glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
2-312
4.77e-174
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]
The actual alignment was detected with superfamily member TIGR02024:
Pssm-ID: 131079 [Multi-domain] Cd Length: 298 Bit Score: 492.35 E-value: 4.77e-174
Formiminotransferase-cyclodeaminase; Members of this family are thought to be ...
323-504
4.28e-58
Formiminotransferase-cyclodeaminase; Members of this family are thought to be Formiminotransferase- cyclodeaminase enzymes EC:4.3.1.4. This domain is found in the C-terminus of the bifunctional animal members of the family.
:
Pssm-ID: 461500 Cd Length: 182 Bit Score: 190.78 E-value: 4.28e-58
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
2-312
4.77e-174
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 131079 [Multi-domain] Cd Length: 298 Bit Score: 492.35 E-value: 4.77e-174
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
1-163
7.08e-101
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.
Pssm-ID: 462283 Cd Length: 176 Bit Score: 301.31 E-value: 7.08e-101
Formiminotransferase-cyclodeaminase; Members of this family are thought to be ...
323-504
4.28e-58
Formiminotransferase-cyclodeaminase; Members of this family are thought to be Formiminotransferase- cyclodeaminase enzymes EC:4.3.1.4. This domain is found in the C-terminus of the bifunctional animal members of the family.
Pssm-ID: 461500 Cd Length: 182 Bit Score: 190.78 E-value: 4.28e-58
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent ...
2-312
4.77e-174
glutamate formiminotransferase; This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines]
Pssm-ID: 131079 [Multi-domain] Cd Length: 298 Bit Score: 492.35 E-value: 4.77e-174
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of ...
1-163
7.08e-101
Formiminotransferase domain, N-terminal subdomain; The formiminotransferase (FT) domain of formiminotransferase- cyclodeaminase (FTCD) forms a homodimer, and each protomer comprises two subdomains. The N-terminal subdomain is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule. The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.
Pssm-ID: 462283 Cd Length: 176 Bit Score: 301.31 E-value: 7.08e-101
Formiminotransferase-cyclodeaminase; Members of this family are thought to be ...
323-504
4.28e-58
Formiminotransferase-cyclodeaminase; Members of this family are thought to be Formiminotransferase- cyclodeaminase enzymes EC:4.3.1.4. This domain is found in the C-terminus of the bifunctional animal members of the family.
Pssm-ID: 461500 Cd Length: 182 Bit Score: 190.78 E-value: 4.28e-58
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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