2.7.13.3	ATP	-	690397, 690950, 692882, 694232, 701785, 701950, 702402, 702733, 702906, 704312, 704324, 704331, 704333, 705134, 705769, 705772, 705782, 705788, 705793, 706173, 706435, 706513, 739983, 740049, 740070, 740082, 740525, 740621, 740624, 740870, 741136, 741222, 741226, 741235, 741283	
2.7.13.3	ATP	DesK displays a compact structure at the ATP-binding pocket: the ATP lid loop is short with no secondary structural organization and becomes ordered upon ATP loading. Sequence conservation mapping onto the molecular surface, semi-flexible protein-protein docking simulations, and structure-based point mutagenesis present a specific domain-domain geometry during autophosphorylation catalysis	740689	
2.7.13.3	ATP	residue Ser492 resides on the ATP lid, near to the Mg2+ ion that coordinates the gamma-phosphate of ATP in the P4 active site	740869	
2.7.13.3	ATP	the ATP-binding domain of histidine kinases contains conserved motifs essential for autokinase activity. These include G1 and G2 boxes, which have the characteristic glycine signatures DxGxG and GxGxG, respectively	740492	
2.7.13.3	FAD	Slr1759-Var I protein contains 0.11-0.26 mM cofactor per 1 mM protein	701950	
2.7.13.3	flavin	-	682858	
2.7.13.3	flavin	flavin-containing histidine kinase functions as a photoreceptor, the flavin chromophore, upon illumination, forms a cysteinyl-flavin adduct, which is the signaling state that activates the histidine kinase	682858	
2.7.13.3	flavin	flavin-containing histidine kinase functions as a photoreceptor, the flavin chromophore, upon illumination, forms a cysteinyl-flavin adduct, which is the signaling state that activates the histidine kinase, regulates Brucella abortus virulence	682858	
2.7.13.3	FMN	bound to the LovK histidine kinase	740049	
2.7.13.3	GDP	this kinase is uniquely specific for GTP in the forward and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP specific histidine kinases, binding structure, modeling, overview	692901	
2.7.13.3	GTP	this kinase is uniquely specific for GTP in the forward and GDP in the reverse reaction. The G1 motif of BA2291 is highly modified from ATP specific histidine kinases, binding structure, modeling, overview	692901	
2.7.13.3	heme	FixL is an oxygen-binding hemoprotein, the heme domain serves as the dioxygen switch in the FixL/FixJ two-component system	441730	
2.7.13.3	heme	the Fe(II) heme-bound inactive form has kcat and Km(ATP) values of 0.0067/s and 0.078 mM, respectively, suggesting that its low activity reflects a low affinity for ATP relative to that of the Fe(III) form. The heme-free form exhibits low activity, with kcat and Km(ATP) values of 0.005/s and 0.0336 mM, respectively, suggesting that the heme iron complex is essential for high catalytic activity. The coordination and oxidation state of the sensor domain heme iron profoundly affect the enzyme's catalytic activity because they modulate its ATP binding affinity and thus change its kcat/Km(ATP) value	740070	
2.7.13.3	heme	the oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. In the absence of bound ligand, the heme domain permits kinase activity. In the presence of bound ligand, this domain turns off kinase activity	441785	
2.7.13.3	additional information	LOV domains are blue-light sensory modules which bind a flavin molecule as cofactor. Activation of LOVHK by blue-light increases the autophosphorylation activity of the HK domain	741235	
2.7.13.3	additional information	no activity with ATP, TTP, or CTP in autophosphorylation	692901	
2.7.13.3	additional information	no FAD	740049	
2.7.13.3	additional information	non-hydrolyzable ATP analogues (but not ATP or ADP) release P1 from the protein core (domains P3P4P5) and increase its mobility	740869