4.99.1.3: sirohydrochlorin cobaltochelatase
This is an abbreviated version!
For detailed information about sirohydrochlorin cobaltochelatase, go to the full flat file.
Word Map on EC 4.99.1.3
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4.99.1.3
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protoporphyrin
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megaterium
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typhimurium
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chlorophyll
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precorrin-2
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uroporphyrinogen
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tetrapyrrole
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primordial
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sirohaem
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dehydrogenation
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histidine-rich
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epr
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atp-independent
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ferrochelation
- 4.99.1.3
- protoporphyrin
- megaterium
- typhimurium
- chlorophyll
- precorrin-2
- uroporphyrinogen
- tetrapyrrole
-
primordial
-
sirohaem
-
dehydrogenation
-
histidine-rich
- epr
-
atp-independent
-
ferrochelation
Reaction
Synonyms
anaerobic cobalt chelatase, archaeal cobaltochelatase, CbiK, CbiKc, CbiKp, CbiX, CbiX0H, CbiXL, CbiXOH, CbiXS, cobalamin cobalt chelatase, cobalt chelatase, cobaltochelatase, More, sirohydrochlorin cobalt chelatase, sirohydrochlorin cobalt-lyase, sirohydrochlorin cobaltochelatase, sirohydrochlorin-ferrochelatase
ECTree
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General Information
General Information on EC 4.99.1.3 - sirohydrochlorin cobaltochelatase
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malfunction
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a cbiX-deficient mutant is unable to respire anaerobically on nitrate
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
physiological function
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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
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