4.1.1.81: threonine-phosphate decarboxylase
This is an abbreviated version!
For detailed information about threonine-phosphate decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.81
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4.1.1.81
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enterica
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cobalamin
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pyridoxal
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cobamides
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aminotransferases
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histidinol
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corrin
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decarboxylases
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dehalogenase
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plp-dependent
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typhimurium
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o-phosphate
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escalante-semerena
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methanosarcina
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aldimine
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mazei
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metal-binding
- 4.1.1.81
- enterica
- cobalamin
- pyridoxal
- cobamides
- aminotransferases
- histidinol
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corrin
- decarboxylases
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dehalogenase
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plp-dependent
- typhimurium
- o-phosphate
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escalante-semerena
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methanosarcina
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aldimine
- mazei
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metal-binding
Reaction
Synonyms
CobD, CobD gene product, L-Thr kinase/L-Thr-P decarboxylase, L-Thr kinase/L-Thr-phosphate decarboxylase, L-threonine-O-3-phosphate decarboxylase, MM2060, MmCobD, More, SMUL_1544
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General Information
General Information on EC 4.1.1.81 - threonine-phosphate decarboxylase
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evolution
malfunction
physiological function
additional information
the CobD protein from Methanosarcina mazei differs from other CobD homologues by the presence of a 111-amino acid cysteine-rich extended C-terminus (MmCobD386-497) annotated as a putative metal-binding domain or zinc finger protein, but it actually is a ferroprotein. This C-terminal domain is sometimes encoded as an independent protein and other times fused to other Cba biosynthetic proteins (e.g. CbiZ, CbiA, CbiH, or BtuC)
evolution
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the CobD protein from Methanosarcina mazei differs from other CobD homologues by the presence of a 111-amino acid cysteine-rich extended C-terminus (MmCobD386-497) annotated as a putative metal-binding domain or zinc finger protein, but it actually is a ferroprotein. This C-terminal domain is sometimes encoded as an independent protein and other times fused to other Cba biosynthetic proteins (e.g. CbiZ, CbiA, CbiH, or BtuC)
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there is a 2600fold decrease in catalytic efficiency (kcat/Km) when the C-terminus is removed, or a 1200fold decrease when the enzyme is purified normoxically
malfunction
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there is a 2600fold decrease in catalytic efficiency (kcat/Km) when the C-terminus is removed, or a 1200fold decrease when the enzyme is purified normoxically
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CobD is able to complement a Salmonella enterica CobD mutant
physiological function
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the product of the SMUL_1544 gene complements a Salmonella enterica CobD mutant lacking an L-threonine-O-3-phosphate decarboxylase
physiological function
MmCobD is a bifunctional enzyme with L-threonine (L-Thr) kinase (PduX, EC 2.7.1.177) and pyridoxal 5'-phosphate (PLP)-dependent L-threonine phosphate (L-Thr-P) decarboxylase activities needed to synthesize the (R)-1-amino-propan-2-ol O-phosphate (a.k.a. (R)-1-amino-2-propanol-O-2-phosphate, AP-P) moiety of cobalamin (Cbl)
physiological function
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CobD is able to complement a Salmonella enterica CobD mutant
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physiological function
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MmCobD is a bifunctional enzyme with L-threonine (L-Thr) kinase (PduX, EC 2.7.1.177) and pyridoxal 5'-phosphate (PLP)-dependent L-threonine phosphate (L-Thr-P) decarboxylase activities needed to synthesize the (R)-1-amino-propan-2-ol O-phosphate (a.k.a. (R)-1-amino-2-propanol-O-2-phosphate, AP-P) moiety of cobalamin (Cbl)
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physiological function
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the product of the SMUL_1544 gene complements a Salmonella enterica CobD mutant lacking an L-threonine-O-3-phosphate decarboxylase
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