Cob(I)yrinic acid a,c-diamide adenosyltransferase

ATP:corrinoid adenosyltransferase
the three-dimensional structure of atp:corrinoid adenosyltransferase from salmonella typhimurium. apo-atp form
Identifiers
Symbol	CobA_CobO_BtuR
Pfam	PF02572
Pfam clan	CL0023
InterPro	IPR003724
SCOP	1g64
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

Cobalamin adenosyltransferase (PduO/EutT)
crystal structure of conserved protein 0546 from thermoplasma acidophilum
Identifiers
Symbol	Cob_adeno_trans
Pfam	PF01923
InterPro	IPR002779
SCOP	1nog
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

In molecular biology, cob(I)yrinic acid a,c-diamide adenosyltransferase (also known as ATP:cob(I)alamin or ATP:corrinoid adenosyltransferase) EC 2.5.1.17 is an enzyme which catalyses the conversion of cobalamin (vitamin B12) into its coenzyme form, adenosylcobalamin (coenzyme B12).^[1] Adenosylcobalamin (AdoCbl) is required for the ativity of certain enzymes. AdoCbl contains an adenosyl moiety liganded to the cobalt ion of cobalamin via a covalent Co-C bond, and its synthesis is unique to certain prokaryotes. ATP:cob(I)alamin adenosyltransferases are classed into three groups: CobA-type,^[2] EutT-type ^[3] and PduO-type.^[4] 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.^[5] CobA is responsible for attaching the adenosyl moiety from ATP to the cobalt ion of the corrin ring, necessary for the convertion of cobalamin to adenosylcobalamin.^[2][1] PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol degradation,^[6] while EutT produces AdoCbl for ethanolamine utilisation.^[7]

References

1. ^ ^{a b} Sheppard DE, Penrod JT, Bobik T, Kofoid E, Roth JR (November 2004). "Evidence that a B12-adenosyl transferase is encoded within the ethanolamine operon of Salmonella enterica". J. Bacteriol. 186 (22): 7635–44. doi:10.1128/JB.186.22.7635-7644.2004. PMC 524904. PMID 15516577. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=524904. 
2. ^ ^{a b} Buan NR, Rehfeld K, Escalante-Semerena JC (May 2006). "Studies of the CobA-type ATP:Co(I)rrinoid adenosyltransferase enzyme of Methanosarcina mazei strain Go1". J. Bacteriol. 188 (10): 3543–50. doi:10.1128/JB.188.10.3543-3550.2006. PMC 1482872. PMID 16672609. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1482872. 
3. ^ Buan NR, Suh SJ, Escalante-Semerena JC (September 2004). "The eutT gene of Salmonella enterica Encodes an oxygen-labile, metal-containing ATP:corrinoid adenosyltransferase enzyme". J. Bacteriol. 186 (17): 5708–14. doi:10.1128/JB.186.17.5708-5714.2004. PMC 516830. PMID 15317775. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=516830. 
4. ^ Johnson CL, Pechonick E, Park SD, Havemann GD, Leal NA, Bobik TA (March 2001). "Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene". J. Bacteriol. 183 (5): 1577–84. doi:10.1128/JB.183.5.1577-1584.2001. PMC 95042. PMID 11160088. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=95042. 
5. ^ Suh SJ, Escalante-Semerena JC (July 1993). "Cloning, sequencing and overexpression of cobA which encodes ATP:corrinoid adenosyltransferase in Salmonella typhimurium". Gene 129 (1): 93–7. doi:10.1016/0378-1119(93)90701-4. PMID 7916712. 
6. ^ Luers F, Seyfried M, Daniel R, Gottschalk G (September 1997). "Glycerol conversion to 1,3-propanediol by Clostridium pasteurianum: cloning and expression of the gene encoding 1,3-propanediol dehydrogenase". FEMS Microbiol. Lett. 154 (2): 337–45. PMID 9311132. 
7. ^ Buan NR, Escalante-Semerena JC (June 2006). "Purification and initial biochemical characterization of ATP:Cob(I)alamin adenosyltransferase (EutT) enzyme of Salmonella enterica". J. Biol. Chem. 281 (25): 16971–7. doi:10.1074/jbc.M603069200. PMID 16636051. 

This article includes text from the public domain Pfam and InterPro IPR003724

This article includes text from the public domain Pfam and InterPro IPR002779