ATP phosphoribosyltransferase, the first enzyme in the histidine biosynthetic pathway, catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP)
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
2-282
8.09e-129
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: 367.11 E-value: 8.09e-129
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
2-282
8.09e-129
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: 367.11 E-value: 8.09e-129
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ...
4-205
5.13e-90
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: 266.01 E-value: 5.13e-90
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
4-185
2.75e-67
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: 207.40 E-value: 2.75e-67
ATP phosphoribosyltransferase [Amino acid transport and metabolism]; ATP ...
2-282
8.09e-129
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: 367.11 E-value: 8.09e-129
The catalytic domain of hexameric long form HisGL2; contains the type 2 periplasmic binding ...
4-205
5.13e-90
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: 266.01 E-value: 5.13e-90
ATP phosphoribosyltransferase; Members of this family from B. subtilis, Aquifex aeolicus, and ...
4-185
2.75e-67
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: 207.40 E-value: 2.75e-67
The catalytic domain of ATP phosphoribosyltransferase contains the type 2 periplasmic ...
4-205
6.61e-57
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: 181.50 E-value: 6.61e-57
The catalytic domain of hexameric long form HisGL4; contains the type 2 periplasmic binding ...
4-205
3.64e-53
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: 172.12 E-value: 3.64e-53
The catalytic domain of hetero-octomeric short form HisGs; contains the type 2 periplasmic ...
4-205
5.60e-51
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: 166.16 E-value: 5.60e-51
The catalytic domain of hexameric long form HisGL3; contains the type 2 periplasmic binding ...
3-209
3.08e-48
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: 159.70 E-value: 3.08e-48
The catalytic domain of hexameric long form HisGL1; contains the type 2 periplasmic binding ...
3-205
4.20e-45
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: 151.39 E-value: 4.20e-45
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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