4.99.1.4	precorrin-2 + Co2+	SirB, much lower specific activity than with sirohydrochlorin	Priestia megaterium	cobalt-precorrin-2 + 2 H+	-	?	368586	
4.99.1.4	precorrin-2 + Co2+	SirB, much lower specific activity than with sirohydrochlorin	Priestia megaterium DSM 509	cobalt-precorrin-2 + 2 H+	-	?	368586	
4.99.1.4	sirohydrochlorin + Co2+	pH 8.0	Arabidopsis thaliana	cobalt-sirohydrochlorin + H+	-	?	368581	
4.99.1.4	sirohydrochlorin + Co2+	-	Salmonella enterica	cobalt-sirohydrochlorin + 2 H+	-	?	368585	
4.99.1.4	sirohydrochlorin + Co2+	-	Saccharomyces cerevisiae	cobalt-sirohydrochlorin + 2 H+	-	?	368585	
4.99.1.4	sirohydrochlorin + Co2+	SirB, lower specificity for cobalt than for iron	Priestia megaterium	cobalt-sirohydrochlorin + 2 H+	-	?	368585	
4.99.1.4	sirohydrochlorin + Co2+	SirB, lower specificity for cobalt than for iron	Priestia megaterium DSM 509	cobalt-sirohydrochlorin + 2 H+	-	?	368585	
4.99.1.4	sirohydrochlorin + Fe2+	-	Saccharomyces cerevisiae	siroheme + H+	-	?	359195	
4.99.1.4	sirohydrochlorin + Fe2+	-	Arabidopsis thaliana	siroheme + H+	-	?	359195	
4.99.1.4	sirohydrochlorin + Fe2+	-	Priestia megaterium	siroheme + H+	-	?	359195	
4.99.1.4	sirohydrochlorin + Fe2+	-	Paracoccus pantotrophus	siroheme + H+	-	?	359195	
4.99.1.4	sirohydrochlorin + Fe2+	pH 8.0	Arabidopsis thaliana	siroheme + H+	-	?	359195	
4.99.1.4	sirohydrochlorin + Fe2+	CysG structure, the multifunctional siroheme synthase CysG synthesizes siroheme from uroporphyrinogen III, CysG contains two structurally independent modules: a bismethyltransferase and a dual-function dehydrogenase-chelatase	Salmonella enterica	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	Met8p catalyzes ferrochelation during the synthesis of siroheme, both ferrochelation and NAD+-dependent dehydrogenation of preccorin-2 to produce sirohydrochlorin take place in a single bifunctional active site, Asp-141 participates in both catalytic reactions, which are not linked mechanistically, mechanism	Saccharomyces cerevisiae	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	Met8p structure, bifunctional Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme, both catalytic activities share a single active site, Asp-141 functions as a general base and plays an essential role in both dehydrogenase and chelatase processes	Saccharomyces cerevisiae	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	SirB, monofunctional ferrochelatase, higher specificity for iron over cobalt	Priestia megaterium	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	CysG, siroheme biosynthesis	Salmonella enterica	siroheme + 2 H+	sulfur metabolism depends on siroheme	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	Met8p catalyzes ferrochelation during the biosynthesis of siroheme	Saccharomyces cerevisiae	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme	Saccharomyces cerevisiae	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	SirB is responsible for the final step in siroheme synthesis	Priestia megaterium	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	SirB, monofunctional ferrochelatase, higher specificity for iron over cobalt	Priestia megaterium DSM 509	siroheme + 2 H+	-	?	368584	
4.99.1.4	sirohydrochlorin + Fe2+	SirB is responsible for the final step in siroheme synthesis	Priestia megaterium DSM 509	siroheme + 2 H+	-	?	368584