bifunctional adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase catalyzes the ATP-dependent phosphorylation of adenosylcobinamide to form adenosylcobinamide phosphate and the addition of guanosine monophosphate to adenosylcobinamide phosphate to form adenosylcobinamide-GDP
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme transport and metabolism]; Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441690 Cd Length: 172 Bit Score: 238.87 E-value: 3.53e-81
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group ...
17-189
1.77e-74
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group of bifunctional cobalamin biosynthesis enzymes which display cobinamide kinase and cobinamide phosphate guanyltransferase activity. The crystal structure of the enzyme reveals the molecule to be a trimer with a propeller-like shape.
Pssm-ID: 426697 Cd Length: 167 Bit Score: 221.59 E-value: 1.77e-74
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a ...
17-187
1.14e-70
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a bacterial bifunctional cobalbumin biosynthesis enzyme which display adenosylcobinamide kinase and adenosylcobinamide phosphate guanyltransferase activity and is a key participant in the final stages of cobalamin biosynthesis where it is involved in nucleotide loop assembly. CobU is a homotrimer which functions both as a kinase and as a nucleotidyl transferase. It phosphorylates of adenosylcobinamide to form adenosylcobinamide phosphate (using a variety of nucleotides as the phosphate donor) and then adds GMP to adenosylcobinamide phosphate to form adenosylcobinamide-GDP, specifically using GTP.
Pssm-ID: 410861 Cd Length: 166 Bit Score: 212.01 E-value: 1.14e-70
Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase [Coenzyme transport and metabolism]; Adenosyl cobinamide kinase/adenosyl cobinamide phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441690 Cd Length: 172 Bit Score: 238.87 E-value: 3.53e-81
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group ...
17-189
1.77e-74
Cobinamide kinase / cobinamide phosphate guanyltransferase; This family is composed of a group of bifunctional cobalamin biosynthesis enzymes which display cobinamide kinase and cobinamide phosphate guanyltransferase activity. The crystal structure of the enzyme reveals the molecule to be a trimer with a propeller-like shape.
Pssm-ID: 426697 Cd Length: 167 Bit Score: 221.59 E-value: 1.77e-74
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a ...
17-187
1.14e-70
Adenosylcobinamide kinase / adenosylcobinamide phosphate guanyltransferase (CobU); CobU is a bacterial bifunctional cobalbumin biosynthesis enzyme which display adenosylcobinamide kinase and adenosylcobinamide phosphate guanyltransferase activity and is a key participant in the final stages of cobalamin biosynthesis where it is involved in nucleotide loop assembly. CobU is a homotrimer which functions both as a kinase and as a nucleotidyl transferase. It phosphorylates of adenosylcobinamide to form adenosylcobinamide phosphate (using a variety of nucleotides as the phosphate donor) and then adds GMP to adenosylcobinamide phosphate to form adenosylcobinamide-GDP, specifically using GTP.
Pssm-ID: 410861 Cd Length: 166 Bit Score: 212.01 E-value: 1.14e-70
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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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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