Enzyme

Download
EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.220
Description:D-erythronate 4-kinase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

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.

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.220
BRENDA Enzyme Link: BRENDA 2.7.1.220
KEGG Enzyme Link: KEGG2.7.1.220
BioCyc Enzyme Link: BioCyc 2.7.1.220
ExPASy Enzyme Link: ExPASy2.7.1.220
EC2PDB Enzyme Link: EC2PDB 2.7.1.220
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.220
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.220
IntEnz Enzyme Link: IntEnz 2.7.1.220
MEDLINE Enzyme Link: MEDLINE 2.7.1.220
MSA:

2.7.1.220;

Phylogenetic Tree:

2.7.1.220;

Uniprot:
M-CSA:
RHEA:52392 ATP + D-erythronate = 4-phospho-D-erythronate + ADP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Assignment of function to a domain of unknown function: DUF1537 is a new kinase family in catabolic pathways for acid sugars.Zhang X, Carter MS, Vetting MW, San Francisco B, Zhao S, Al-Obaidi NF, Solbiati JO, Thiaville JJ, de Crécy-Lagard V, Jacobson MP, Almo SC, Gerlt JA2016 Jul 1927402745