Information on EC 4.1.1.81 - threonine-phosphate decarboxylase

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The expected taxonomic range for this enzyme is: Salmonella enterica

EC NUMBER
COMMENTARY
4.1.1.81
-
RECOMMENDED NAME
GeneOntology No.
threonine-phosphate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-threonine O-3-phosphate = (R)-1-aminopropan-2-yl phosphate + CO2
show the reaction diagram
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-
-
-
PATHWAY
KEGG Link
MetaCyc Link
aminopropanol phosphate biosynthesis I
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Porphyrin and chlorophyll metabolism
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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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CobD
-
-
-
-
CobD gene product
-
-
L-threonine-O-3-phosphate decarboxylase
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
205069-45-0
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
no activity in eukaryota
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-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
show the reaction diagram
P97084, -
-
-
-
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
show the reaction diagram
-
-
-
-
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
-
-
-
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
-
-
-
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
P97084, -
enzyme shows stereospecificity for the L-isomer, unable to decarboxylate the D-isomer
-
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
P97084, -
adenosylcobalamin biosynthesis, end product of the corrin ring biosynthetic pathway is 5'-deoxyadenosylcobinamide phosphate, not 5'-deoxyadenosylcobinamide
-
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
-
biosynthetic pathway of cobalamin, essential cofactor for many living organisms, only synthesized de novo by bacteria and archaea
precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
-
de novo synthesis of enzymatic cofactors, cobalamin biosynthetic pathway
precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
additional information
?
-
P97084, -
CobD does not have lactaldehyde aminotransferase activity
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
show the reaction diagram
P97084, -
-
-
-
?
L-threonine O-3-phosphate
(R)-1-aminopropan-2-yl phosphate + CO2
show the reaction diagram
-
-
-
-
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
P97084, -
adenosylcobalamin biosynthesis, end product of the corrin ring biosynthetic pathway is 5'-deoxyadenosylcobinamide phosphate, not 5'-deoxyadenosylcobinamide
-
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
-
biosynthetic pathway of cobalamin, essential cofactor for many living organisms, only synthesized de novo by bacteria and archaea
precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
L-threonine O-3-phosphate
2-amino-1-methylethyl phosphate + CO2
show the reaction diagram
-
de novo synthesis of enzymatic cofactors, cobalamin biosynthetic pathway
precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin
?
PDB
SCOP
CATH
ORGANISM
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40800
-
P97084, -
predicted from nucleotide sequence
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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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Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overproduced in Escherichia coli
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cloned, sequenced and overexpressed
P97084, -