EC number:2.7.1.101

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.101
Description:Tagatose kinase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.101
BRENDA Enzyme Link: BRENDA 2.7.1.101
KEGG Enzyme Link: KEGG2.7.1.101
BioCyc Enzyme Link: BioCyc 2.7.1.101
ExPASy Enzyme Link: ExPASy2.7.1.101
EC2PDB Enzyme Link: EC2PDB 2.7.1.101
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.101
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.101
IntEnz Enzyme Link: IntEnz 2.7.1.101
MEDLINE Enzyme Link: MEDLINE 2.7.1.101

EC number:2.7.1.101

MSA:

2.7.1.101;
Phylogenetic Tree:

2.7.1.101;
Uniprot:
M-CSA:
RHEA:15513 ATP + keto-D-tagatose = ADP + H(+) + keto-D-tagatose 6-phosphate
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
A novel enzyme, tagatose kinase, from Mycobacterium butyricum.Szumiøo T1981 Aug 136269638
ATP-binding Cassette (ABC) Transport System Solute-binding Protein-guided Identification of Novel d-Altritol and Galactitol Catabolic Pathways in Agrobacterium tumefaciens C58.Wichelecki DJ, Vetting MW, Chou L, Al-Obaidi N, Bouvier JT, Almo SC, Gerlt JA2015 Nov 2726472925