Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.177
Description:L-threonine kinase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.177
BRENDA Enzyme Link: BRENDA 2.7.1.177
KEGG Enzyme Link: KEGG2.7.1.177
BioCyc Enzyme Link: BioCyc 2.7.1.177
ExPASy Enzyme Link: ExPASy2.7.1.177
EC2PDB Enzyme Link: EC2PDB 2.7.1.177
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.177
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.177
IntEnz Enzyme Link: IntEnz 2.7.1.177
MEDLINE Enzyme Link: MEDLINE 2.7.1.177
MSA:

2.7.1.177;

Phylogenetic Tree:

2.7.1.177;

Uniprot:
M-CSA:
RHEA:33707 ATP + L-threonine = ADP + H(+) + O-phospho-L-threonine
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
Kinetic and functional analysis of L-threonine kinase, the PduX enzyme of Salmonella enterica.Fan C, Fromm HJ, Bobik TA2009 Jul 2419509296
The PduX enzyme of Salmonella enterica is an L-threonine kinase used for coenzyme B12 synthesis.Fan C, Bobik TA2008 Apr 2518308727