phosphotransacetylase family protein containing the BioD-like N-terminal domain of phosphotransacetylase (containing a DRTGG domain), similar to Archaeoglobus fulgidus protein Af1212
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ...
213-317
3.34e-36
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).
Pssm-ID: 429285 [Multi-domain] Cd Length: 105 Bit Score: 126.84 E-value: 3.34e-36
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
2-191
2.11e-19
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: 84.54 E-value: 2.11e-19
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
5-171
1.66e-06
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 129447 [Multi-domain] Cd Length: 166 Bit Score: 47.35 E-value: 1.66e-06
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated ...
213-317
3.34e-36
DRTGG domain; This presumed domain is about 120 amino acids in length. It is found associated with CBS domains pfam00571, as well as the CbiA domain pfam01656. The function of this domain is unknown. It is named the DRTGG domain after some of the most conserved residues. This domain may be very distantly related to a pair of CBS domains. There are no significant sequence similarities, but its length and association with CBS domains supports this idea (Bateman A, pers. obs.).
Pssm-ID: 429285 [Multi-domain] Cd Length: 105 Bit Score: 126.84 E-value: 3.34e-36
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
2-210
5.24e-26
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: 103.11 E-value: 5.24e-26
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
2-191
2.11e-19
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: 84.54 E-value: 2.11e-19
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses ...
5-171
1.66e-06
dethiobiotin synthase; Dethiobiotin synthase is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP). The enzyme binds ATP (see motif in first 12 residues of the SEED alignment) and requires magnesium as a co-factor. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 129447 [Multi-domain] Cd Length: 166 Bit Score: 47.35 E-value: 1.66e-06
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
12-206
2.46e-06
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: 48.11 E-value: 2.46e-06
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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