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Information on EC 4.99.1.3 - sirohydrochlorin cobaltochelatase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29537

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IUBMB Comments
This enzyme, which forms part of the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway, is an ATP-independent type II chelatase. Two distinct forms are known - a primordial form named CbiX, which is most common in archaea, and a strictly bacterial form named CbiK. See EC 6.6.1.2, cobaltochelatase, for the cobaltochelatase that participates in the aerobic cobalamin biosynthesis pathway.
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Archaeoglobus fulgidus
UNIPROT: O29537
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Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
cobalt chelatase, cbixl, cbixs, sirohydrochlorin-ferrochelatase, sirohydrochlorin cobaltochelatase, anaerobic cobalt chelatase, archaeal cobaltochelatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sirohydrochlorin cobalt-lyase
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sirohydrochlorin cobaltochelatase
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anaerobic cobalt chelatase
-
-
-
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CbiK
-
-
-
-
CbiXS
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-
-
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cobaltochelatase
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
cobalt-sirohydrochlorin cobalt-lyase (sirohydrochlorin-forming)
This enzyme, which forms part of the anaerobic (early cobalt insertion) cobalamin biosynthesis pathway, is an ATP-independent type II chelatase. Two distinct forms are known - a primordial form named CbiX, which is most common in archaea, and a strictly bacterial form named CbiK. See EC 6.6.1.2, cobaltochelatase, for the cobaltochelatase that participates in the aerobic cobalamin biosynthesis pathway.
CAS REGISTRY NUMBER
COMMENTARY hide
81295-49-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
show the reaction diagram
-
-
-
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
non His-tagged protein
0.017
His-tagged protein
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using the sitting drop vapor diffusion technique in 96-well plates, in two different crystal forms consisting of a central mixed b-sheet flanked by four alpha helices
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by using a metal chelating affinity column charged with Ni2+ or a chelating Sepharose-column charged with Co2+
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli as non His-tagged protein, as His-tagged protein fusion protein and as selenomethionine-substituted protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yin, J.; Xu, L.X.; Cherney, M.M.; Raux-Deery, E.; Bindley, A.A.; Savchenko, A.; Walker, J.R.; Cuff, M.E.; Warren, M.J.; James, M.N.
Crystal structure of the vitamin B12 biosynthetic cobaltochelatase, CbiXS, from Archaeoglobus fulgidus
J. Struct. Funct. Genomics
7
37-50
2006
Archaeoglobus fulgidus (O29537)
Manually annotated by BRENDA team
Romao, C.V.; Ladakis, D.; Lobo, S.A.; Carrondo, M.A.; Brindley, A.A.; Deery, E.; Matias, P.M.; Pickersgill, R.W.; Saraiva, L.M.; Warren, M.J.
Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization
Proc. Natl. Acad. Sci. USA
108
97-102
2011
Archaeoglobus fulgidus, Desulfovibrio vulgaris (Q72EC8), Salmonella enterica
Manually annotated by BRENDA team