page_title: Cob(I)yrinic acid a,c-diamide adenosyltransferase
hierarchical_section_title: Cob(I)yrinic acid a,c-diamide adenosyltransferase
caption_attribution_description: English: Cartoon representation of the molecular structure of protein registered with 1g5t code. Deutsch: Grafik des Molekularstruktur von jenem Protein, das mit 1g5t code registriert ist. Plattdüütsch: Grafik, de de Molekularstruktur von dat Protein wiest, dat mit’n Kood 1g5t registreert is.
context_page_description: In molecular biology, cob(I)yrinic acid a, c-diamide adenosyltransferase EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin into one of its coenzyme forms, adenosylcobalamin. Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.
  ATP:cob(I)alamin adenosyltransferases are classed into three groups: CobA-type, EutT-type and PduO-type. Each of the three enzyme types appears to be specialised for particular AdoCbl-dependent enzymes or for the de novo synthesis of AdoCbl. PduO and EutT are distantly related, sharing short conserved motifs, while CobA is evolutionarily unrelated and is an example of convergent evolution.
  The CobA group includes the ATP:cob(I)alamin adenosyltransferases CobA, CobO, and ButR. There is a high degree of sequence identity between these proteins. CobA is responsible for attaching the adenosyl moiety from ATP to the cobalt ion of the corrin ring, necessary for the conversion of cobalamin to adenosylcobalamin.
context_section_description: In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase (also known as ATP:cob(I)alamin adenosyltransferase or ATP:corrinoid adenosyltransferase) EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin (vitamin B12) into one of its coenzyme forms, adenosylcobalamin (coenzyme B12, AdoCbl). Adenosylcobalamin is required as a cofactor for the activity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond.
  ATP:cob(I)alamin adenosyltransferases are classed into three groups: CobA-type, EutT-type  and PduO-type. Each of the three enzyme types appears to be specialised for particular AdoCbl-dependent enzymes or for the de novo synthesis of AdoCbl. PduO and EutT are distantly related, sharing short conserved motifs, while CobA is evolutionarily unrelated and is an example of convergent evolution.
  The CobA group includes the ATP:cob(I)alamin adenosyltransferases CobA (Salmonella typhimurium), CobO (Pseudomonas denitrificans), and ButR (Escherichia coli). There is a high degree of sequence identity between these proteins. CobA is responsible for attaching the adenosyl moiety from ATP to the cobalt ion of the corrin ring, necessary for the conversion of cobalamin to adenosylcobalamin. PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol degradation, while EutT produces AdoCbl for ethanolamine utilisation.
caption: the three-dimensional structure of atp:corrinoid adenosyltransferase from salmonella typhimurium. apo-atp form
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