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Information on EC 4.1.99.12 - 3,4-dihydroxy-2-butanone-4-phosphate synthase and Organism(s) Arabidopsis thaliana and UniProt Accession P47924
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4.1.99.12 3,4-dihydroxy-2-butanone-4-phosphate synthaseIUBMB Comments
Requires a divalent cation, preferably Mg2+, for activity . The reaction involves an intramolecular skeletal rearrangement, with the bonds in D-ribulose 5-phosphate that connect C-3 and C-5 to C-4 being broken, C-4 being removed as formate and reconnection of C-3 and C-5 . The phosphorylated four-carbon product (L-3,4-dihydroxybutan-2-one 4-phosphate) is an intermediate in the biosynthesis of riboflavin .
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- 4.1.99.12
-
disinfection
-
trihalomethanes
-
haloacetic
-
brominate
-
halogen
-
haloacetonitriles
-
chloramination
- bromide
-
genotoxicity
- chloroform
-
effluent
-
wastewater
-
iodin
- ozone
-
swimming
-
humic
-
unregulated
-
trichloronitromethane
- n-nitrosodimethylamine
-
carbonaceous
- chloral
-
speciation
-
dichloroacetic
-
dichloroacetonitrile
- monochloramine
- haloketones
-
bromodichloromethane
-
swimmers
-
fulvic
-
hypochlorite
-
non-regulated
-
micropollutants
- clo2
-
pilot-scale
-
n-nitrosamines
- naclo
-
excitation-emission
-
bromoacetic
- chlorite
-
ballast
-
shower
-
acid-like
- pipe
-
potable
-
suwannee
- drug development
- synthesis
-
nanofiltration
-
biofiltration
- bromoform
-
indoor
- iodate
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dbps, dhbps, 3,4-dihydroxy-2-butanone-4-phosphate synthase, mtb-riba2, atriba1, mtb-dhbps, dhbp synthase, atriba2, vdhbps, dihydroxybutanone phosphate synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
D-ribulose 5-phosphate formate-lyase (L-3,4-dihydroxybutan-2-one 4-phosphate-forming)
Requires a divalent cation, preferably Mg2+, for activity [1]. The reaction involves an intramolecular skeletal rearrangement, with the bonds in D-ribulose 5-phosphate that connect C-3 and C-5 to C-4 being broken, C-4 being removed as formate and reconnection of C-3 and C-5 [1]. The phosphorylated four-carbon product (L-3,4-dihydroxybutan-2-one 4-phosphate) is an intermediate in the biosynthesis of riboflavin [1].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
isozyme AtRIBA1
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
isozyme AtRIBA2
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
D-ribulose 5-phosphate
formate + L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
angiosperms share a small RIBA gene family consisting of three members. The monofunctional, bipartite RIBA3 proteins AtRIBA2, and AtRIBA3, which have lost DHBPS activity, evolved early in tracheophyte evolution, phylogenetic analysis, overview. While AtRIBA2 is lacking GCHII activity, AtRIBA3 does not display DHBPS function
malfunction
bleaching leaf phenotype of RIBA1 deficient plants, overview. The bleaching phenotype of the seedlings is not counterbalanced by the simultaneous AtRIBA2 and AtRIBA3 expression
metabolism
the enzyme is involved in biosynthesis of riboflavin, overview. Riboflavin is the precursor for the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are essential cofactors for numerous enzymes (e.g., dehydrogenases, oxidases, reductases)
physiological function
isozyme AtRIBA1 is required for pigmentation of the rosettes leaves
evolution
angiosperms share a small RIBA gene family consisting of three members. The monofunctional, bipartite RIBA3 proteins AtRIBA2, and AtRIBA3, which have lost DHBPS activity, evolved early in tracheophyte evolution, phylogenetic analysis, overview. While AtRIBA2 is lacking GCHII activity, AtRIBA3 does not display DHBPS function
malfunction
bleaching leaf phenotype of RIBA1 deficient plants, overview. The bleaching phenotype of the seedlings is not counterbalanced by the simultaneous AtRIBA2 and AtRIBA3 expression
metabolism
the enzyme is involved in biosynthesis of riboflavin, overview. Riboflavin is the precursor for the synthesis of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are essential cofactors for numerous enzymes (e.g., dehydrogenases, oxidases, reductases)
physiological function
isozyme AtRIBA1 is required for pigmentation of the rosettes leaves
additional information
additional information
in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS
additional information
in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS
additional information
in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS
additional information
in plants bifunctional RIBA enzymes comprise of N-terminal GTP cyclohydrolase II, GCHII, and C-terminal 3,4-dihydroxy-2-butanone-4-phosphate synthase, DHBPS
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RIBA1_ARATH
543
0
59056
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
47600
x * 47600, recombinant His-tagged N-terminally truncated AtRIBA1
42300
x * 42300, recombinant His-tagged N-terminally truncated AtRIBA2
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 47600, recombinant His-tagged N-terminally truncated AtRIBA1
?
x * 42300, recombinant His-tagged N-terminally truncated AtRIBA2
additional information
additional information
both isozymes AtRIBA2 and AtRIBA3 have amino acid exchanges in conserved peptides domains that are essential for the two enzymatic functions
additional information
both isozymes AtRIBA2 and AtRIBA3 have amino acid exchanges in conserved peptides domains that are essential for the two enzymatic functions
additional information
both isozymes AtRIBA2 and AtRIBA3 have amino acid exchanges in conserved peptides domains that are essential for the two enzymatic functions
additional information
both isozymes AtRIBA2 and AtRIBA3 have amino acid exchanges in conserved peptides domains that are essential for the two enzymatic functions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged N-terminally truncated AtRIBA1 protein from Escherichia coli by nickel affinity chromatography
recombinant His-tagged N-terminally truncated AtRIBA2 protein from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene At5g64300, phylogenetic analysis , recombinant expression of His-tagged N-terminally truncated AtRIBA1 protein in Escherichia coli, recombinant expression of GFP-tagged isozymes AtRIBA1, AtRIBA2, and AtRIBA3 in transgenic Nicotiana benthaminana chloroplasts using Agrobacterium tumefaciens pGV2260 transfection, isozymes AtRIBA2 and AtRIBA3 fail to sufficiently compensate for a lack of RIBA1 expression
gene At2g22450, phylogenetic analysis, recombinant expression of His-tagged N-terminally truncated AtRIBA2 protein in Escherichia coli, recombinant expression fo GFP-tagged isozymes AtRIBA1, AtRIBA2, and AtRIBA3 in transgenic Nicotiana benthaminana chloroplasts using Agrobacterium tumefaciens pGV2260 transfection, isozymes AtRIBA2 and AtRIBA3 fail to sufficiently compensate for a lack of RIBA1 expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hiltunen, H.M.; Illarionov, B.; Hedtke, B.; Fischer, M.; Grimm, B.
Arabidopsis RIBA proteins: two out of three isoforms have lost their bifunctional activity in riboflavin biosynthesis
Int. J. Mol. Sci.
13
14086-14105
2012
Arabidopsis thaliana (P47924), Arabidopsis thaliana (Q6NLQ7), Arabidopsis thaliana Col-0 (P47924), Arabidopsis thaliana Col-0 (Q6NLQ7)
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