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Information on EC 4.1.1.81 - threonine-phosphate decarboxylase
for references in articles please use BRENDA:EC4.1.1.81
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EC Tree 4 Lyases
4.1 Carbon-carbon lyases
4.1.1 Carboxy-lyases
4.1.1.81 threonine-phosphate decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein. This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate. The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 4.1.1.81
- enterica
- cobalamin
- pyridoxal
- cobamides
- aminotransferases
- histidinol
-
corrin
- decarboxylases
-
dehalogenase
-
plp-dependent
- typhimurium
- o-phosphate
-
escalante-semerena
-
methanosarcina
-
aldimine
- mazei
-
metal-binding
showSynonyms
mmcobd, smul_1544, l-threonine-o-3-phosphate decarboxylase, mm2060, threonine-phosphate decarboxylase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CobD
L-threonine-O-3-phosphate decarboxylase
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-
-
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MM2060
SMUL_1544
CobD
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO2
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-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
aminopropanol phosphate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
L-threonine-O-3-phosphate carboxy-lyase [(R)-1-aminopropan-2-yl-phosphate-forming]
A pyridoxal-phosphate protein. This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate. The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
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CAS REGISTRY NUMBER
COMMENTARY
205069-45-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-serine O-3-phosphate
ethanolamine-phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
L-serine O-3-phosphate
ethanolamine-phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: biosynthetic pathway of cobalamin, essential cofactor for many living organisms, only synthesized de novo by bacteria and archaea
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: de novo synthesis of enzymatic cofactors, cobalamin biosynthetic pathway
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: enzyme shows stereospecificity for the L-isomer, unable to decarboxylate the D-isomer
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: adenosylcobalamin biosynthesis, end product of the corrin ring biosynthetic pathway is 5'-deoxyadenosylcobinamide phosphate, not 5'-deoxyadenosylcobinamide
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: CobD does not have lactaldehyde aminotransferase activity
Products: -
Products: -
?
additional information
?
-
Substrates: CobD does not have lactaldehyde aminotransferase activity
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-serine O-3-phosphate
ethanolamine-phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
L-serine O-3-phosphate
ethanolamine-phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: biosynthetic pathway of cobalamin, essential cofactor for many living organisms, only synthesized de novo by bacteria and archaea
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
-
Substrates: de novo synthesis of enzymatic cofactors, cobalamin biosynthetic pathway
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
Products: precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: -
Products: -
Products: -
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
Substrates: adenosylcobalamin biosynthesis, end product of the corrin ring biosynthetic pathway is 5'-deoxyadenosylcobinamide phosphate, not 5'-deoxyadenosylcobinamide
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein
additional information
-
enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177)
UniProt
brenda
bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177)
UniProt
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
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
physiological function
additional information
physiological function
-
the product of the SMUL_1544 gene complements a Salmonella enterica CobD mutant lacking an L-threonine-O-3-phosphate decarboxylase
physiological function
CobD is able to complement a Salmonella enterica CobD mutant
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
-
CobD is able to complement a Salmonella enterica CobD mutant
-
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
-
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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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40800
40800
predicted from nucleotide sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals belong to space group I222 with unit cell dimensions a : 66.6 A, b : 103.2 A, and c : 117.1 A, apo-CobD crystals belong to space group I222 with unit cell dimensions a : 76.0 A, b : 103.3 A, and c : 109.3 A
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crystals grown from hanging drops, CobD crystallizes in orthorhombic space group I222, unit cell dimensions a = 67.96 A, b = 101.55 A, and c = 117.23 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
-
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
when purified under anoxic conditions, CobD displayed Michaelis-Menten kinetics and has 1000fold higher affinity for ATP and 1300fold higher catalytic efficiency than CobD purified under oxic conditions
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned, sequenced and overexpressed
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheong, C.G.; Bauer, C.B.; Brushaber, K.R.; Escalante-Semerena, J.C.; Rayment, I.
Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica
Biochemistry
41
4798-4808
2002
no activity in eukaryota, Salmonella enterica
brenda
Brushaber, K.R.; O'Toole, G.A.; Escalante-Semerena, J.C.
CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2
J. Biol. Chem.
273
2684-2691
1998
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium (P97084)
brenda
Cheong, C.G.; Escalante-Semerena, J.C.; Rayment, I.
Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: The apo, substrate, and product-aldimine complexes
Biochemistry
41
9079-9089
2002
Salmonella enterica
brenda
Tavares, N.K.; Zayas, C.L.; Escalante-Semerena, J.C.
The Methanosarcina mazei MM2060 gene encodes a bifunctional kinase/decarboxylase enzyme involved in cobamide biosynthesis
Biochemistry
57
4478-4495
2018
Methanosarcina mazei (Q8PVB1), Methanosarcina mazei, Methanosarcina mazei Goe1 (Q8PVB1)
brenda
Keller, S.; Treder, A.; von Reuss, S.H.; Escalante-Semerena, J.C.; Schubert, T.
The SMUL_1544 gene product governs norcobamide biosynthesis in the tetrachloroethene-respiring bacterium Sulfurospirillum multivorans
J. Bacteriol.
198
2236-2243
2016
Sulfurospirillum multivorans, Sulfurospirillum multivorans DSM 12446
brenda
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
Biochemistry
58
3260-3279
2019
Methanosarcina mazei (Q8PVB2), Methanosarcina mazei, Methanosarcina mazei Goe1 (Q8PVB2)
brenda
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