Literature summary for 4.99.1.3 extracted from

Lobo, S.; Videira, M.; Pacheco, I.; Wass, M.; Warren, M.; Teixeira, M.; Matias, P.; Romao, C.; Saraiva, L.
Desulfovibrio vulgaris CbiKP cobaltochelatase evolution of a haem binding protein orchestrated by the incorporation of two histidine residues (2017), Environ. Microbiol., 19, 106-118 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Desulfovibrio vulgaris

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with cobalt and sirohydrochlorin, to 1.7 A resolution	Desulfovibrio vulgaris

Protein Variants

Protein Variants	Comment	Organism
E184L	mutation in metal binding site, about 3fold increase in activity	Desulfovibrio vulgaris
E184L/H216L	mutation in metal binding site, strong decrease in activity	Desulfovibrio vulgaris
H154L	mutation in metal binding site. Mutant has negligible activity	Desulfovibrio vulgaris
H154L/E184L	mutation in metal binding site, negligible activity	Desulfovibrio vulgaris
H154L/E184L/H216L	mutation in metal binding site. Mutant has negligible activity	Desulfovibrio vulgaris
H154L/H216L	mutation in metal binding site. Mutant has negligible activity	Desulfovibrio vulgaris
H216L	mutation in metal binding site. Mutant has negligible activity	Desulfovibrio vulgaris

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Desulfovibrio vulgaris	-	-

Organism

Organism	UniProt	Comment	Textmining
Desulfovibrio vulgaris	Q72EC8	-	-
Desulfovibrio vulgaris DSM 644	Q72EC8	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	sequence contains a 28 amino acid N-terminal signal peptide	Desulfovibrio vulgaris

Synonyms

Synonyms	Comment	Organism
CbiKp	-	Desulfovibrio vulgaris

General Information

General Information	Comment	Organism
physiological function	residues His154 and His216 are essential for metal-chelation of sirohydrochlorin. The tetrameric form of the protein is stabilized by residues Arg54 and Glu76, which form hydrogen bonds between two subunits. His96 is responsible for the binding of two heme groups within the main central cavity of the tetramer. CbiKP binds two additional heme groups through interaction with His103	Desulfovibrio vulgaris

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Release 2023.1 (January 2023)