37000
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
71000
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
137000
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
sirohydrochlorin + Co2+
Brucella melitensis
involved in the formation of a octahedrally co-ordinated cobalt ion. In the oxygen-dependent cobalamin, i.e. vitamin B12, biosynthetic pathway, cobalt is inserted into a ring-contracted tetrapyrrole called hydrogenobyrinic acid a,c-diamide, HBAD, by a cobaltochelatase that is constituted by three subunits, CobN, CobS and CobT
cobalt-sirohydrochlorin + 2 H+
?
sirohydrochlorin + Co2+
involved in the formation of a octahedrally co-ordinated cobalt ion. In the oxygen-dependent cobalamin, i.e. vitamin B12, biosynthetic pathway, cobalt is inserted into a ring-contracted tetrapyrrole called hydrogenobyrinic acid a,c-diamide, HBAD, by a cobaltochelatase that is constituted by three subunits, CobN, CobS and CobT
699853
Brucella melitensis
cobalt-sirohydrochlorin + 2 H+
?
More
the molecules are arranged in a two-tiered ring structure with the six subunits in each ring organized as a trimer of dimers, subunits CobS and CobT form a chaperone-like complex. Homology modelling of subunit CobS, overview
Brucella melitensis
oligomer
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
37000
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
71000
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
137000
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
sirohydrochlorin + Co2+
Brucella melitensis
involved in the formation of a octahedrally co-ordinated cobalt ion. In the oxygen-dependent cobalamin, i.e. vitamin B12, biosynthetic pathway, cobalt is inserted into a ring-contracted tetrapyrrole called hydrogenobyrinic acid a,c-diamide, HBAD, by a cobaltochelatase that is constituted by three subunits, CobN, CobS and CobT
cobalt-sirohydrochlorin + 2 H+
?
sirohydrochlorin + Co2+
involved in the formation of a octahedrally co-ordinated cobalt ion. In the oxygen-dependent cobalamin, i.e. vitamin B12, biosynthetic pathway, cobalt is inserted into a ring-contracted tetrapyrrole called hydrogenobyrinic acid a,c-diamide, HBAD, by a cobaltochelatase that is constituted by three subunits, CobN, CobS and CobT
699853
Brucella melitensis
cobalt-sirohydrochlorin + 2 H+
?
More
the molecules are arranged in a two-tiered ring structure with the six subunits in each ring organized as a trimer of dimers, subunits CobS and CobT form a chaperone-like complex. Homology modelling of subunit CobS, overview
Brucella melitensis
oligomer
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT
Brucella melitensis
747658
Lobo
Desulfovibrio vulgaris CbiKP ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris DSM 644
Environ. Microbiol.
19
106-118
2017
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1
1
7
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1
1
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730419
Bali
Identification and characteriz ...
Paracoccus denitrificans, Paracoccus pantotrophus
Mol. Microbiol.
92
153-163
2014
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1
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2
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2
1
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1
1
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730479
Moore
Towards a cell factory for vit ...
Bacillus megaterium, Bacillus megaterium DSM 319
New Biotechnol.
31
553-561
2014
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2
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4
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2
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1
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1
-
-
716791
Romao
Evolution in a family of chela ...
Archaeoglobus fulgidus, Desulfovibrio vulgaris, Salmonella enterica
Proc. Natl. Acad. Sci. USA
108
97-102
2011
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1
1
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3
3
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699853
Lundqvist
The AAA(+) motor complex of su ...
Brucella melitensis
J. Struct. Biol.
167
227-234
2009
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1
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3
1
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1
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2
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690966
Lobo
Two distinct roles for two fun ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
Biochemistry
47
5851-5857
2008
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1
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1
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2
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2
10
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4
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2
1
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6
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24
1
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1
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2
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10
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6
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24
2
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682635
Pisarchik
Probing the structural plastic ...
Methanosarcina barkeri
Protein Eng. Des. Sel.
20
257-265
2007
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1
1
3
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2
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11
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2
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1
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11
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1
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3
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11
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1
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11
-
1
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681658
Yin
Crystal structure of the vitam ...
Archaeoglobus fulgidus
J. Struct. Funct. Genomics
7
37-50
2006
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1
1
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1
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644512
Brindley
A story of chelatase evolution ...
Methanobacter thermoautotrophicum, Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
J. Biol. Chem.
278
22388-22395
2003
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2
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5
6
6
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17
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2
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3
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12
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2
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5
6
6
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3
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12
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652468
Leech
Characterization of the cobalt ...
Bacillus megaterium, Bacillus megaterium DSM 509, Synechocystis sp.
J. Biol. Chem.
278
41900-41907
2003
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2
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3
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6
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649817
Schubert
Structural diversity in metal ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochem. Soc. Trans.
30
595-600
2002
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1
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1
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1
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4
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649818
Leech
Production of cobalamin and si ...
Bacillus megaterium
Biochem. Soc. Trans.
30
610-613
2002
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650801
Raux
Biosynthesis of cobalamin (vit ...
Bacillus megaterium, Clostridioides difficile, Clostridium acetobutylicum, no activity in Bacillus subtilis, no activity in eukaryota, Porphyromonas gingivalis, Pseudomonas aeruginosa, Rhodobacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhimurium
Cell. Mol. Life Sci.
57
1880-1893
2000
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1
1
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7
-
10
1
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1
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16
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1
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1
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7
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1
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1
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16
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644511
Schubert
Common chelatase design in the ...
Salmonella enterica subsp. enterica serovar Typhimurium
Biochemistry
38
10660-10669
1999
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1
1
1
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3
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651631
Raux
A role for Salmonella typhimur ...
Salmonella enterica subsp. enterica serovar Typhimurium
J. Bacteriol.
179
3202-3212
1997
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