Enzyme

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     5. Isomerases
        5.3 Intramolecular oxidoreductases
            5.3.1 Interconverting aldoses and ketoses, and related compounds
ID:5.3.1.28
Description:D-sedoheptulose 7-phosphate isomerase.
Alternative Name: Sedoheptulose-7-phosphate isomerase.
Phosphoheptose isomerase.
Cath: 3.40.50.10490;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.3.1.28
BRENDA Enzyme Link: BRENDA 5.3.1.28
KEGG Enzyme Link: KEGG5.3.1.28
BioCyc Enzyme Link: BioCyc 5.3.1.28
ExPASy Enzyme Link: ExPASy5.3.1.28
EC2PDB Enzyme Link: EC2PDB 5.3.1.28
ExplorEnz Enzyme Link: ExplorEnz 5.3.1.28
PRIAM enzyme-specific profiles Link: PRIAM 5.3.1.28
IntEnz Enzyme Link: IntEnz 5.3.1.28
MEDLINE Enzyme Link: MEDLINE 5.3.1.28
MSA:

5.3.1.28;

Phylogenetic Tree:

5.3.1.28;

Uniprot:
M-CSA:
RHEA:27489 2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate
RULE(radius=1) [*:1]-[CH;+0:2](-[O;H0;+0:3]-[*:4])-[CH;+0:5](-[*:6])-[OH;+0:7]>>([*:1]-[CH2;+0:2]-[C;H0;+0:5](-[*:6])=[O;H0;+0:7].[*:4]-[OH;+0:3])
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site.Harmer NJ2010 Jul 1620447408
A preliminary X-ray study of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei.Kim MS, Shin DH2009 Nov 119923728
Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants.Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS2008 Feb 118056714