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Information on EC 5.3.1.27 - 6-phospho-3-hexuloisomerase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58644

for references in articles please use BRENDA:EC5.3.1.27
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EC Tree
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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Methanocaldococcus jannaschii
UNIPROT: Q58644
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Word Map
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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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6-phospho-3-hexuloisomerase
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phospho-3-hexuloisomerase
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[acyl-carrier protein]:acetate ligase
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
diffraction to 2.0 A resolution. MJ1247 is an alpha/beta structure consisting of a five-stranded parallel beta-sheet flanked on both sides by alpha-helices, forming a three-layered alpha-beta-alpha sandwich. The fold represents the nucleotide binding motif of a flavodoxin type. Protein forms a tetramer in the crystal an in solution and each monomer has a folding similar to the isomerase domain of glucosamine 6-phosphate synthase
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martinez-Cruz, L.A.; Dreyer, M.K.; Boisvert, D.C.; Yokota, H.; Martinez-Chantar, M.L.; Kim, R.; Kim, S.
Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase
Structure
10
195-204
2002
Methanocaldococcus jannaschii (Q58644), Methanocaldococcus jannaschii
Manually annotated by BRENDA team