ID: | 4.2.3.152 |
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Description: | 2-epi-5-epi-valiolone synthase. |
Alternative Name: |
C(7)-cyclitol synthase. |
Cath: | 1.20.1090.10; 3.40.50.1970; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 4.2.3.152 |
BRENDA Enzyme Link: | BRENDA 4.2.3.152 |
KEGG Enzyme Link: | KEGG4.2.3.152 |
BioCyc Enzyme Link: | BioCyc 4.2.3.152 |
ExPASy Enzyme Link: | ExPASy4.2.3.152 |
EC2PDB Enzyme Link: | EC2PDB 4.2.3.152 |
ExplorEnz Enzyme Link: | ExplorEnz 4.2.3.152 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.2.3.152 |
IntEnz Enzyme Link: | IntEnz 4.2.3.152 |
MEDLINE Enzyme Link: | MEDLINE 4.2.3.152 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:44184 | D-sedoheptulose 7-phosphate = 2-epi-5-epi-valiolone + phosphate |
RULE(radius=1) | ([*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[O;H0;+0:6]-[CH2;+0:7]-[CH;+0:8](-[*:9])-[OH;+0:10])>>[*:1]-[C;H0;+0:2](-[*:3])(-[OH;+0:4])-[CH2;+0:7]-[C;H0;+0:8](-[*:9])=[O;H0;+0:10].[*:5]-[OH;+0:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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2-epi-5-epi-Valiolone synthase activity is essential for maintaining phycobilisome composition in the cyanobacterium Anabaena variabilis ATCC 29413 when grown in the presence of a carbon source. | Spence E, Bryan SJ, Lisfi M, Cullum J, Dunlap WC, Shick JM, Mullineaux CW, Long PF | 2013 Sep | 23857509 |
ValC, a new type of C7-Cyclitol kinase involved in the biosynthesis of the antifungal agent validamycin A. | Minagawa K, Zhang Y, Ito T, Bai L, Deng Z, Mahmud T | 2007 Apr 16 | 17335096 |
Synthesis of 5-epi-[6-(2)H(2)]valiolone and stereospecifically monodeuterated 5-epi-valiolones: exploring the steric course of 5-epi-valiolone dehydratase in validamycin A biosynthesis. | Mahmud T, Xu J, Choi YU | 2001 Jul 27 | 11463258 |