MULTISPECIES: ATP phosphoribosyltransferase [Rhizobium/Agrobacterium group]
Protein Classification
PBP2_HisGL3 domain-containing protein( domain architecture ID 10194429)
PBP2_HisGL3 domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| PBP2_HisGL3 | cd13593 | The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding ... |
1-229 | 3.77e-83 | ||||
The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. : Pssm-ID: 270311 Cd Length: 220 Bit Score: 246.75 E-value: 3.77e-83
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| Name | Accession | Description | Interval | E-value | ||||
| PBP2_HisGL3 | cd13593 | The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding ... |
1-229 | 3.77e-83 | ||||
The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. Pssm-ID: 270311 Cd Length: 220 Bit Score: 246.75 E-value: 3.77e-83
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| HisG | COG0040 | ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ... |
1-230 | 3.53e-72 | ||||
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP phosphoribosyltransferase is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439810 [Multi-domain] Cd Length: 281 Bit Score: 221.12 E-value: 3.53e-72
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| hisG | TIGR00070 | ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ... |
2-207 | 3.95e-56 | ||||
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and Synechocystis PCC6803 (and related taxa) lack the C-terminal third of the sequence. The sole homolog from Archaeoglobus fulgidus lacks the N-terminal 50 residues (as reported) and is otherwise atypical of the rest of the family. This model excludes the C-terminal extension. [Amino acid biosynthesis, Histidine family] Pssm-ID: 272888 Cd Length: 183 Bit Score: 176.97 E-value: 3.95e-56
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| HisG | pfam01634 | ATP phosphoribosyltransferase; |
53-228 | 1.08e-49 | ||||
ATP phosphoribosyltransferase; Pssm-ID: 460274 Cd Length: 157 Bit Score: 159.45 E-value: 1.08e-49
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| PLN02245 | PLN02245 | ATP phosphoribosyl transferase |
2-228 | 2.45e-36 | ||||
ATP phosphoribosyl transferase Pssm-ID: 215136 [Multi-domain] Cd Length: 403 Bit Score: 131.84 E-value: 2.45e-36
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| Name | Accession | Description | Interval | E-value | ||||
| PBP2_HisGL3 | cd13593 | The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding ... |
1-229 | 3.77e-83 | ||||
The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. Pssm-ID: 270311 Cd Length: 220 Bit Score: 246.75 E-value: 3.77e-83
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| HisG | COG0040 | ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ... |
1-230 | 3.53e-72 | ||||
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP phosphoribosyltransferase is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439810 [Multi-domain] Cd Length: 281 Bit Score: 221.12 E-value: 3.53e-72
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| hisG | TIGR00070 | ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ... |
2-207 | 3.95e-56 | ||||
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and Synechocystis PCC6803 (and related taxa) lack the C-terminal third of the sequence. The sole homolog from Archaeoglobus fulgidus lacks the N-terminal 50 residues (as reported) and is otherwise atypical of the rest of the family. This model excludes the C-terminal extension. [Amino acid biosynthesis, Histidine family] Pssm-ID: 272888 Cd Length: 183 Bit Score: 176.97 E-value: 3.95e-56
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| HisG | pfam01634 | ATP phosphoribosyltransferase; |
53-228 | 1.08e-49 | ||||
ATP phosphoribosyltransferase; Pssm-ID: 460274 Cd Length: 157 Bit Score: 159.45 E-value: 1.08e-49
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| PBP2_ATP-Prtase_HisG | cd13525 | The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic ... |
1-229 | 3.67e-42 | ||||
The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic substrate-binding fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. Pssm-ID: 270243 Cd Length: 208 Bit Score: 141.82 E-value: 3.67e-42
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| PBP2_HisGL4 | cd13594 | The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic binding ... |
1-203 | 1.32e-38 | ||||
The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic binding fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. Pssm-ID: 270312 Cd Length: 207 Bit Score: 132.83 E-value: 1.32e-38
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| PBP2_HisGL2 | cd13592 | The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ... |
4-228 | 1.14e-37 | ||||
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. Pssm-ID: 270310 Cd Length: 208 Bit Score: 130.42 E-value: 1.14e-37
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| PLN02245 | PLN02245 | ATP phosphoribosyl transferase |
2-228 | 2.45e-36 | ||||
ATP phosphoribosyl transferase Pssm-ID: 215136 [Multi-domain] Cd Length: 403 Bit Score: 131.84 E-value: 2.45e-36
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| PBP2_HisGs | cd13595 | The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ... |
1-206 | 6.37e-31 | ||||
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. Pssm-ID: 270313 Cd Length: 205 Bit Score: 113.01 E-value: 6.37e-31
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| PBP2_HisGL1 | cd13591 | The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding ... |
1-226 | 1.25e-27 | ||||
The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding protein fold; Encoded by the hisG gene, the ATP phosphoribosyltransferase (ATP-PRT, EC 2.4.2.17) is the first enzyme in histidine biosynthetic pathway that catalyzes the condensation of ATP and PRPP (5'-phosphoribosyl 1'-pyrophosphate), and is regulated by a feedback inhibition from the product histidine. ATP-PRT has two distinct forms: a hexameric long form, HisGL, containing two catalytic domains and a C-terminal regulatory domain; and a hetero-octomeric short form, HisGs, without the regulatory domain. HisGL is catalytically competent, but the hetero-octameric HisGs requires the second subunit HisZ, a paralog to the catalytic domain of functional histidyl-tRNA synthetases (HisRSs), for the enzyme activity. This catalytic domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. Pssm-ID: 270309 Cd Length: 204 Bit Score: 104.39 E-value: 1.25e-27
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| Blast search parameters | ||||
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