ATP:cob(I)alamin adenosyltransferase catalyzes the final step in the conversion of cyanocobalamin (vitamin B12) to adenosylcobalamin, catalyzing the transfer of the adenosyl moiety from ATP to cobalamin
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
1-176
2.15e-91
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
:
Pssm-ID: 441699 Cd Length: 180 Bit Score: 263.91 E-value: 2.15e-91
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
1-176
2.15e-91
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441699 Cd Length: 180 Bit Score: 263.91 E-value: 2.15e-91
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene ...
4-165
2.86e-78
Cobalamin adenosyltransferase; 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.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.
Pssm-ID: 460384 Cd Length: 163 Bit Score: 230.08 E-value: 2.86e-78
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin ...
4-177
1.08e-67
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213544 Cd Length: 171 Bit Score: 203.72 E-value: 1.08e-67
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin ...
1-176
2.15e-91
Cob(II)alamin adenosyltransferase [Coenzyme transport and metabolism]; Cob(II)alamin adenosyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441699 Cd Length: 180 Bit Score: 263.91 E-value: 2.15e-91
Cobalamin adenosyltransferase; Cobalamin adenosyltransferase This family contains the gene ...
4-165
2.86e-78
Cobalamin adenosyltransferase; 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.The EutT enzyme appears to be an adenosyl transferase, converting CNB12 to AdoB12.
Pssm-ID: 460384 Cd Length: 163 Bit Score: 230.08 E-value: 2.86e-78
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin ...
4-177
1.08e-67
ATP:cob(I)alamin adenosyltransferase; This model represents as ATP:cob(I)alamin adenosyltransferase family corresponding to the N-terminal half of Salmonella PduO, a 1,2-propanediol utilization protein that probably is bifunctional. PduO represents one of at least three families of ATP:corrinoid adenosyltransferase: others are CobA (which partially complements PduO) and EutT. It was not clear originally whether ATP:cob(I)alamin adenosyltransferase activity resides in the N-terminal region of PduO, modeled here, but this has now become clear from the characterization of MeaD from Methylobacterium extorquens. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 213544 Cd Length: 171 Bit Score: 203.72 E-value: 1.08e-67
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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