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41  structures 2347  species 1  interaction 2946  sequences 7  architectures

Family: Cob_adeno_trans (PF01923)

Summary: Cobalamin adenosyltransferase

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This is the Wikipedia entry entitled "Cob(I)yrinic acid a,c-diamide adenosyltransferase". More...

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

ATP:corrinoid adenosyltransferase
PDB 1g5t EBI.jpg
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
SUPERFAMILY 1g64
Cobalamin adenosyltransferase (PduO/EutT)
PDB 1nog EBI.jpg
crystal structure of conserved protein 0546 from thermoplasma acidophilum
Identifiers
Symbol Cob_adeno_trans
Pfam PF01923
InterPro IPR002779
SCOP 1nog
SUPERFAMILY 1nog

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 activity 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 conversion of cobalamin to adenosylcobalamin.[1][2] PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol degradation,[6] while EutT produces AdoCbl for ethanolamine utilisation.[7]

References[edit]

  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. 
  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. 
  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. 
  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. 
  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 incorporates text from the public domain Pfam and InterPro IPR003724

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

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Cobalamin adenosyltransferase Provide feedback

Cobalamin adenosyltransferase This family contains the gene products of PduO and EutT which are both cobalamin adenosyltransferases. PduO is a protein with ATP:cob(I)alamin adenosyltransferase activity. The main role of this protein is the conversion of inactive cobalamins to AdoCbl for 1,2-propanediol degradation [1].The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12 [2].

Literature references

  1. Johnson CL, Pechonick E, Park SD, Havemann GD, Leal NA, Bobik TA; , J Bacteriol 2001;183:1577-1584.: Functional genomic, biochemical, and genetic characterization of the Salmonella pduO gene, an ATP:cob(I)alamin adenosyltransferase gene. PUBMED:11160088 EPMC:11160088

  2. Kofoid E, Rappleye C, Stojiljkovic I, Roth J; , J Bacteriol 1999;181:5317-5329.: The 17-gene ethanolamine (eut) operon of Salmonella typhimurium encodes five homologues of carboxysome shell proteins. PUBMED:10464203 EPMC:10464203


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002779

ATP:cob(I)alamin (or ATP:corrinoid) adenosyltransferases (EC), catalyse the conversion of cobalamin (vitamin B12) into its coenzyme form, adenosylcobalamin (coenzyme B12) [PUBMED:15516577]. 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 [PUBMED:16672609], EutT-type [PUBMED:15317775] and PduO-type [PUBMED:11160088]. Each of the three enzyme types appears to be specialised for particular AdoCbl-dependent enzymes or for the de novo synthesis AdoCbl. PduO and EutT are distantly related, sharing short conserved motifs, while CobA is evolutionarily unrelated and is an example of convergent evolution.

This entry represents EutT- and PduO-type ATP:cob(I)alamin adenosyltransferases. PduO functions to convert cobalamin to AdoCbl for 1,2-propanediol degradation [PUBMED:9311132], while EutT produces AdoCbl for ethanolamine utilisation [PUBMED:16636051].

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(180)
Full
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Representative proteomes NCBI
(2068)
Meta
(1103)
RP15
(266)
RP35
(472)
RP55
(598)
RP75
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  Seed
(180)
Full
(2946)
Representative proteomes NCBI
(2068)
Meta
(1103)
RP15
(266)
RP35
(472)
RP55
(598)
RP75
(715)
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Seed source: Enright A
Previous IDs: DUF80;
Type: Domain
Author: Moxon SJ
Number in seed: 180
Number in full: 2946
Average length of the domain: 162.40 aa
Average identity of full alignment: 34 %
Average coverage of the sequence by the domain: 75.35 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.3 21.4
Noise cut-off 21.1 21.1
Model length: 163
Family (HMM) version: 13
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Cob_adeno_trans

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Cob_adeno_trans domain has been found. There are 41 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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