Enzyme

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     5. Isomerases
        5.3 Intramolecular oxidoreductases
            5.3.1 Interconverting aldoses and ketoses, and related compounds
ID:5.3.1.29
Description:Ribose 1,5-bisphosphate isomerase.
Alternative Name: RuBP synthase.
Ribulose 1,5-bisphosphate synthase.
Cath: 1.20.120.420; 3.40.50.10470;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.3.1.29
BRENDA Enzyme Link: BRENDA 5.3.1.29
KEGG Enzyme Link: KEGG5.3.1.29
BioCyc Enzyme Link: BioCyc 5.3.1.29
ExPASy Enzyme Link: ExPASy5.3.1.29
EC2PDB Enzyme Link: EC2PDB 5.3.1.29
ExplorEnz Enzyme Link: ExplorEnz 5.3.1.29
PRIAM enzyme-specific profiles Link: PRIAM 5.3.1.29
IntEnz Enzyme Link: IntEnz 5.3.1.29
MEDLINE Enzyme Link: MEDLINE 5.3.1.29
MSA:

5.3.1.29;

Phylogenetic Tree:

5.3.1.29;

Uniprot:
M-CSA:
RHEA:32243 alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate
RULE(radius=1) [*:1]-[CH;+0:2]1-[*:3]-[*:4]-[CH;+0:5](-[*:6])-[O;H0;+0:7]-1>>[*:1]-[CH2;+0:2]-[*:3]-[*:4]-[C;H0;+0:5](-[*:6])=[O;H0;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway.Aono R, Sato T, Yano A, Yoshida S, Nishitani Y, Miki K, Imanaka T, Atomi H2012 Dec23065974
Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1.Nakamura A, Fujihashi M, Aono R, Sato T, Nishiba Y, Yoshida S, Yano A, Atomi H, Imanaka T, Miki K2012 Jun 1522511789
Archaeal type III RuBisCOs function in a pathway for AMP metabolism.Sato T, Atomi H, Imanaka T2007 Feb 1617303759
Modified pathway to synthesize ribulose 1,5-bisphosphate in methanogenic archaea.Finn MW, Tabita FR2004 Oct15375115