selD

Summary: Mg2+ is an assigned SelD cofactor and is coordinated at predicted catalytic sites.

Reason: The reviewed UniProt/HAMAP record states that one Mg2+ is bound per monomer and annotates three Mg2+-contacting positions.

Summary: This term precisely represents the selenophosphate-forming SelD reaction.

Reason: Reviewed UniProt, HAMAP, NCBIfam, TIGRFAM, and the PANTHER family all support selenide, water dikinase identity. The PANTHER SF0 display name says "inactive ...-like," but that subfamily also contains canonical bacterial selD proteins and conflicts with the conserved catalytic cysteine and ATP/Mg2+ sites in P59392; it is not credible negative evidence for this target.

Summary: ATP is a substrate in selenophosphate synthesis and has multiple predicted contacts.

Reason: The reviewed reaction consumes ATP and forms AMP, and UniProt maps several ATP-binding residues across the dimer interface.

Summary: Cytoplasm is the appropriate location for this soluble bacterial enzyme.

Reason: TreeGrafter assigns cytoplasm, and the reviewed sequence lacks signal peptide and transmembrane features.

Summary: SelD supplies the activated selenium donor required for bacterial Sec-tRNA synthesis.

Reason: Selenophosphate made from selenide and ATP is the substrate used by SelA. This pathway assignment covers donor synthesis only and does not assign SelD any function of the downstream selenoprotein.