Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.156
Description:Adenosylcobinamide kinase.
Alternative Name: AdoCbi kinase/AdoCbi-phosphate guanylyltransferase.
guanylyltransferase.
Adenosylcobinamide kinase/adenosylcobinamide-phosphate
Cath: 3.90.550.10; 3.40.50.300;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.156
BRENDA Enzyme Link: BRENDA 2.7.1.156
KEGG Enzyme Link: KEGG2.7.1.156
BioCyc Enzyme Link: BioCyc 2.7.1.156
ExPASy Enzyme Link: ExPASy2.7.1.156
EC2PDB Enzyme Link: EC2PDB 2.7.1.156
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.156
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.156
IntEnz Enzyme Link: IntEnz 2.7.1.156
MEDLINE Enzyme Link: MEDLINE 2.7.1.156
MSA:

2.7.1.156;

Phylogenetic Tree:

2.7.1.156;

Uniprot:
M-CSA:
RHEA:15769 adenosylcob(III)inamide + ATP = adenosylcob(III)inamide phosphate + ADP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:1]-[O;H0;+0:2]-[P;H0;+0:4](=[*:3])(-[*:5])-[*:6].[*:8]-[OH;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 A resolution,.Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I1998 May 269601028
Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate.O'Toole GA, Escalante-Semerena JC1995 Oct 67559521
Analysis of the adenosylcobinamide kinase/adenosylcobinamide-phosphate guanylyltransferase (CobU) enzyme of Salmonella typhimurium LT2. Identification of residue His-46 as the site of guanylylation.Thomas MG, Thompson TB, Rayment I, Escalante-Semerena JC2000 Sep 810869342
Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase (CobU) complexed with GMP: evidence for a substrate-induced transferase active site.Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I1999 Oct 510529169

RHEA:15765 adenosylcob(III)inamide + GTP = adenosylcob(III)inamide phosphate + GDP + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase from Salmonella typhimurium determined to 2.3 A resolution,.Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I1998 May 269601028
Purification and characterization of the bifunctional CobU enzyme of Salmonella typhimurium LT2. Evidence for a CobU-GMP intermediate.O'Toole GA, Escalante-Semerena JC1995 Oct 67559521
Three-dimensional structure of adenosylcobinamide kinase/adenosylcobinamide phosphate guanylyltransferase (CobU) complexed with GMP: evidence for a substrate-induced transferase active site.Thompson TB, Thomas MG, Escalante-Semerena JC, Rayment I1999 Oct 510529169