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Literature summary extracted from

  • Tavares, N.K.; Stracey, N.; Brunold, T.C.; Escalante-Semerena, J.C.
    The L-Thr kinase/l-Thr-phosphate decarboxylase (CobD) enzyme from Methanosarcina mazei Goe1 contains metallocenters needed for optimal activity (2019), Biochemistry, 58, 3260-3279 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.177 C434A site-directed mutagenesis, the MmCobDC434A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control Methanosarcina mazei
2.7.1.177 C458A site-directed mutagenesis, the MmCobDC458A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control. The mutant variant has the lowest Fe to protein ratio Methanosarcina mazei
2.7.1.177 K234A site-directed mutagenesis, the mutat variant lacks the ability to bind PLP effectively, resulting in 19 Fe per monomer, which is reduced compared to wild-type Methanosarcina mazei
4.1.1.81 C434A site-directed mutagenesis, the MmCobDC434A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control Methanosarcina mazei
4.1.1.81 C458A site-directed mutagenesis, the MmCobDC458A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control. The mutant variant has the lowest Fe to protein ratio Methanosarcina mazei
4.1.1.81 K234A site-directed mutagenesis, the mutat variant lacks the ability to bind PLP effectively, resulting in 19 Fe per monomer, which is reduced compared to wild-type Methanosarcina mazei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.177 additional information
-
 additional information Michaelis-Menten kinetics Methanosarcina mazei
4.1.1.81 additional information
-
 additional information Michaelis-Menten kinetics Methanosarcina mazei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.177 Fe2+ the wild-type MmCobD that is normoxically or anoxically purified and then reconstituted, or anoxically purified without reconstitution contains an average of 25 Fe atoms per monomer, with rather poor standard deviations. The C-terminus of MmCobD contains one or more [4Fe-4S] 2+ cluster(s). Although these [4Fe-4S]2+ cluster(s) are not required for activity, perturbations in the C-terminal domain result in the loss of Fe2+ and alterations in the enzyme activities associated with the N-terminus. The C-terminus is not required for the kinase or decarboxylase activities, the [4Fe-4S]2+ cluster-containing C-terminus may have a regulatory role, perhaps by gating the active site or facilitating the decarboxylation and or kinase reactions. Fe2+ is not detected in the N-terminus only (MmCobD1-385) protein sample Methanosarcina mazei
2.7.1.177 Mg2+ required Methanosarcina mazei
2.7.1.177 additional information enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein Methanosarcina mazei
4.1.1.81 Fe2+ the wild-type MmCobD that is normoxically or anoxically purified and then reconstituted, or anoxically purified without reconstitution contains an average of 25 Fe atoms per monomer, with rather poor standard deviations . The C-terminus of MmCobD contains one or more [4Fe-4S] 2+ cluster(s). Although these [4Fe-4S]2+ cluster(s) are not required for activity, perturbations in the C-terminal domain result in the loss of Fe2+ and alterations in the enzyme activities associated with the N-terminus. The C-terminus is not required for the kinase or decarboxylase activities, the [4Fe-4S]2+ cluster-containing C-terminus may have a regulatory role, perhaps by gating the active site or facilitating the decarboxylation and or kinase reactions. Fe2+ is not detected in the N-terminus only (MmCobD1-385) protein sample Methanosarcina mazei
4.1.1.81 additional information enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein Methanosarcina mazei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.177 ATP + L-threonine Methanosarcina mazei
-
 ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine Methanosarcina mazei Goe1
-
 ADP + O-phospho-L-threonine
-
 ?
4.1.1.81 L-threonine O-3-phosphate Methanosarcina mazei
-
 (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?
4.1.1.81 L-threonine O-3-phosphate Methanosarcina mazei Goe1
-
 (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.177 Methanosarcina mazei Q8PVB2
-
-
2.7.1.177 Methanosarcina mazei Goe1 Q8PVB2
-
-
4.1.1.81 Methanosarcina mazei Q8PVB2
-
-
4.1.1.81 Methanosarcina mazei Goe1 Q8PVB2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.177 ATP + L-threonine
-
 Methanosarcina mazei ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine
-
 Methanosarcina mazei Goe1 ADP + O-phospho-L-threonine
-
 ?
4.1.1.81 L-threonine O-3-phosphate
-
 Methanosarcina mazei (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?
4.1.1.81 L-threonine O-3-phosphate
-
 Methanosarcina mazei Goe1 (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.177 L-Thr kinase
-
 Methanosarcina mazei
2.7.1.177 L-Thr kinase/L-Thr-P decarboxylase
-
 Methanosarcina mazei
2.7.1.177 L-Thr kinase/L-Thr-phosphate decarboxylase
-
 Methanosarcina mazei
2.7.1.177 MmCobD
-
 Methanosarcina mazei
2.7.1.177 More also see for L-Thr-phosphate decarboxylase, gene MM2060, EC 4.1.1.81 Methanosarcina mazei
2.7.1.177 PduX
-
 Methanosarcina mazei
4.1.1.81 CobD
-
 Methanosarcina mazei
4.1.1.81 L-Thr kinase/L-Thr-P decarboxylase
-
 Methanosarcina mazei
4.1.1.81 L-Thr kinase/L-Thr-phosphate decarboxylase
-
 Methanosarcina mazei
4.1.1.81 MmCobD
-
 Methanosarcina mazei
4.1.1.81 More also see for L-Thr kinase, EC 2.7.1.177 Methanosarcina mazei

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.177 4Fe-4S-center
-
 Methanosarcina mazei
2.7.1.177 ATP
-
 Methanosarcina mazei
4.1.1.81 4Fe-4S-center
-
 Methanosarcina mazei
4.1.1.81 pyridoxal 5'-phosphate
-
 Methanosarcina mazei

General Information

EC Number General Information Comment Organism
2.7.1.177 evolution 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) Methanosarcina mazei
2.7.1.177 malfunction 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 Methanosarcina mazei
2.7.1.177 additional information MmCobD displays redox-sensitivity Methanosarcina mazei
2.7.1.177 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 cobalamine (Cbl) Methanosarcina mazei
4.1.1.81 evolution 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) Methanosarcina mazei
4.1.1.81 malfunction 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 Methanosarcina mazei
4.1.1.81 additional information MmCobD displays redox-sensitivity Methanosarcina mazei
4.1.1.81 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) Methanosarcina mazei