bifunctional phosphopantothenoylcysteine decarboxylase (CoaC)/phosphopantothenate synthase (CoaB) catalyzes two steps in the biosynthesis of coenzyme A, the conjugation of cysteine to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, followed by its decarboxylation to form 4'-phosphopantotheine
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
14-421
8.73e-171
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
:
Pssm-ID: 273116 [Multi-domain] Cd Length: 391 Bit Score: 483.80 E-value: 8.73e-171
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
14-421
8.73e-171
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 273116 [Multi-domain] Cd Length: 391 Bit Score: 483.80 E-value: 8.73e-171
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
14-422
1.31e-120
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440221 [Multi-domain] Cd Length: 399 Bit Score: 356.26 E-value: 1.31e-120
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
202-394
1.80e-41
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4.1.1.36) affects synthesis of DNA, and pantothenate metabolism.
Pssm-ID: 461186 [Multi-domain] Cd Length: 183 Bit Score: 144.86 E-value: 1.80e-41
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model ...
14-421
8.73e-171
phosphopantothenoylcysteine decarboxylase / phosphopantothenate--cysteine ligase; This model represents a bifunctional enzyme that catalyzes the second and third steps (cysteine ligation, EC 6.3.2.5, and decarboxylation, EC 4.1.1.36) in the biosynthesis of coenzyme A (CoA) from pantothenate in bacteria. In early descriptions of this flavoprotein, a ts mutation in one region of the protein appeared to cause a defect in DNA metaobolism rather than an increased need for the pantothenate precursor beta-alanine. This protein was then called dfp, for DNA/pantothenate metabolism flavoprotein. The authors responsible for detecting phosphopantothenate--cysteine ligase activity suggest renaming this bifunctional protein coaBC for its role in CoA biosynthesis. This enzyme contains the FMN cofactor, but no FAD or pyruvoyl group. The amino-terminal region contains the phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 273116 [Multi-domain] Cd Length: 391 Bit Score: 483.80 E-value: 8.73e-171
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; ...
14-422
1.31e-120
Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC [Coenzyme transport and metabolism]; Phosphopantothenoylcysteine synthetase/decarboxylase CoaBC is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440221 [Multi-domain] Cd Length: 399 Bit Score: 356.26 E-value: 1.31e-120
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4. ...
202-394
1.80e-41
DNA / pantothenate metabolism flavoprotein; The DNA/pantothenate metabolism flavoprotein (EC:4.1.1.36) affects synthesis of DNA, and pantothenate metabolism.
Pssm-ID: 461186 [Multi-domain] Cd Length: 183 Bit Score: 144.86 E-value: 1.80e-41
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single ...
17-189
4.86e-41
phosphopantothenoylcysteine decarboxylase, streptococcal; In most bacteria, a single bifunctional protein catalyses phosphopantothenoylcysteine decarboxylase and phosphopantothenate--cysteine ligase activities, sequential steps in coenzyme A biosynthesis (see TIGR00521). These activities reside in separate proteins encoded by tandem genes in some bacterial lineages. This model describes proteins from the genera Streptococcus and Enterococcus homologous to the N-terminal region of TIGR00521, corresponding to phosphopantothenoylcysteine decarboxylase activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pantothenate and coenzyme A]
Pssm-ID: 131168 Cd Length: 177 Bit Score: 143.80 E-value: 4.86e-41
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
17-196
1.72e-33
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyzes the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond. This family also includes the B chain of dipicolinate synthase a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance. dipicolinate synthase catalyzes the formation of dipicolinic acid from dihydroxydipicolinic acid. This family also includes phenyl-acrylic acid decarboxylase (EC:4.1.1.-).
Pssm-ID: 426775 [Multi-domain] Cd Length: 177 Bit Score: 123.64 E-value: 1.72e-33
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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Functional characterization of the conserved domain architecture found on the query.
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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