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Information on EC 2.7.6.3 - 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q1ENB6

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IUBMB Comments
Binds 2 Mg2+ ions that are essential for activity . The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants, fungi, and some archaeal species, including the haloarchaea) and methanopterin (in some archaeal species such as the Archaeoglobi and Methanobacteria). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase , the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase , while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities .
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Arabidopsis thaliana
UNIPROT: Q1ENB6
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
Synonyms
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (hppk), 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, cythppk/dhps, fthppk-dhps, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase, hydroxymethyldihydropterin pyrophosphokinase (hppk), hppk/dhps, 6-hydroxymethylpterin pyrophosphokinase, dihydropterin pyrophosphokinase, 7,8-dihydroxymethylpterin-pyrophosphokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
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6-hydroxy-7,8-dihydropterin pyrophosphokinase
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6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK)
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7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase
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7,8-dihydroxymethylpterin-pyrophosphokinase
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ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-pyrophosphotransferase
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H2-pteridine-CH2-OH pyrophosphokinase
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H2-pteridine-CH2OH pyrophosphokinase
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HPPK
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hydroxymethyldihydropteridine pyrophosphokinase
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hydroxymethyldihydropterin pyrophosphokinase (HPPK)
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pyrophosphokinase, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphosphate transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:6-hydroxymethyl-7,8-dihydropterin 6'-diphosphotransferase
Binds 2 Mg2+ ions that are essential for activity [4]. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants, fungi, and some archaeal species, including the haloarchaea) and methanopterin (in some archaeal species such as the Archaeoglobi and Methanobacteria). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase [4], the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase [7], while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities [6].
CAS REGISTRY NUMBER
COMMENTARY hide
37278-23-2
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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
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
show the reaction diagram
6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
show the reaction diagram
tetrahydrofolate biosynthesis
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?
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
ATP + 6-hydroxymethyl-7,8-dihydropterin
AMP + (7,8-dihydropterin-6-yl)methyl diphosphate
show the reaction diagram
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase/7,8-dihydropteroate synthase, i.e. mitHPPK/DHPS, is a bifunctional mitochondrial enzyme, which catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis, folate biosynthesis in Arabidopsis thaliana, overview
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6-hydroxymethyl-7,8-dihydropterin + ATP
6-hydroxymethyl-7,8-dihydropterin diphosphate + AMP
show the reaction diagram
tetrahydrofolate biosynthesis
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
developing, isozyme cytHPPK/DHPS gene is exclusively expressed in developing seeds, histochemical analysis of a transgenic cytHPPK/DHPS promoter-GUS line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isozyme cytHPPK/DHPS lacking a potential transit peptide
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FOLC_ARATH
484
0
54110
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54053
x * 54053, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 54053, sequence calculation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His6-tagged isozyme cytHPPK/DHPS from Escherichia coli strains DH-5alpha and BL-21AI
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme cytHPPK/DHPS DNA and amino acid sequence determination and analysis, and phylogenetic analysis, transient expression of GFP-tagged isozyme cytHPPK/DHPS in the cytosol of Arabidopsis thaliana protoplasts using transfection via Agrobacterium tumefaciens strain GV3101/pMP90, functional complementation of a Saccharomyces cerevisiae mutant, that lacks the enzyme activity, by expression of isozyme cytHPPK/DHPS, expression and subcloning of N-terminally His6-tagged isozyme cytHPPK/DHPS in Escherichia coli strains DH-5alpha and BL-21AI, co-expression with GroESL chaperones
expression in Escherichia coli and Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Storozhenko, S.; Navarrete, O.; Ravanel, S.; De Brouwer, V.; Chaerle, P.; Zhang, G.F.; Bastien, O.; Lambert, W.; Rebeille, F.; Van Der Straeten, D.
Cytosolic hydroxymethyldihydropterin pyrophosphokinase/dihydropteroate synthase from Arabidopsis thaliana: a specific role in early development and stress response
J. Biol. Chem.
282
10749-10761
2007
Arabidopsis thaliana, Arabidopsis thaliana (Q1ENB6)
Manually annotated by BRENDA team