EC Number | Cloned (Comment) | Organism |
---|---|---|
4.99.1.3 | genes cobN, cobS and cobT, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3) | Brucella melitensis |
6.6.1.2 | subunits separately overexpressed in Escherichia coli BL21star (DE3)pLysS | Brucella melitensis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
4.99.1.3 | 37000 | - |
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT | Brucella melitensis |
4.99.1.3 | 71000 | - |
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT | Brucella melitensis |
4.99.1.3 | 137000 | - |
x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT | Brucella melitensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.99.1.3 | 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+ | - |
? | |
6.6.1.2 | ATP + hydrogenobyrinic acid a,c-diamide + Co2+ | Brucella melitensis | - |
ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+ | - |
ir |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.99.1.3 | Brucella melitensis | - |
genes cobN, cobS and cobT encoding the tree subunits | - |
6.6.1.2 | Brucella melitensis | - |
cobaltochelatase consists of three subunits, CobN, CobS and CobT, while subunits CobS and CobT form a chaperone-like complex, characteristic for the AAA+ class of proteins | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.99.1.3 | 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 | Brucella melitensis | cobalt-sirohydrochlorin + 2 H+ | - |
? | |
6.6.1.2 | ATP + hydrogenobyrinic acid a,c-diamide + Co2+ | - |
Brucella melitensis | ADP + phosphate + cob(II)yrinic acid a,c-diamide + H+ | - |
ir |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.99.1.3 | 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 |
4.99.1.3 | oligomer | x * 137000, subunit CobN, + x * 37000, subunit CobS, + x * 71000, subunit CobT | Brucella melitensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.99.1.3 | cobaltochelatase | - |
Brucella melitensis |
4.99.1.3 | More | the enzyme belongs to the AAA+ superfamily of proteins | Brucella melitensis |
6.6.1.2 | cobaltochelatase | - |
Brucella melitensis |