Score: 37.63 E-value: 8.63e-03
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