EC number:1.1.1.137
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.1.1.137 |
|---|---|
| Description: | Ribitol-5-phosphate 2-dehydrogenase. |
| Alternative Name: |
Ribitol 5-phosphate dehydrogenase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.137 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.137 |
| KEGG Enzyme Link: | KEGG1.1.1.137 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.137 |
| ExPASy Enzyme Link: | ExPASy1.1.1.137 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.137 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.137 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.137 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.137 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.137 |
EC number:1.1.1.137
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:19925 | D-ribitol 5-phosphate + NAD(+) = D-ribulose 5-phosphate + H(+) + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Ribitol-5-phosphate dehydrogenase from Lactobacillus plantarum. | GLASER L | 1963 Apr 9 | 13948358 |
| RHEA:19921 | D-ribitol 5-phosphate + NADP(+) = D-ribulose 5-phosphate + H(+) + NADPH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Synthesis of CDP-activated ribitol for teichoic acid precursors in Streptococcus pneumoniae. | Baur S, Marles-Wright J, Buckenmaier S, Lewis RJ, Vollmer W | 2009 Feb | 19074383 |
| Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus. | Pereira MP, Brown ED | 2004 Sep 21 | 15362865 |
| Ribitol-5-phosphate dehydrogenase from Lactobacillus plantarum. | GLASER L | 1963 Apr 9 | 13948358 |
| Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae. | Zolli M, Kobric DJ, Brown ED | 2001 Apr 24 | 11305920 |
| acs1 of Haemophilus influenzae type a capsulation locus region II encodes a bifunctional ribulose 5-phosphate reductase- CDP-ribitol pyrophosphorylase. | Follens A, Veiga-da-Cunha M, Merckx R, van Schaftingen E, van Eldere J | 1999 Apr | 10094675 |
| Duplication of teichoic acid biosynthetic genes in Staphylococcus aureus leads to functionally redundant poly(ribitol phosphate) polymerases. | Pereira MP, D'Elia MA, Troczynska J, Brown ED | 2008 Aug | 18556787 |