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Information on EC 2.1.2.1 - glycine hydroxymethyltransferase and Organism(s) Thermus thermophilus and UniProt Accession Q5SI56

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EC Tree
IUBMB Comments
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
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This record set is specific for:
Thermus thermophilus
UNIPROT: Q5SI56
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Word Map
The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
serine hydroxymethyltransferase, shmt2, shmt1, serine hydroxymethyl transferase, serine transhydroxymethylase, serine hydroxymethyltransferase 2, mitochondrial serine hydroxymethyltransferase, serine hydroxymethyltransferase 1, bsshmt, pvshmt, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
serine hydroxymethyltransferase
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L-serine hydroxymethyltransferase
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serine hydroxymethylase hydroxymethyltransferase, serine
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serine hydroxymethyltransferase
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-
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serine transhydroxymethylase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxymethyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
5,10-methylenetetrahydrofolate:glycine hydroxymethyltransferase
A pyridoxal-phosphate protein. Also catalyses the reaction of glycine with acetaldehyde to form L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy-N6,N6,N6-trimethyl-L-lysine.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-83-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
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-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5,10-methylenetetrahydrofolate + glycine + H2O
tetrahydrofolate + L-serine
show the reaction diagram
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-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,10-methylenetetrahydrofolate
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pyridoxal 5'-phosphate
dependent on
tetrahydrofolate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene glyA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process
physiological function
SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism. SHMT also catalyzes the H4PteGlu-independent cleavage of many 3-hydroxyamino acids and the decarboxylation of aminomalonate, at rates similar to that of H4PteGlu-dependent serine cleavage
additional information
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, PDB 2DKJ, molecular dynamics, overview
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
analysis of buried water clusters in the inner region of the SHMT dimers using the enzyme crystal structure, molecular dynamics, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme represents a potential target for chemotherapeutics
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Milano, T.; Di Salvo, M.L.; Angelaccio, S.; Pascarella, S.
Conserved water molecules in bacterial serine hydroxymethyltransferases
Protein Eng. Des. Sel.
28
415-426
2015
Burkholderia pseudomallei (A0A069BAT4), Psychromonas ingrahamii (A1SUU0), Rickettsia rickettsii (A8GTI9), Burkholderia cenocepacia (B4ECY9), Salmonella enterica subsp. enterica serovar Typhimurium (P0A2E1), Escherichia coli (P0A825), Mycobacterium tuberculosis (P9WGI9), Staphylococcus aureus (Q5HE87), Thermus thermophilus (Q5SI56), Geobacillus stearothermophilus (Q7SIB6), Campylobacter jejuni (Q9S6K1), Campylobacter jejuni ATCC 33560 (Q9S6K1), Psychromonas ingrahamii 37 (A1SUU0), Mycobacterium tuberculosis H37Rv (P9WGI9), Staphylococcus aureus COL (Q5HE87), Burkholderia pseudomallei ATCC 23343 (A0A069BAT4), Rickettsia rickettsii Sheila Smith (A8GTI9)
Manually annotated by BRENDA team