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Information on EC 5.3.1.27 - 6-phospho-3-hexuloisomerase and Organism(s) Bacillus subtilis and UniProt Accession P42404

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IUBMB Comments
This enzyme, along with EC 4.1.2.43, 3-hexulose-6-phosphate synthase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds . The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of EC 4.1.2.43 (3-hexulose-6-phosphate synthase) and this enzyme .
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Bacillus subtilis
UNIPROT: P42404
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
6-phospho-3-hexuloisomerase, 3-hexulose-6-phosphate isomerase, phospho-3-hexuloisomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hexulose-6-phosphate isomerase
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-
-
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6-phospho-3-hexuloisomerase
phospho-3-hexuloisomerase
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-
-
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[acyl-carrier protein]:acetate ligase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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-
SYSTEMATIC NAME
IUBMB Comments
D-arabino-hex-3-ulose-6-phosphate isomerase
This enzyme, along with EC 4.1.2.43, 3-hexulose-6-phosphate synthase, plays a key role in the ribulose-monophosphate cycle of formaldehyde fixation, which is present in many microorganisms that are capable of utilizing C1-compounds [1]. The hyperthermophilic and anaerobic archaeon Pyrococcus horikoshii OT3 constitutively produces a bifunctional enzyme that sequentially catalyses the reactions of EC 4.1.2.43 (3-hexulose-6-phosphate synthase) and this enzyme [4].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
?
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
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-
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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
D-arabino-hex-3-ulose 6-phosphate
D-fructose 6-phosphate
show the reaction diagram
-
-
-
-
?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
formaldehyde
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concomitant induction of 3-hexulose 6-phosphate synthase and 6-phospho-3-hexuloisomerase by formaldehyde
additional information
-
no induction by by methanol, formate, or methylamine
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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6-phospho-3-hexuloisomerase is a key enzyme catalyzing key exergonic reactions of the formaldehyde-fixing reaction and the isomerization of sugar phosphate in the ribulose monophosphate pathway
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 1.7 A, space group P6522 or P6122
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
gene disruption causes moderate sensitivity to formaldehyde
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Corynebacterium glutamicum
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Taylor, E.J.; Charnock, S.J.; Colby, J.; Davies, G.J.; Black, G.W.
Cloning, purification and characterization of the 6-phospho-3-hexulose isomerase YckF from Bacillus subtilis
Acta Crystallogr. Sect. D
D57
1138-1140
2001
Bacillus subtilis (P42404)
Manually annotated by BRENDA team
Yasueda, H.; Kawahara, Y.; Sugimoto, S.
Bacillus subtilis yckG and yckF encode two key enzymes of the ribulose monophosphate pathway used by methylotrophs, and yckH is required for their expression
J. Bacteriol.
181
7154-7160
1999
Bacillus subtilis
Manually annotated by BRENDA team
Yurimoto, H.; Kato, N.; Sakai, Y.
Genomic organization and biochemistry of the ribulose monophosphate pathway and its application in biotechnology
Appl. Microbiol. Biotechnol.
84
407-416
2009
Bacillus methanolicus, Bacillus subtilis, Brevibacillus brevis, Methanosarcina sp., Methylobacillus flagellatus KT, Methylococcus capsulatus, Methylomonas aminofaciens, Mycobacterium gastri, Pyrococcus horikoshii, Pyrococcus sp., Thermococcus kodakarensis, Thermococcus sp.
Manually annotated by BRENDA team
Witthoff, S.; Schmitz, K.; Niedenfuehr, S.; Noeh, K.; Noack, S.; Bott, M.; Marienhagen, J.
Metabolic engineering of Corynebacterium glutamicum for methanol metabolism
Appl. Environ. Microbiol.
81
2215-2225
2015
Bacillus subtilis (P42404), Bacillus subtilis, Bacillus subtilis 168 (P42404)
Manually annotated by BRENDA team
Lessmeier, L.; Pfeifenschneider, J.; Carnicer, M.; Heux, S.; Portais, J.C.; Wendisch, V.F.
Production of carbon-13-labeled cadaverine by engineered Corynebacterium glutamicum using carbon-13-labeled methanol as co-substrate
Appl. Microbiol. Biotechnol.
99
10163-10176
2015
Bacillus subtilis (P42404), Bacillus subtilis 168 (P42404)
Manually annotated by BRENDA team