L-threonine kinase that catalyzes the conversion of L-threonine to L-threonine-O-3-phosphate. Involved in the de novo synthesis of adenosylcobalamin (coenzyme B12) and the assimilation of cobyric acid. Uses ATP; the activity with CTP, GTP or UTP is 6, 11, and 3% of the activity with ATP, respectively. The 1,2-propanediol (1,2-PD)-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low. This gene probably benefits from its induction via the Pdu promoter, rather than a physical interaction with the BMC. ATP + L-threonine = ADP + H(+) + O-phospho-L-threonine Cofactor biosynthesis; adenosylcobalamin biosynthesis. Polyol metabolism; 1,2-propanediol degradation. The BMC operon and BMC production is induced by growth on 1,2-PD vitamin B12 medium. Growth is impaired on 1,2-PD minimal medium supplemented with cobyric acid, but is restored on similar medium supplemented with vitamin B12, cobinamide (PubMed:18308727). A double pduW-pduX deletion grows as well as wild-type on 1,2-PD (PubMed:12700259). Catalysis proceeds by a steady-state ordered bi-bi complex mechanism in which ATP is the first substrate to bind. Belongs to the GHMP kinase family. PduX subfamily.